DB code: M00159

CATH domain -.-.-.- :
-.-.-.- :
-.-.-.- :
2.40.30.10 : Elongation Factor Tu (Ef-tu); domain 3
3.40.50.80 : Rossmann fold Catalytic domain
E.C. 1.7.1.1
CSA 2cnd
M-CSA 2cnd
MACiE

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

Uniprot Enzyme Name
UniprotKB Protein name Synonyms Pfam
P17571 Nitrate reductase {NADH}
NR
EC 1.7.1.1
PF00173 (Cyt-b5)
PF00970 (FAD_binding_6)
PF03404 (Mo-co_dimer)
PF00175 (NAD_binding_1)
PF00174 (Oxidored_molyb)
[Graphical View]

KEGG enzyme name
nitrate reductase (NADH)
assimilatory nitrate reductase
NADH-nitrate reductase
NADH-dependent nitrate reductase
assimilatory NADH: nitrate reductase
nitrate reductase (NADH2)
NADH2:nitrate oxidoreductase

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P17571 NIA1_MAIZE Nitrite + NAD(+) + H(2)O = nitrate + NADH. Homodimer. Binds 1 FAD. Binds 1 heme group. The heme group is called cytochrome b-557. Binds 1 molybdenum ion.

KEGG Pathways
Map code Pathways E.C.
MAP00910 Nitrogen metabolism

Compound table
Cofactors Substrates Products Intermediates
KEGG-id C00016 C00150 C00032 C00003 C00088 C00001 C00004 C00244 C00080
E.C.
Compound FAD Molybdenum Heme NAD+ Nitrite H2O NADH Nitrate H+
Type amide group,amine group,aromatic ring (only carbon atom),aromatic ring (with nitrogen atoms),carbohydrate,nucleotide heavy metal aromatic ring (with nitrogen atoms),carboxyl group,heavy metal amide group,amine group,nucleotide others H2O amide group,amine group,nucleotide organic ion others
ChEBI 16238
 16238
 		28685
 28685
 		17627
 26355
 17627
 26355
 		15846
 15846
 		25567
 25567
 		15377
 15377
 		16908
 16908
 		48107
 48107
 		15378
 15378
PubChem 643975
 643975
 		23932
 23932
 		5893
 5893
 		24529
 24529
 		22247451
 962
 22247451
 962
 		439153
 439153
 		944
 944
 		1038
 1038
1cndA01 Bound:FAD Unbound Unbound Unbound Unbound Unbound Unbound
1cneA01 Bound:FAD Unbound Unbound Unbound Unbound Unbound Unbound
1cnfA01 Bound:FAD Unbound Unbound Unbound Unbound Unbound Unbound
2cndA01 Bound:FAD Unbound Unbound Unbound Unbound Unbound Unbound
1cndA02 Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1cneA02 Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1cnfA02 Unbound Unbound Unbound Unbound Unbound Analogue:ADP Unbound
2cndA02 Unbound Unbound Unbound Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
literature [7], [10]

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1cndA01
1cneA01
1cnfA01
2cndA01
1cndA02 CYS 242
1cneA02 mutant C242S
1cnfA02 CYS 242
2cndA02 CYS 242

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[2]
Fig.6
[6]
p.13788-13789

References
[1]
Resource
Comments
Medline ID
PubMed ID 3007465
Journal J Biol Chem
Year 1986
Volume 261
Pages 4562-7
Authors Barber MJ, Solomonson LP
Title The role of the essential sulfhydryl group in assimilatory NADH: nitrate reductase of Chlorella.
Related PDB
Related UniProtKB
[2]
Resource
Comments
Medline ID
PubMed ID 3015963
Journal J Biol Chem
Year 1986
Volume 261
Pages 11290-4
Authors Solomonson LP, Barber MJ, Robbins AP, Oaks A
Title Functional domains of assimilatory NADH:nitrate reductase from Chlorella.
Related PDB
Related UniProtKB
[3]
Resource
Comments
Medline ID
PubMed ID 2189408
Journal Biochem Biophys Res Commun
Year 1990
Volume 168
Pages 1285-91
Authors Hyde GE, Campbell WH
Title High-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.
Related PDB
Related UniProtKB
[4]
Resource
Comments
Medline ID
PubMed ID 2176886
Journal Biochemistry
Year 1990
Volume 29
Pages 10823-8
Authors Kay CJ, Solomonson LP, Barber MJ
Title Oxidation-reduction potentials of flavin and Mo-pterin centers in assimilatory nitrate reductase: variation with pH.
Related PDB
Related UniProtKB
[5]
Resource
Comments
Medline ID
PubMed ID 1548707
Journal J Mol Biol
Year 1992
Volume 224
Pages 277-9
Authors Lu G, Campbell W, Lindqvist Y, Schneider G
Title Crystallization and preliminary crystallographic studies of the FAD domain of corn NADH: nitrate reductase.
Related PDB
Related UniProtKB
[6]
Resource
Comments MUTAGENESIS OF CYS-593
Medline ID 94245686
PubMed ID 8188655
Journal J Biol Chem
Year 1994
Volume 269
Pages 13785-91
Authors Dwivedi UN, Shiraishi N, Campbell WH
Title Identification of an "essential" cysteine of nitrate reductase via mutagenesis of its recombinant cytochrome b reductase domain.
Related PDB
Related UniProtKB P17571
[7]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF FAD DOMAIN
Medline ID 95111952
PubMed ID 7812715
Journal Structure
Year 1994
Volume 2
Pages 809-21
Authors Lu G, Campbell WH, Schneider G, Lindqvist Y
Title Crystal structure of the FAD-containing fragment of corn nitrate reductase at 2.5 A resolution: relationship to other flavoprotein reductases.
Related PDB
Related UniProtKB P17571
[8]
Resource
Comments
Medline ID
PubMed ID 7656976
Journal FEBS Lett
Year 1995
Volume 370
Pages 197-202
Authors Meyer C, Gonneau M, Caboche M, Rouze P
Title Identification by mutational analysis of four critical residues in the molybdenum cofactor domain of eukaryotic nitrate reductase.
Related PDB
Related UniProtKB
[9]
Resource
Comments
Medline ID
PubMed ID 7592606
Journal J Biol Chem
Year 1995
Volume 270
Pages 24067-72
Authors Ratnam K, Shiraishi N, Campbell WH, Hille R
Title Spectroscopic and kinetic characterization of the recombinant wild-type and C242S mutant of the cytochrome b reductase fragment of nitrate reductase.
Related PDB
Related UniProtKB
[10]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 232-501
Medline ID 95280311
PubMed ID 7760334
Journal J Mol Biol
Year 1995
Volume 248
Pages 931-48
Authors Lu G, Lindqvist Y, Schneider G, Dwivedi U, Campbell W
Title Structural 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 PDB 1cnd 1cne 1cnf 2cnd
Related UniProtKB P17571
[11]
Resource
Comments
Medline ID
PubMed ID 8552051
Journal Mol Gen Genet
Year 1995
Volume 249
Pages 456-64
Authors Gonzalez C, Brito N, Marzluf GA
Title Functional analysis by site-directed mutagenesis of individual amino acid residues in the flavin domain of Neurospora crassa nitrate reductase.
Related PDB
Related UniProtKB
[12]
Resource
Comments
Medline ID
PubMed ID 8880927
Journal Proteins
Year 1996
Volume 26
Pages 32-41
Authors Nishida H, Miki K
Title Electrostatic 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.
Related PDB
Related UniProtKB
[13]
Resource
Comments
Medline ID
PubMed ID 9507089
Journal Biochim Biophys Acta
Year 1998
Volume 1382
Pages 129-36
Authors Wei X, Ming LJ, Cannons AC, Solomonson LP
Title 1H and 13C NMR studies of a truncated heme domain from Chlorella vulgaris nitrate reductase: signal assignment of the heme moiety.
Related PDB
Related UniProtKB
[14]
Resource
Comments
Medline ID
PubMed ID 11566032
Journal Arch Biochem Biophys
Year 2001
Volume 394
Pages 99-110
Authors Barber MJ, Desai SK, Marohnic CC
Title Assimilatory nitrate reductase: lysine 741 participates in pyridine nucleotide binding via charge complementarity.
Related PDB
Related UniProtKB
[15]
Resource
Comments
Medline ID
PubMed ID 11356830
Journal J Biol Chem
Year 2001
Volume 276
Pages 26995-7002
Authors Skipper L, Campbell WH, Mertens JA, Lowe DJ
Title Pre-steady-state kinetic analysis of recombinant Arabidopsis NADH:nitrate reductase: rate-limiting processes in catalysis.
Related PDB
Related UniProtKB

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.

Created Updated
2004-12-20 2009-02-26