DB code: D00498

CATH domain 1.10.760.10 : Cytochrome Bc1 Complex; Chain D, domain 2 Catalytic domain
2.140.10.20 : Methanol Dehydrogenase; Chain A Catalytic domain
E.C. 1.7.2.1 1.7.99.1 1.9.3.1
CSA
M-CSA
MACiE

CATH domain Related DB codes (homologues)
2.140.10.20 : Methanol Dehydrogenase; Chain A D00055
1.10.760.10 : Cytochrome Bc1 Complex; Chain D, domain 2 D00055 M00179

Uniprot Enzyme Name
UniprotKB Protein name Synonyms
P72181 Nitrite reductase
EC 1.7.2.1
Cytochrome cd1
Cytochrome oxidase
Hydroxylamine reductase
EC 1.7.99.1

KEGG enzyme name
nitrite reductase (NO-forming)
(EC 1.7.2.1 )
cd-cytochrome nitrite reductase
(EC 1.7.2.1 )
[nitrite reductase (cytochrome)] [misleading, see comments.]
(EC 1.7.2.1 )
cytochrome c-551:O2, NO2+ oxidoreductase
(EC 1.7.2.1 )
cytochrome cd
(EC 1.7.2.1 )
cytochrome cd1
(EC 1.7.2.1 )
hydroxylamine (acceptor) reductase
(EC 1.7.2.1 )
methyl viologen-nitrite reductase
(EC 1.7.2.1 )
nitrite reductase (cytochrome
(EC 1.7.2.1 )
NO-forming)
(EC 1.7.2.1 )
hydroxylamine reductase
(EC 1.7.99.1 )
hydroxylamine (acceptor) reductase
(EC 1.7.99.1 )
ammonia:(acceptor) oxidoreductase
(EC 1.7.99.1 )
cytochrome-c oxidase
(EC 1.9.3.1 )
cytochrome oxidase
(EC 1.9.3.1 )
cytochrome a3
(EC 1.9.3.1 )
cytochrome aa3
(EC 1.9.3.1 )
Warburg's respiratory enzyme
(EC 1.9.3.1 )
indophenol oxidase
(EC 1.9.3.1 )
indophenolase
(EC 1.9.3.1 )
complex IV (mitochondrial electron transport)
(EC 1.9.3.1 )
ferrocytochrome c oxidase
(EC 1.9.3.1 )
NADH cytochrome c oxidase
(EC 1.9.3.1 )

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P72181 NIRS_PARPN NH(3) + H(2)O + acceptor = hydroxylamine + reduced acceptor. Nitric oxide + H(2)O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H(+). Homodimer. Periplasm. Binds 2 heme groups per subunit.

KEGG Pathways
Map code Pathways E.C.
MAP00910 Nitrogen metabolism 1.7.2.1 1.7.99.1
MAP00190 Oxidative phosphorylation 1.9.3.1

Compound table
Cofactors Substrates Products Intermediates
KEGG-id C00032 C00032 C00088 C00126 C00080 C00014 C00028 C00007 C00533 C00001 C00125 C00192 C00030
E.C. 1.7.2.1
1.7.99.1
1.9.3.1
1.7.2.1
1.7.99.1
1.9.3.1
1.7.2.1
1.7.2.1
1.9.3.1
1.7.2.1
1.9.3.1
1.7.99.1
1.7.99.1
1.9.3.1
1.7.2.1
1.7.2.1
1.7.99.1
1.9.3.1
1.7.2.1
1.9.3.1
1.7.99.1
1.7.99.1
Compound c heme d1 heme Nitrite Ferrocytochrome c H+ Ammonia Acceptor O2 Nitric oxide H2O Ferricytochrome c Hydroxylamine Reduced acceptor
Type aromatic ring (with nitrogen atoms),carboxyl group,heavy metal aromatic ring (with nitrogen atoms),carboxyl group,heavy metal others amide group,amine group,aromatic ring (with nitrogen atoms),carboxyl group,heavy metal,sulfide group others amine group,organic ion others others others H2O amide group,amine group,aromatic ring (with nitrogen atoms),carboxyl group,heavy metal,sulfide group amine group others
ChEBI 17627
26355
17627
26355
25567
15378
16134
15379
26689
27140
16480
15377
15429
PubChem 24529
1038
222
977
145068
22247451
962
787
1aofA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:HEM Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1aofB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:HEM Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1aomB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:HEM Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1aoqA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:HEM Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1aoqB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:HEM Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1dy7B01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:HEC Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1e2rA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:HEC Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1e2rB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:HEC Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1gq1A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:HEC Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1gq1B01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:HEC Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1h9xA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:HEC Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1h9xB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:HEC Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1h9yA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:HEC Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1h9yB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:HEC Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1hcmA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:HEC Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1hcmB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:HEC Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1hj3A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:HEC Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1hj3B01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:HEC Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1hj4A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:HEC Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1hj4B01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:HEC Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1hj5A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:HEC Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1hj5B01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:HEC Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1qksA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:HEC Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1qksB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:HEC Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1aofA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Bound:DHE Analogue:SO2 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1aofB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Bound:DHE Analogue:SO2 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1aomA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Bound:DHE Bound:2NO Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1aomB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Bound:DHE Unbound Unbound Unbound Unbound Unbound Bound:_NO Unbound Unbound Unbound
1aoqA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Bound:DHE Bound:2NO Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1aoqB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Bound:DHE Unbound Unbound Unbound Unbound Unbound Bound:_NO Unbound Unbound Unbound
1dy7A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Bound:DHE Unbound Unbound Unbound Unbound Unbound Analogue:CMO Unbound Unbound Unbound
1dy7B02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Bound:DHE Unbound Unbound Unbound Unbound Unbound Analogue:CMO Unbound Unbound Unbound
1e2rA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Bound:DHE Unbound Unbound Unbound Unbound Unbound Analogue:CYN Unbound Unbound Unbound
1e2rB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Bound:DHE Unbound Unbound Unbound Unbound Unbound Analogue:CYN Unbound Unbound Unbound
1gq1A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Bound:DHE Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1gq1B02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Bound:DHE Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1h9xA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Bound:DHE Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1h9xB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Bound:DHE Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1h9yA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Bound:DHE Unbound Unbound Unbound Unbound Unbound Analogue:CYN Unbound Unbound Unbound
1h9yB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Bound:DHE Unbound Unbound Unbound Unbound Unbound Analogue:CYN Unbound Unbound Unbound
1hcmA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Bound:DHE Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1hcmB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Bound:DHE Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1hj3A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Bound:DHE Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1hj3B02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Bound:DHE Unbound Unbound Unbound Unbound Bound:OXY Unbound Unbound Unbound Unbound
1hj4A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Bound:DHE Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1hj4B02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Bound:DHE Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1hj5A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Bound:DHE Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1hj5B02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Bound:DHE Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1qksA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Bound:DHE Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1qksB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Bound:DHE Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1aofA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ;HIS 69;MET 106(Heme c axial binding);CYS 65;CYS 68(Heme c covalent); truncated 1-35
1aofB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ;HIS 69;MET 106(Heme c axial binding);CYS 65;CYS 68(Heme c covalent); truncated 1-35
1aomB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 17;HIS 69; (Heme c axial binding);CYS 65;CYS 68(Heme c covalent);TYR 25(Heme d1)
1aoqA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 17;HIS 69; (Heme c axial binding);CYS 65;CYS 68(Heme c covalent);TYR 25(Heme d1)
1aoqB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 17;HIS 69; (Heme c axial binding);CYS 65;CYS 68(Heme c covalent);TYR 25(Heme d1)
1dy7B01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ;HIS 69;MET 106(Heme c axial binding);CYS 65;CYS 68(Heme c covalent); truncated 1-31
1e2rA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ;HIS 69;MET 106(Heme c axial binding);CYS 65;CYS 68(Heme c covalent); truncated 1-35
1e2rB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ;HIS 69;MET 106(Heme c axial binding);CYS 65;CYS 68(Heme c covalent); truncated 1-35
1gq1A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 17;HIS 69; (Heme c axial binding);CYS 65;CYS 68(Heme c covalent); mutant Y25S
1gq1B01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 17;HIS 69; (Heme c axial binding);CYS 65;CYS 68(Heme c covalent); mutant Y25S
1h9xA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ;HIS 69;MET 106(Heme c axial binding);CYS 65;CYS 68(Heme c covalent); truncated 1-41
1h9xB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ;HIS 69;MET 106(Heme c axial binding);CYS 65;CYS 68(Heme c covalent); truncated 1-41
1h9yA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ;HIS 69;MET 106(Heme c axial binding);CYS 65;CYS 68(Heme c covalent); truncated 1-47
1h9yB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ;HIS 69;MET 106(Heme c axial binding);CYS 65;CYS 68(Heme c covalent); truncated 1-47
1hcmA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ;HIS 69;MET 106(Heme c axial binding);CYS 65;CYS 68(Heme c covalent); truncated 1-41
1hcmB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ;HIS 69;MET 106(Heme c axial binding);CYS 65;CYS 68(Heme c covalent); truncated 1-41
1hj3A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 17;HIS 69; (Heme c axial binding);CYS 65;CYS 68(Heme c covalent);TYR 25(Heme d1)
1hj3B01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ;HIS 69; (Heme c axial binding);CYS 65;CYS 68(Heme c covalent); truncated 1-25
1hj4A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 17;HIS 69; (Heme c axial binding);CYS 65;CYS 68(Heme c covalent);TYR 25(Heme d1)
1hj4B01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ;HIS 69; (Heme c axial binding);CYS 65;CYS 68(Heme c covalent); truncated 1-25
1hj5A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 17;HIS 69; (Heme c axial binding);CYS 65;CYS 68(Heme c covalent);TYR 25(Heme d1)
1hj5B01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 17;HIS 69; (Heme c axial binding);CYS 65;CYS 68(Heme c covalent);TYR 25(Heme d1)
1qksA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 17;HIS 69; (Heme c axial binding);CYS 65;CYS 68(Heme c covalent);TYR 25(Heme d1)
1qksB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 17;HIS 69; (Heme c axial binding);CYS 65;CYS 68(Heme c covalent);TYR 25(Heme d1)
1aofA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 345;HIS 388 HIS 200(Heme d1 proximal binding)
1aofB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 345;HIS 388 HIS 200(Heme d1 proximal binding)
1aomA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 345;HIS 388 HIS 200(Heme d1 proximal binding)
1aomB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 345;HIS 388 HIS 200(Heme d1 proximal binding)
1aoqA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 345;HIS 388 HIS 200(Heme d1 proximal binding)
1aoqB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 345;HIS 388 HIS 200(Heme d1 proximal binding)
1dy7A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 345;HIS 388 HIS 200(Heme d1 proximal binding)
1dy7B02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 345;HIS 388 HIS 200(Heme d1 proximal binding)
1e2rA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 345;HIS 388 HIS 200(Heme d1 proximal binding)
1e2rB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 345;HIS 388 HIS 200(Heme d1 proximal binding)
1gq1A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 345;HIS 388 HIS 200(Heme d1 proximal binding)
1gq1B02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 345;HIS 388 HIS 200(Heme d1 proximal binding)
1h9xA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 345;HIS 388 HIS 200(Heme d1 proximal binding)
1h9xB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 345;HIS 388 HIS 200(Heme d1 proximal binding)
1h9yA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 345;HIS 388 HIS 200(Heme d1 proximal binding)
1h9yB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 345;HIS 388 HIS 200(Heme d1 proximal binding)
1hcmA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 345;HIS 388 HIS 200(Heme d1 proximal binding)
1hcmB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 345;HIS 388 HIS 200(Heme d1 proximal binding)
1hj3A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 345;HIS 388 HIS 200(Heme d1 proximal binding)
1hj3B02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 345;HIS 388 HIS 200(Heme d1 proximal binding)
1hj4A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 345;HIS 388 HIS 200(Heme d1 proximal binding)
1hj4B02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 345;HIS 388 HIS 200(Heme d1 proximal binding)
1hj5A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 345;HIS 388 HIS 200(Heme d1 proximal binding)
1hj5B02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 345;HIS 388 HIS 200(Heme d1 proximal binding)
1qksA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 345;HIS 388 HIS 200(Heme d1 proximal binding)
1qksB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 345;HIS 388 HIS 200(Heme d1 proximal binding)

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[1]
Fig.7, p.373-374
[3]
p.442-446
[4]
[5]
Fig.3, p.236-239
[6]
p.4034-4035
[8]
Fig.6, p.10972-10974
[11]
Fig.4
[12]
p.1007-1008
[13]
[14]
p.13075-13076

References
[1]
Resource
Comments
Medline ID
PubMed ID 7736589
Journal Cell
Year 1995
Volume 81
Pages 369-77
Authors Fulop V, Moir JW, Ferguson SJ, Hajdu J
Title The anatomy of a bifunctional enzyme: structural basis for reduction of oxygen to water and synthesis of nitric oxide by cytochrome cd1.
Related PDB 1qks
Related UniProtKB
[2]
Resource
Comments
Medline ID
PubMed ID 9405061
Journal Biochemistry
Year 1997
Volume 36
Pages 16267-76
Authors Cheesman MR, Ferguson SJ, Moir JW, Richardson DJ, Zumft WG, Thomson AJ
Title Two enzymes with a common function but different heme ligands in the forms as isolated. Optical and magnetic properties of the heme groups in the oxidized forms of nitrite reductase, cytochrome cd1, from Pseudomonas stutzeri and Thiosphaera pantotropha.
Related PDB
Related UniProtKB
[3]
Resource
Comments
Medline ID
PubMed ID 9199411
Journal J Mol Biol
Year 1997
Volume 269
Pages 440-55
Authors Baker SC, Saunders NF, Willis AC, Ferguson SJ, Hajdu J, Fulop V
Title Cytochrome cd1 structure: unusual haem environments in a nitrite reductase and analysis of factors contributing to beta-propeller folds.
Related PDB
Related UniProtKB
[4]
Resource
Comments
Medline ID
PubMed ID 9311786
Journal Nature
Year 1997
Volume 389
Pages 406-12
Authors Williams PA, Fulop V, Garman EF, Saunders NF, Ferguson SJ, Hajdu J
Title Haem-ligand switching during catalysis in crystals of a nitrogen-cycle enzyme.
Related PDB 1aof 1aom 1aoq
Related UniProtKB
[5]
Resource
Comments
Medline ID
PubMed ID 10320660
Journal Biochim Biophys Acta
Year 1999
Volume 1411
Pages 231-49
Authors Cutruzzola F
Title Bacterial nitric oxide synthesis.
Related PDB
Related UniProtKB
[6]
Resource
Comments
Medline ID
PubMed ID 10747791
Journal Biochemistry
Year 2000
Volume 39
Pages 4028-36
Authors Koppenhofer A, Little RH, Lowe DJ, Ferguson SJ, Watmough NJ
Title Oxidase reaction of cytochrome cd(1) from Paracoccus pantotrophus.
Related PDB
Related UniProtKB
[7]
Resource
Comments
Medline ID
PubMed ID 10757972
Journal Biochemistry
Year 2000
Volume 39
Pages 4243-9
Authors Koppenhofer A, Turner KL, Allen JW, Chapman SK, Ferguson SJ
Title Cytochrome cd(1) from Paracoccus pantotrophus exhibits kinetically gated, conformationally dependent, highly cooperative two-electron redox behavior.
Related PDB
Related UniProtKB
[8]
Resource
Comments
Medline ID
PubMed ID 10998233
Journal Biochemistry
Year 2000
Volume 39
Pages 10967-74
Authors Sjogren T, Svensson-Ek M, Hajdu J, Brzezinski P
Title Proton-coupled structural changes upon binding of carbon monoxide to cytochrome cd1: a combined flash photolysis and X-ray crystallography study.
Related PDB 1dy7
Related UniProtKB
[9]
Resource
Comments
Medline ID
PubMed ID 10827177
Journal J Biol Chem
Year 2000
Volume 275
Pages 25089-94
Authors Jafferji A, Allen JW, Ferguson SJ, Fulop V
Title X-ray crystallographic study of cyanide binding provides insights into the structure-function relationship for cytochrome cd1 nitrite reductase from Paracoccus pantotrophus.
Related PDB 1e2r
Related UniProtKB
[10]
Resource
Comments
Medline ID
PubMed ID 10708389
Journal Microbiology
Year 2000
Volume 146
Pages 509-16
Authors Saunders NF, Ferguson SJ, Baker SC
Title Transcriptional analysis of the nirS gene, encoding cytochrome cd1 nitrite reductase, of Paracoccus pantotrophus LMD 92.63.
Related PDB
Related UniProtKB
[11]
Resource
Comments
Medline ID
PubMed ID 11062553
Journal Nat Struct Biol
Year 2000
Volume 7
Pages 1006-12
Authors Hajdu J, Neutze R, Sjogren T, Edman K, Szoke A, Wilmouth RC, Wilmot CM
Title Analyzing protein functions in four dimensions.
Related PDB
Related UniProtKB
[12]
Resource
Comments
Medline ID
PubMed ID 11373294
Journal J Biol Chem
Year 2001
Volume 276
Pages 29450-5
Authors Sjogren T, Hajdu J
Title The Structure of an alternative form of Paracoccus pantotrophus cytochrome cd(1) nitrite reductase.
Related PDB 1h9x 1h9y 1hcm
Related UniProtKB
[13]
Resource
Comments
Medline ID
PubMed ID 11278884
Journal J Biol Chem
Year 2001
Volume 276
Pages 13072-6
Authors Sjogren T, Hajdu J
Title Structure of the bound dioxygen species in the cytochrome oxidase reaction of cytochrome cd1 nitrite reductase.
Related PDB 1hj3 1hj4 1hj5
Related UniProtKB
[14]
Resource
Comments
Medline ID
PubMed ID 11035020
Journal J Biol Chem
Year 2001
Volume 276
Pages 5846-55
Authors Steensma E, Gordon E, Oster LM, Ferguson SJ, Hajdu J
Title Heme ligation and conformational plasticity in the isolated c domain of cytochrome cd1 nitrite reductase.
Related PDB
Related UniProtKB
[15]
Resource
Comments
Medline ID
PubMed ID 12086580
Journal Biochem J
Year 2002
Volume 366
Pages 883-8
Authors Allen JW, Higham CW, Zajicek RS, Watmough NJ, Ferguson SJ
Title A novel, kinetically stable, catalytically active, all-ferric, nitrite-bound complex of Paracoccus pantotrophus cytochrome cd1.
Related PDB
Related UniProtKB
[16]
Resource
Comments
Medline ID
PubMed ID 12556530
Journal J Biol Chem
Year 2003
Volume 278
Pages 11773-81
Authors Gordon EH, Sjogren T, Lofqvist M, Richter CD, Allen JW, Higham CW, Hajdu J, Fulop V, Ferguson SJ
Title Structure and kinetic properties of Paracoccus pantotrophus cytochrome cd1 nitrite reductase with the d1 heme active site ligand tyrosine 25 replaced by serine.
Related PDB 1gq1
Related UniProtKB

Comments
This structure contains a heme protein, cytochrome cd1.
Although this enzyme is homologous to the counterpart from Pseudomonas aeriginosa (Swiss-prot; P24474, D00055 in EzCatDB), the active site residues and positions are slightly different from that. In this enzyme, c heme iron coordination can change from His17/His69 to Met106/His69, whereas the counterpart enzyme has got c heme iron coordination with Met88/His51. Moreover, the counterpart enzyme does not have a residue corresponding to Tyr25 in this enzyme.
Although only two E.C. numbers (1.7.2.1 and 1.7.99.1) have been annotated in Swiss-prot data (Swiss-prot; P72181), this enzyme also seems to catalyze the reaction, corresponding to E.C. 1.9.3.1, according to the literature.
Thus, this enzyme catalyzes the following reactions:
(a) NO2(-) + 2 H(+) + e- = NO + H2O
(b) NH3 + H2O + acceptor = hydroxylamine + reduced acceptor.
(c) O2 + 4 H(+) + 4 e- = 2 H2O
#####
There are some other kind of "nitrite reductases":
E.C. 1.7.1.4 nitrite reductase [NAD(P)H]
E.C. 1.7.2.2 nitrite reductase (cytochrome; ammonia-forming)
E.C. 1.7.7.1 ferredoxin-nitrite reductase
Another nitrite reductase enzyme (E.C. 1.7.2.1) which contains multiple copper centres, is described in D00449 in EzCatDB.

Created Updated
2005-07-05 2009-02-26