Reviewed, UniProtKB/Swiss-Prot P17571 (NIA1_MAIZE)

Names and origin

Protein names	Recommended name:     Nitrate reductase [NADH]       Short name=NR     EC=1.7.1.1
Organism	Zea mays (Maize)
Taxonomic identifier	4577 [NCBI]
Taxonomic lineage	Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › Liliopsida › Poales › Poaceae › PACCAD clade › Panicoideae › Andropogoneae › Zea

Protein attributes

Sequence length	621 AA.
Sequence status	Fragment.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Nitrate reductase is a key enzyme involved in the first step of nitrate assimilation in plants, fungi and bacteria.
Catalytic activity	Nitrite + NAD+ + H2O = nitrate + NADH.
Cofactor	Binds 1 FAD. Binds 1 heme group. The heme group is called cytochrome b-557. Binds 1 molybdenum ion.
Subunit structure	Homodimer.
Sequence similarities	Belongs to the nitrate reductase family. Contains 1 cytochrome b5 heme-binding domain. Contains 1 FAD-binding FR-type domain.

Ontologies

Keywords
Biological process	Nitrate assimilation
Ligand	FAD Flavoprotein Heme Iron Metal-binding Molybdenum NAD
Molecular function	Oxidoreductase
PTM	Disulfide bond
Technical term	3D-structure
Gene Ontology (GO)
Biological process	nitrate assimilation Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	electron carrier activity Inferred from electronic annotation. Source: InterPro heme binding Inferred from electronic annotation. Source: InterPro molybdenum ion binding Inferred from electronic annotation. Source: UniProtKB-KW nitrate reductase (NADH) activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

‹1 – 621

›621

Nitrate reductase [NADH]

PRO_0000166062

Regions

Domain

249 – 324

76

Cytochrome b5 heme-binding

Domain

361 – 473

113

FAD-binding FR-type

Sites

Metal binding

284

1

Iron (heme axial ligand) By similarity

Metal binding

307

1

Iron (heme axial ligand) By similarity

Site

593

1

Necessary for efficient electron Transfer

Amino acid modifications

Disulfide bond

138

Interchain Potential

Experimental info

Mutagenesis

593

1

C → S: Reduction of activity. Ref.4

Non-terminal residue

1

1

Secondary structure

1

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621

Helix Strand Turn

Details...

Beta strand

367 – 371

5

Beta strand

378 – 384

7

Beta strand

425 – 432

8

Beta strand

436 – 438

3

Helix

447 – 454

8

Beta strand

474 – 479

6

Beta strand

481 – 486

6

Beta strand

488 – 492

5

Helix

500 – 511

12

Turn

513 – 515

3

Beta strand

519 – 522

4

Helix

536 – 539

4

Helix

541 – 544

4

Turn

546 – 548

3

Turn

561 – 563

3

Helix

574 – 578

5

Turn

585 – 587

3

Helix

597 – 600

4

Turn

601 – 603

3

Helix

606 – 609

4

Turn

615 – 617

3

Sequences

	Sequence		Length	Mass (Da)
	P17571-1 [UniParc]. Last modified February 1, 1995. Version 2. Checksum: ACC276E4ED0FF5D3	FASTA	621	69,773
	10 20 30 40 50 60 GFPVRVIIPG CIGGRMVKWL KRIIVTPAES DNYYHFKDNR VLPSHVDAEL ANAEAWWYKP 70 80 90 100 110 120 EYIINELNIN SVITTPCHDE ILPINAFTTQ RPYTLKGYAY SGGGKKVTRV EVTLDGGETW 130 140 150 160 170 180 LVCTDHPEKP TKYGKYWCWC FWSLEVEVLD LLSAKEIAVR AWDESLNTQP EKLIWNVMGM 190 200 210 220 230 240 MNNCWFRVKT NVCKPHKGEI GIVFDHPTLP GNESGGWMAK EKHLETAEAA APGLKRSTST 250 260 270 280 290 300 PFMNTTDVGK EFTMSEVRKH ASQESAWIVV HGHVYDCTKF LKDHPGGADS ILINAGTDCT 310 320 330 340 350 360 EEFDAIHSDK AKALLDTYRI GELITTGTGY SSDNSVHGGS VLSHLAPIRR AVRAPALSNP 370 380 390 400 410 420 REKIHCRLVG KKELSRDVRL FRFSLPSPDQ VLGLPIGKHI FVCASIEGKL CMRAYTPTSM 430 440 450 460 470 480 VDEIGHFDLL VKVYFKNEHP KFPNGGLMTQ YLDSLPVGSY IDVKGPLGHV EYTGRGSFVI 490 500 510 520 530 540 NGKQRHASRL AMICGGSGIT PMYQIIQAVL RDQPEDHTEM HLVYANRTED DILLRDELDR 550 560 570 580 590 600 WAAEYPDRLK VWYVIDQVKR PEEGWKYSVG FVTEAVLREH VPEGGDDTLA LACGPPPMIQ 610 620 FAISPNLEKM KYDMANSFVV F

References

[1]	"cDNA clones for corn leaf NADH: nitrate reductase and chloroplast NAD(P)(+): glyceraldehyde-3-phosphate dehydrogenase." Gowri G., Campbell W.H. Plant Physiol. 90:792-798(1989) [PubMed: 16666879] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. W64 X W128E. Tissue: Leaf.
[2]	"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." Hyde G.E., Campbell W.H. Biochem. Biophys. Res. Commun. 168:1285-1291(1990) [PubMed: 2189408] [Abstract] Cited for: SEQUENCE REVISION TO 389-390; 405-406 AND 414-417, CHARACTERIZATION. Strain: cv. W64 X W128E. Tissue: Leaf.
[3]	"The sequence of squash NADH:nitrate reductase and its relationship to the sequences of other flavoprotein oxidoreductases. A family of flavoprotein pyridine nucleotide cytochrome reductases." Hyde G.E., Crawford N.M., Campbell W.H. J. Biol. Chem. 266:23542-23547(1991) [PubMed: 1748631] [Abstract] Cited for: SECONDARY STRUCTURE OF FAD DOMAIN.
[4]	"Identification of an 'essential' cysteine of nitrate reductase via mutagenesis of its recombinant cytochrome b reductase domain." Dwivedi U.N., Shiraishi N., Campbell W.H. J. Biol. Chem. 269:13785-13791(1994) [PubMed: 8188655] [Abstract] Cited for: MUTAGENESIS OF CYS-593.
[5]	"Crystal structure of the FAD-containing fragment of corn nitrate reductase at 2.5-A resolution: relationship to other flavoprotein reductases." Lu G., Campbell W.H., Schneider G., Lindqvist Y. Structure 2:809-821(1994) [PubMed: 7812715] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF FAD DOMAIN.
[6]	"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." Lu G., Lindqvist Y., Schneider G., Dwivedi U., Campbell W.H. J. Mol. Biol. 248:931-948(1995) [PubMed: 7760334] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 232-501.

Cross-references

Sequence databases

EMBLGenBankDDBJ

M27821 mRNA. Translation: AAA03202.1. Sequence problems.

PIR

S19254.

UniGene

Zm.15815

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1CNE	X-ray	3.00	A	352-621	[»]
1CNF	X-ray	2.70	A	352-621	[»]
2CND	X-ray	2.50	A	352-621	[»]

ModBase

Search...

Organism-specific databases

Gramene

P17571.

MaizeGDB

25899.

Enzyme and pathway databases

BRENDA

1.7.1.1. 289.

Family and domain databases

InterPro

IPR001199. Cyt_B5.
IPR018506. Cyt_B5_heme-BS.
IPR017927. Fd_Rdtase_FAD-bd.
IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
IPR005066. MoCF_OxRdtse_dimer.
IPR008335. Mopterin_OxRdtase_euk.
IPR001834. NADH-Cyt_B5_reductase.
IPR008333. OxRdtase_FAD-bd.
IPR001433. OxRdtase_FAD/NAD_bd.
IPR000572. OxRdtase_Mopterin-bd.
[Graphical view]

Gene3D

G3DSA:3.10.120.10. Cyt_B5. 1 hit.
G3DSA:2.60.40.650. MoCF_oxrdtse_dimer. 1 hit.
G3DSA:3.90.420.10. Oxred_molyb_bd. 1 hit.

Pfam

PF00173. Cyt-b5. 1 hit.
PF00970. FAD_binding_6. 1 hit.
PF03404. Mo-co_dimer. 1 hit.
PF00175. NAD_binding_1. 1 hit.
PF00174. Oxidored_molyb. 1 hit.
[Graphical view]

PRINTS

PR00406. CYTB5RDTASE.
PR00363. CYTOCHROMEB5.
PR00407. EUMOPTERIN.
PR00371. FPNCR.

ProDom

PD000612. Cyt_B5. 1 hit.
[Graphical view] [Entries sharing at least one domain]

PROSITE

PS00191. CYTOCHROME_B5_1. 1 hit.
PS50255. CYTOCHROME_B5_2. 1 hit.
PS51384. FAD_FR. 1 hit.
PS00559. MOLYBDOPTERIN_EUK. Partial match.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

NIA1_MAIZE

Accession

Primary (citable) accession number: P17571

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1990
Last sequence update:	February 1, 1995
Last modified:	June 16, 2009
This is version 91 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)