EzCatDB: D00498
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DB codeD00498
CATH domainDomain 11.10.760.10 : Cytochrome Bc1 Complex; Chain D, domain 2Catalytic domain
Domain 22.140.10.20 : Methanol Dehydrogenase; Chain ACatalytic domain
E.C.1.7.2.1,1.7.99.1,1.9.3.1

CATH domainRelated DB codes (homologues)
1.10.760.10 : Cytochrome Bc1 Complex; Chain D, domain 2D00055,M00179
2.140.10.20 : Methanol Dehydrogenase; Chain AD00055

Enzyme Name
UniProtKBKEGG

P72181
Protein nameNitrite reductasenitrite 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)

SynonymsEC 1.7.2.1
Cytochrome cd1
Cytochrome oxidase
Hydroxylamine reductase
EC 1.7.99.1

KEGG pathways
MAP codePathwaysE.C.
MAP00190Oxidative phosphorylation1.9.3.1
MAP00910Nitrogen metabolism1.7.2.1,1.7.99.1

UniProtKB:Accession NumberP72181
Entry nameNIRS_PARPN
ActivityNitric oxide + H(2)O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H(+).,NH(3) + H(2)O + acceptor = hydroxylamine + reduced acceptor.
SubunitHomodimer.
Subcellular locationPeriplasm.
CofactorBinds 2 heme groups per subunit.

Compound table: links to PDB-related databases & PoSSuM

CofactorsSubstratesProducts
KEGG-idC00032C00032C00088C00126C00080C00014C00028C00007C00533C00001C00125C00192C00030
E.C.1.7.2.1,1.7.99.1,1.9.3.11.7.2.1,1.7.99.1,1.9.3.11.7.2.11.7.2.1,1.9.3.11.7.2.1,1.9.3.11.7.99.11.7.99.11.9.3.11.7.2.11.7.2.1,1.7.99.1,1.9.3.11.7.2.1,1.9.3.11.7.99.11.7.99.1
Compoundc hemed1 hemeNitriteFerrocytochrome cH+AmmoniaAcceptorO2Nitric oxideH2OFerricytochrome cHydroxylamineReduced acceptor
Typearomatic ring (with nitrogen atoms),carboxyl group,heavy metalaromatic ring (with nitrogen atoms),carboxyl group,heavy metalothersamide group,amine group,aromatic ring (with nitrogen atoms),carboxyl group,heavy metal,sulfide groupothersamine group,organic ionothersothersothersH2Oamide group,amine group,aromatic ring (with nitrogen atoms),carboxyl group,heavy metal,sulfide groupamine groupothers
ChEBI17627
26355
17627
26355
25567

15378
16134

27140
26689
15379
16480
15377

15429

PubChem

24529

1038
222

977
145068
962
22247451

787

                     
1aofA01Bound:HEMUnboundUnboundUnbound UnboundUnboundUnboundUnbound UnboundUnboundUnbound
1aofB01Bound:HEMUnboundUnboundUnbound UnboundUnboundUnboundUnbound UnboundUnboundUnbound
1aomB01Bound:HEMUnboundUnboundUnbound UnboundUnboundUnboundUnbound UnboundUnboundUnbound
1aoqA01Bound:HEMUnboundUnboundUnbound UnboundUnboundUnboundUnbound UnboundUnboundUnbound
1aoqB01Bound:HEMUnboundUnboundUnbound UnboundUnboundUnboundUnbound UnboundUnboundUnbound
1dy7B01Bound:HECUnboundUnboundUnbound UnboundUnboundUnboundUnbound UnboundUnboundUnbound
1e2rA01Bound:HECUnboundUnboundUnbound UnboundUnboundUnboundUnbound UnboundUnboundUnbound
1e2rB01Bound:HECUnboundUnboundUnbound UnboundUnboundUnboundUnbound UnboundUnboundUnbound
1gq1A01Bound:HECUnboundUnboundUnbound UnboundUnboundUnboundUnbound UnboundUnboundUnbound
1gq1B01Bound:HECUnboundUnboundUnbound UnboundUnboundUnboundUnbound UnboundUnboundUnbound
1h9xA01Bound:HECUnboundUnboundUnbound UnboundUnboundUnboundUnbound UnboundUnboundUnbound
1h9xB01Bound:HECUnboundUnboundUnbound UnboundUnboundUnboundUnbound UnboundUnboundUnbound
1h9yA01Bound:HECUnboundUnboundUnbound UnboundUnboundUnboundUnbound UnboundUnboundUnbound
1h9yB01Bound:HECUnboundUnboundUnbound UnboundUnboundUnboundUnbound UnboundUnboundUnbound
1hcmA01Bound:HECUnboundUnboundUnbound UnboundUnboundUnboundUnbound UnboundUnboundUnbound
1hcmB01Bound:HECUnboundUnboundUnbound UnboundUnboundUnboundUnbound UnboundUnboundUnbound
1hj3A01Bound:HECUnboundUnboundUnbound UnboundUnboundUnboundUnbound UnboundUnboundUnbound
1hj3B01Bound:HECUnboundUnboundUnbound UnboundUnboundUnboundUnbound UnboundUnboundUnbound
1hj4A01Bound:HECUnboundUnboundUnbound UnboundUnboundUnboundUnbound UnboundUnboundUnbound
1hj4B01Bound:HECUnboundUnboundUnbound UnboundUnboundUnboundUnbound UnboundUnboundUnbound
1hj5A01Bound:HECUnboundUnboundUnbound UnboundUnboundUnboundUnbound UnboundUnboundUnbound
1hj5B01Bound:HECUnboundUnboundUnbound UnboundUnboundUnboundUnbound UnboundUnboundUnbound
1qksA01Bound:HECUnboundUnboundUnbound UnboundUnboundUnboundUnbound UnboundUnboundUnbound
1qksB01Bound:HECUnboundUnboundUnbound UnboundUnboundUnboundUnbound UnboundUnboundUnbound
1aofA02UnboundBound:DHEAnalogue:SO2Unbound UnboundUnboundUnboundUnbound UnboundUnboundUnbound
1aofB02UnboundBound:DHEAnalogue:SO2Unbound UnboundUnboundUnboundUnbound UnboundUnboundUnbound
1aomA02UnboundBound:DHEBound:2NOUnbound UnboundUnboundUnboundUnbound UnboundUnboundUnbound
1aomB02UnboundBound:DHEUnboundUnbound UnboundUnboundUnboundBound:_NO UnboundUnboundUnbound
1aoqA02UnboundBound:DHEBound:2NOUnbound UnboundUnboundUnboundUnbound UnboundUnboundUnbound
1aoqB02UnboundBound:DHEUnboundUnbound UnboundUnboundUnboundBound:_NO UnboundUnboundUnbound
1dy7A02UnboundBound:DHEUnboundUnbound UnboundUnboundUnboundAnalogue:CMO UnboundUnboundUnbound
1dy7B02UnboundBound:DHEUnboundUnbound UnboundUnboundUnboundAnalogue:CMO UnboundUnboundUnbound
1e2rA02UnboundBound:DHEUnboundUnbound UnboundUnboundUnboundAnalogue:CYN UnboundUnboundUnbound
1e2rB02UnboundBound:DHEUnboundUnbound UnboundUnboundUnboundAnalogue:CYN UnboundUnboundUnbound
1gq1A02UnboundBound:DHEUnboundUnbound UnboundUnboundUnboundUnbound UnboundUnboundUnbound
1gq1B02UnboundBound:DHEUnboundUnbound UnboundUnboundUnboundUnbound UnboundUnboundUnbound
1h9xA02UnboundBound:DHEUnboundUnbound UnboundUnboundUnboundUnbound UnboundUnboundUnbound
1h9xB02UnboundBound:DHEUnboundUnbound UnboundUnboundUnboundUnbound UnboundUnboundUnbound
1h9yA02UnboundBound:DHEUnboundUnbound UnboundUnboundUnboundAnalogue:CYN UnboundUnboundUnbound
1h9yB02UnboundBound:DHEUnboundUnbound UnboundUnboundUnboundAnalogue:CYN UnboundUnboundUnbound
1hcmA02UnboundBound:DHEUnboundUnbound UnboundUnboundUnboundUnbound UnboundUnboundUnbound
1hcmB02UnboundBound:DHEUnboundUnbound UnboundUnboundUnboundUnbound UnboundUnboundUnbound
1hj3A02UnboundBound:DHEUnboundUnbound UnboundUnboundUnboundUnbound UnboundUnboundUnbound
1hj3B02UnboundBound:DHEUnboundUnbound UnboundUnboundBound:OXYUnbound UnboundUnboundUnbound
1hj4A02UnboundBound:DHEUnboundUnbound UnboundUnboundUnboundUnbound UnboundUnboundUnbound
1hj4B02UnboundBound:DHEUnboundUnbound UnboundUnboundUnboundUnbound UnboundUnboundUnbound
1hj5A02UnboundBound:DHEUnboundUnbound UnboundUnboundUnboundUnbound UnboundUnboundUnbound
1hj5B02UnboundBound:DHEUnboundUnbound UnboundUnboundUnboundUnbound UnboundUnboundUnbound
1qksA02UnboundBound:DHEUnboundUnbound UnboundUnboundUnboundUnbound UnboundUnboundUnbound
1qksB02UnboundBound:DHEUnboundUnbound UnboundUnboundUnboundUnbound UnboundUnboundUnbound

Active-site residues
pdbCatalytic residuesCofactor-binding residuescomment
           
1aofA01 
       ;HIS  69;MET 106(Heme c axial binding);CYS  65;CYS  68(Heme c covalent);               
truncated 1-35
1aofB01 
       ;HIS  69;MET 106(Heme c axial binding);CYS  65;CYS  68(Heme c covalent);               
truncated 1-35
1aomB01 
HIS  17;HIS  69;       (Heme c axial binding);CYS  65;CYS  68(Heme c covalent);TYR 25(Heme d1)
 
1aoqA01 
HIS  17;HIS  69;       (Heme c axial binding);CYS  65;CYS  68(Heme c covalent);TYR 25(Heme d1)
 
1aoqB01 
HIS  17;HIS  69;       (Heme c axial binding);CYS  65;CYS  68(Heme c covalent);TYR 25(Heme d1)
 
1dy7B01 
       ;HIS  69;MET 106(Heme c axial binding);CYS  65;CYS  68(Heme c covalent);               
truncated 1-31
1e2rA01 
       ;HIS  69;MET 106(Heme c axial binding);CYS  65;CYS  68(Heme c covalent);               
truncated 1-35
1e2rB01 
       ;HIS  69;MET 106(Heme c axial binding);CYS  65;CYS  68(Heme c covalent);               
truncated 1-35
1gq1A01 
HIS  17;HIS  69;       (Heme c axial binding);CYS  65;CYS  68(Heme c covalent);               
mutant Y25S
1gq1B01 
HIS  17;HIS  69;       (Heme c axial binding);CYS  65;CYS  68(Heme c covalent);               
mutant Y25S
1h9xA01 
       ;HIS  69;MET 106(Heme c axial binding);CYS  65;CYS  68(Heme c covalent);               
truncated 1-41
1h9xB01 
       ;HIS  69;MET 106(Heme c axial binding);CYS  65;CYS  68(Heme c covalent);               
truncated 1-41
1h9yA01 
       ;HIS  69;MET 106(Heme c axial binding);CYS  65;CYS  68(Heme c covalent);               
truncated 1-47
1h9yB01 
       ;HIS  69;MET 106(Heme c axial binding);CYS  65;CYS  68(Heme c covalent);               
truncated 1-47
1hcmA01 
       ;HIS  69;MET 106(Heme c axial binding);CYS  65;CYS  68(Heme c covalent);               
truncated 1-41
1hcmB01 
       ;HIS  69;MET 106(Heme c axial binding);CYS  65;CYS  68(Heme c covalent);               
truncated 1-41
1hj3A01 
HIS  17;HIS  69;       (Heme c axial binding);CYS  65;CYS  68(Heme c covalent);TYR 25(Heme d1)
 
1hj3B01 
       ;HIS  69;       (Heme c axial binding);CYS  65;CYS  68(Heme c covalent);               
truncated 1-25
1hj4A01 
HIS  17;HIS  69;       (Heme c axial binding);CYS  65;CYS  68(Heme c covalent);TYR 25(Heme d1)
 
1hj4B01 
       ;HIS  69;       (Heme c axial binding);CYS  65;CYS  68(Heme c covalent);               
truncated 1-25
1hj5A01 
HIS  17;HIS  69;       (Heme c axial binding);CYS  65;CYS  68(Heme c covalent);TYR 25(Heme d1)
 
1hj5B01 
HIS  17;HIS  69;       (Heme c axial binding);CYS  65;CYS  68(Heme c covalent);TYR 25(Heme d1)
 
1qksA01 
HIS  17;HIS  69;       (Heme c axial binding);CYS  65;CYS  68(Heme c covalent);TYR 25(Heme d1)
 
1qksB01 
HIS  17;HIS  69;       (Heme c axial binding);CYS  65;CYS  68(Heme c covalent);TYR 25(Heme d1)
 
1aofA02HIS 345;HIS 388
HIS 200(Heme d1 proximal binding)
 
1aofB02HIS 345;HIS 388
HIS 200(Heme d1 proximal binding)
 
1aomA02HIS 345;HIS 388
HIS 200(Heme d1 proximal binding)
 
1aomB02HIS 345;HIS 388
HIS 200(Heme d1 proximal binding)
 
1aoqA02HIS 345;HIS 388
HIS 200(Heme d1 proximal binding)
 
1aoqB02HIS 345;HIS 388
HIS 200(Heme d1 proximal binding)
 
1dy7A02HIS 345;HIS 388
HIS 200(Heme d1 proximal binding)
 
1dy7B02HIS 345;HIS 388
HIS 200(Heme d1 proximal binding)
 
1e2rA02HIS 345;HIS 388
HIS 200(Heme d1 proximal binding)
 
1e2rB02HIS 345;HIS 388
HIS 200(Heme d1 proximal binding)
 
1gq1A02HIS 345;HIS 388
HIS 200(Heme d1 proximal binding)
 
1gq1B02HIS 345;HIS 388
HIS 200(Heme d1 proximal binding)
 
1h9xA02HIS 345;HIS 388
HIS 200(Heme d1 proximal binding)
 
1h9xB02HIS 345;HIS 388
HIS 200(Heme d1 proximal binding)
 
1h9yA02HIS 345;HIS 388
HIS 200(Heme d1 proximal binding)
 
1h9yB02HIS 345;HIS 388
HIS 200(Heme d1 proximal binding)
 
1hcmA02HIS 345;HIS 388
HIS 200(Heme d1 proximal binding)
 
1hcmB02HIS 345;HIS 388
HIS 200(Heme d1 proximal binding)
 
1hj3A02HIS 345;HIS 388
HIS 200(Heme d1 proximal binding)
 
1hj3B02HIS 345;HIS 388
HIS 200(Heme d1 proximal binding)
 
1hj4A02HIS 345;HIS 388
HIS 200(Heme d1 proximal binding)
 
1hj4B02HIS 345;HIS 388
HIS 200(Heme d1 proximal binding)
 
1hj5A02HIS 345;HIS 388
HIS 200(Heme d1 proximal binding)
 
1hj5B02HIS 345;HIS 388
HIS 200(Heme d1 proximal binding)
 
1qksA02HIS 345;HIS 388
HIS 200(Heme d1 proximal binding)
 
1qksB02HIS 345;HIS 388
HIS 200(Heme d1 proximal binding)
 

References for Catalytic Mechanism
ReferencesSectionsNo. 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]
PubMed ID7736589
JournalCell
Year1995
Volume81
Pages369-77
AuthorsFulop V, Moir JW, Ferguson SJ, Hajdu J
TitleThe anatomy of a bifunctional enzyme: structural basis for reduction of oxygen to water and synthesis of nitric oxide by cytochrome cd1.
Related PDB1qks
[2]
PubMed ID9405061
JournalBiochemistry
Year1997
Volume36
Pages16267-76
AuthorsCheesman MR, Ferguson SJ, Moir JW, Richardson DJ, Zumft WG, Thomson AJ
TitleTwo 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.
[3]
PubMed ID9199411
JournalJ Mol Biol
Year1997
Volume269
Pages440-55
AuthorsBaker SC, Saunders NF, Willis AC, Ferguson SJ, Hajdu J, Fulop V
TitleCytochrome cd1 structure: unusual haem environments in a nitrite reductase and analysis of factors contributing to beta-propeller folds.
[4]
PubMed ID9311786
JournalNature
Year1997
Volume389
Pages406-12
AuthorsWilliams PA, Fulop V, Garman EF, Saunders NF, Ferguson SJ, Hajdu J
TitleHaem-ligand switching during catalysis in crystals of a nitrogen-cycle enzyme.
Related PDB1aof,1aom,1aoq
[5]
PubMed ID10320660
JournalBiochim Biophys Acta
Year1999
Volume1411
Pages231-49
AuthorsCutruzzola F
TitleBacterial nitric oxide synthesis.
[6]
PubMed ID10747791
JournalBiochemistry
Year2000
Volume39
Pages4028-36
AuthorsKoppenhofer A, Little RH, Lowe DJ, Ferguson SJ, Watmough NJ
TitleOxidase reaction of cytochrome cd(1) from Paracoccus pantotrophus.
[7]
PubMed ID10757972
JournalBiochemistry
Year2000
Volume39
Pages4243-9
AuthorsKoppenhofer A, Turner KL, Allen JW, Chapman SK, Ferguson SJ
TitleCytochrome cd(1) from Paracoccus pantotrophus exhibits kinetically gated, conformationally dependent, highly cooperative two-electron redox behavior.
[8]
PubMed ID10998233
JournalBiochemistry
Year2000
Volume39
Pages10967-74
AuthorsSjogren T, Svensson-Ek M, Hajdu J, Brzezinski P
TitleProton-coupled structural changes upon binding of carbon monoxide to cytochrome cd1: a combined flash photolysis and X-ray crystallography study.
Related PDB1dy7
[9]
PubMed ID10827177
JournalJ Biol Chem
Year2000
Volume275
Pages25089-94
AuthorsJafferji A, Allen JW, Ferguson SJ, Fulop V
TitleX-ray crystallographic study of cyanide binding provides insights into the structure-function relationship for cytochrome cd1 nitrite reductase from Paracoccus pantotrophus.
Related PDB1e2r
[10]
PubMed ID10708389
JournalMicrobiology
Year2000
Volume146
Pages509-16
AuthorsSaunders NF, Ferguson SJ, Baker SC
TitleTranscriptional analysis of the nirS gene, encoding cytochrome cd1 nitrite reductase, of Paracoccus pantotrophus LMD 92.63.
[11]
PubMed ID11062553
JournalNat Struct Biol
Year2000
Volume7
Pages1006-12
AuthorsHajdu J, Neutze R, Sjogren T, Edman K, Szoke A, Wilmouth RC, Wilmot CM
TitleAnalyzing protein functions in four dimensions.
[12]
PubMed ID11373294
JournalJ Biol Chem
Year2001
Volume276
Pages29450-5
AuthorsSjogren T, Hajdu J
TitleThe Structure of an alternative form of Paracoccus pantotrophus cytochrome cd(1) nitrite reductase.
Related PDB1h9x,1h9y,1hcm
[13]
PubMed ID11278884
JournalJ Biol Chem
Year2001
Volume276
Pages13072-6
AuthorsSjogren T, Hajdu J
TitleStructure of the bound dioxygen species in the cytochrome oxidase reaction of cytochrome cd1 nitrite reductase.
Related PDB1hj3,1hj4,1hj5
[14]
PubMed ID11035020
JournalJ Biol Chem
Year2001
Volume276
Pages5846-55
AuthorsSteensma E, Gordon E, Oster LM, Ferguson SJ, Hajdu J
TitleHeme ligation and conformational plasticity in the isolated c domain of cytochrome cd1 nitrite reductase.
[15]
PubMed ID12086580
JournalBiochem J
Year2002
Volume366
Pages883-8
AuthorsAllen JW, Higham CW, Zajicek RS, Watmough NJ, Ferguson SJ
TitleA novel, kinetically stable, catalytically active, all-ferric, nitrite-bound complex of Paracoccus pantotrophus cytochrome cd1.
[16]
PubMed ID12556530
JournalJ Biol Chem
Year2003
Volume278
Pages11773-81
AuthorsGordon EH, Sjogren T, Lofqvist M, Richter CD, Allen JW, Higham CW, Hajdu J, Fulop V, Ferguson SJ
TitleStructure and kinetic properties of Paracoccus pantotrophus cytochrome cd1 nitrite reductase with the d1 heme active site ligand tyrosine 25 replaced by serine.
Related PDB1gq1

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.

createdupdated
2005-07-052009-02-26


Copyright: Nozomi Nagano, JST & CBRC-AIST
Funded by PRESTO/Japan Science and Technology Corporation (JST) (December 2001 - November 2004)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2012 - March 2013)
Supported by the commission for the Development of Artificial Gene Synthesis Technology for Creating Innovative Biomaterial from the Ministry of Economy, Trade and Industry (METI) (October 2012 - )
© Biotechnology Research Institute for Drug Discovery, AIST, 2015-2016 All Rights Reserved.
© Computational Biology Research Center, AIST, 2004-2016 All Rights Reserved.