EzCatDB: M00159
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DB codeM00159
CATH domainDomain 1-.-.-.-
Domain 2-.-.-.-
Domain 3-.-.-.-
Domain 42.40.30.10 : Elongation Factor Tu (Ef-tu); domain 3
Domain 53.40.50.80 : Rossmann foldCatalytic domain
E.C.1.7.1.1
CSA2cnd

CATH domainRelated DB codes (homologues)
2.40.30.10 : Elongation Factor Tu (Ef-tu); domain 3D00043,M00006,M00141,M00164
3.40.50.80 : Rossmann foldD00043,M00006,M00141,M00164

Enzyme Name
UniProtKBKEGG

P17571
Protein nameNitrate reductase {NADH}nitrate reductase (NADH)
assimilatory nitrate reductase
NADH-nitrate reductase
NADH-dependent nitrate reductase
assimilatory NADH: nitrate reductase
nitrate reductase (NADH2)
NADH2:nitrate oxidoreductase
SynonymsNR
EC 1.7.1.1
PfamPF00173 (Cyt-b5)
PF00970 (FAD_binding_6)
PF03404 (Mo-co_dimer)
PF00175 (NAD_binding_1)
PF00174 (Oxidored_molyb)
[Graphical view]

KEGG pathways
MAP codePathways
MAP00910Nitrogen metabolism

UniProtKB:Accession NumberP17571
Entry nameNIA1_MAIZE
ActivityNitrite + NAD(+) + H(2)O = nitrate + NADH.
SubunitHomodimer.
Subcellular location
CofactorBinds 1 FAD.,Binds 1 heme group. The heme group is called cytochrome b-557.,Binds 1 molybdenum ion.

Compound table: links to PDB-related databases & PoSSuM

CofactorsSubstratesProducts
KEGG-idC00016C00150C00032C00003C00088C00001C00004C00244C00080
CompoundFADMolybdenumHemeNAD+NitriteH2ONADHNitrateH+
Typeamide group,amine group,aromatic ring (only carbon atom),aromatic ring (with nitrogen atoms),carbohydrate,nucleotideheavy metalaromatic ring (with nitrogen atoms),carboxyl group,heavy metalamide group,amine group,nucleotideothersH2Oamide group,amine group,nucleotideorganic ionothers
ChEBI16238
28685
17627
26355
15846
25567
15377
16908
48107
15378
PubChem643975
23932

5893
24529
962
22247451
439153
944
1038
                 
1cndA01Bound:FADUnboundUnboundUnboundUnbound UnboundUnbound 
1cneA01Bound:FADUnboundUnboundUnboundUnbound UnboundUnbound 
1cnfA01Bound:FADUnboundUnboundUnboundUnbound UnboundUnbound 
2cndA01Bound:FADUnboundUnboundUnboundUnbound UnboundUnbound 
1cndA02UnboundUnboundUnboundUnboundUnbound UnboundUnbound 
1cneA02UnboundUnboundUnboundUnboundUnbound UnboundUnbound 
1cnfA02UnboundUnboundUnboundUnboundUnbound Analogue:ADPUnbound 
2cndA02UnboundUnboundUnboundUnboundUnbound UnboundUnbound 

Active-site residues
resource
literature [7], [10]
pdbCatalytic residuescomment
          
1cndA01       
 
1cneA01       
 
1cnfA01       
 
2cndA01       
 
1cndA02CYS 242
 
1cneA02       
mutant C242S
1cnfA02CYS 242
 
2cndA02CYS 242
 

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[2]Fig.6
[6]p.13788-13789

references
[1]
PubMed ID3007465
JournalJ Biol Chem
Year1986
Volume261
Pages4562-7
AuthorsBarber MJ, Solomonson LP
TitleThe role of the essential sulfhydryl group in assimilatory NADH: nitrate reductase of Chlorella.
[2]
PubMed ID3015963
JournalJ Biol Chem
Year1986
Volume261
Pages11290-4
AuthorsSolomonson LP, Barber MJ, Robbins AP, Oaks A
TitleFunctional domains of assimilatory NADH:nitrate reductase from Chlorella.
[3]
PubMed ID2189408
JournalBiochem Biophys Res Commun
Year1990
Volume168
Pages1285-91
AuthorsHyde GE, Campbell WH
TitleHigh-level expression in Escherichia coli of the catalytically active flavin domain of corn leaf NADH:nitrate reductase and its comparison to human NADH:cytochrome B5 reductase.
[4]
PubMed ID2176886
JournalBiochemistry
Year1990
Volume29
Pages10823-8
AuthorsKay CJ, Solomonson LP, Barber MJ
TitleOxidation-reduction potentials of flavin and Mo-pterin centers in assimilatory nitrate reductase: variation with pH.
[5]
PubMed ID1548707
JournalJ Mol Biol
Year1992
Volume224
Pages277-9
AuthorsLu G, Campbell W, Lindqvist Y, Schneider G
TitleCrystallization and preliminary crystallographic studies of the FAD domain of corn NADH: nitrate reductase.
[6]
CommentsMUTAGENESIS OF CYS-593
Medline ID94245686
PubMed ID8188655
JournalJ Biol Chem
Year1994
Volume269
Pages13785-91
AuthorsDwivedi UN, Shiraishi N, Campbell WH
TitleIdentification of an "essential" cysteine of nitrate reductase via mutagenesis of its recombinant cytochrome b reductase domain.
Related UniProtKBP17571
[7]
CommentsX-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF FAD DOMAIN
Medline ID95111952
PubMed ID7812715
JournalStructure
Year1994
Volume2
Pages809-21
AuthorsLu G, Campbell WH, Schneider G, Lindqvist Y
TitleCrystal structure of the FAD-containing fragment of corn nitrate reductase at 2.5 A resolution: relationship to other flavoprotein reductases.
Related UniProtKBP17571
[8]
PubMed ID7656976
JournalFEBS Lett
Year1995
Volume370
Pages197-202
AuthorsMeyer C, Gonneau M, Caboche M, Rouze P
TitleIdentification by mutational analysis of four critical residues in the molybdenum cofactor domain of eukaryotic nitrate reductase.
[9]
PubMed ID7592606
JournalJ Biol Chem
Year1995
Volume270
Pages24067-72
AuthorsRatnam K, Shiraishi N, Campbell WH, Hille R
TitleSpectroscopic and kinetic characterization of the recombinant wild-type and C242S mutant of the cytochrome b reductase fragment of nitrate reductase.
[10]
CommentsX-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 232-501
Medline ID95280311
PubMed ID7760334
JournalJ Mol Biol
Year1995
Volume248
Pages931-48
AuthorsLu G, Lindqvist Y, Schneider G, Dwivedi U, Campbell W
TitleStructural studies on corn nitrate reductase: refined structure of the cytochrome b reductase fragment at 2.5 A, its ADP complex and an active-site mutant and modeling of the cytochrome b domain.
Related PDB1cnd,1cne,1cnf,2cnd
Related UniProtKBP17571
[11]
PubMed ID8552051
JournalMol Gen Genet
Year1995
Volume249
Pages456-64
AuthorsGonzalez C, Brito N, Marzluf GA
TitleFunctional analysis by site-directed mutagenesis of individual amino acid residues in the flavin domain of Neurospora crassa nitrate reductase.
[12]
PubMed ID8880927
JournalProteins
Year1996
Volume26
Pages32-41
AuthorsNishida H, Miki K
TitleElectrostatic properties deduced from refined structures of NADH-cytochrome b5 reductase and the other flavin-dependent reductases: pyridine nucleotide-binding and interaction with an electron-transfer partner.
[13]
PubMed ID9507089
JournalBiochim Biophys Acta
Year1998
Volume1382
Pages129-36
AuthorsWei X, Ming LJ, Cannons AC, Solomonson LP
Title1H and 13C NMR studies of a truncated heme domain from Chlorella vulgaris nitrate reductase: signal assignment of the heme moiety.
[14]
PubMed ID11566032
JournalArch Biochem Biophys
Year2001
Volume394
Pages99-110
AuthorsBarber MJ, Desai SK, Marohnic CC
TitleAssimilatory nitrate reductase: lysine 741 participates in pyridine nucleotide binding via charge complementarity.
[15]
PubMed ID11356830
JournalJ Biol Chem
Year2001
Volume276
Pages26995-7002
AuthorsSkipper L, Campbell WH, Mertens JA, Lowe DJ
TitlePre-steady-state kinetic analysis of recombinant Arabidopsis NADH:nitrate reductase: rate-limiting processes in catalysis.

comments
This enzyme was transferred from E.C. 1.6.6.1 to E.C. 1.7.1.1.
This enzyme belongs to "assimilatory nitrate reductase" family.
This enzyme is composed of N-terminal Acidic domain, Molybdopterin-binding domain, Heme-binding domain, FAD-binding domain and C-terminal NADH-binding domain (see [7]).
The PDB structures correspond to the C-terminal domains, FAD-binding and NADH-binding domains.

createdupdated
2004-12-202009-02-26


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