Reviewed, UniProtKB/Swiss-Prot P49102 (NIA3_MAIZE)

Names and origin

Protein names	Recommended name:     Nitrate reductase [NADH] 3       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	889 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

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(+) + H(2)O = nitrate + NADH.
Cofactor	Binds 1 FAD per subunit By similarity. Binds 1 heme group per subunit By similarity. Binds 1 molybdenum-pterin group per subunit By similarity.
Subunit structure	Homodimer By similarity.
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
Gene Ontology (GO)
Biological process	nitrate assimilation Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	FAD binding Inferred from electronic annotation. Source: InterPro electron carrier activity Inferred from electronic annotation. Source: InterPro heme binding Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: InterPro molybdenum ion binding Inferred from electronic annotation. Source: InterPro 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 – 889	889	Nitrate reductase [NADH] 3		PRO_0000166064
Regions
	Domain	520 – 595	76	Cytochrome b5 heme-binding
	Domain	630 – 742	113	FAD-binding FR-type
Sites
	Metal binding	181	1	Molybdenum-pterin Potential
	Metal binding	235	1	Molybdenum-pterin Potential
	Metal binding	555	1	Iron (heme axial ligand) By similarity
	Metal binding	578	1	Iron (heme axial ligand) By similarity
Amino acid modifications
	Disulfide bond	404		Interchain Potential

Sequences

	Sequence		Length	Mass (Da)
	P49102-1 [UniParc]. Last modified February 1, 1996. Version 1. Checksum: 3614A8BB44B822F5	FASTA	889	98,811
	10 20 30 40 50 60 MSTCVEQPTH SASLDPTAAQ RLPYPDLPVD ILRRSSVRGS GFVAAALVSS ARKADDDARH 70 80 90 100 110 120 DDDDPSGDRH ETYGSHYLAN LGVEQSVRDE GTVDAWVESS QSLIRLTGKH SLNGELPRLM 130 140 150 160 170 180 RHGFITPVPR HYVRNHGPVP RGDWATWTVE VTGLVRRPRA LTMDELARDF PALELPVTLV 190 200 210 220 230 240 CAGNRRKEQN MVRQTLGFNW GPGAVSTSVW RGARLSDVLR RCGSMSRKGG ALFVCFEGAE 250 260 270 280 290 300 DLPGGGGTKY GTSITREVAL DPTMDVMLAY QQNGGPLLPD HGFPVRLIVP GCTAGRMVKW 310 320 330 340 350 360 LKRIVVAPAE SDNYYHYRDN RFLPSHVDAK LADAEGWWYK PEYVINEMNT NSVITTPAHN 370 380 390 400 410 420 EFLPINAITT QRIYTMKGFA YSGGGKKVTR VEVTLDGGEN WLLCELDHPE KPTKYGRYWC 430 440 450 460 470 480 WCFWSIDVEL IDLLACKEIA VRAWDQSLNT QPEFLTWNLM GMMTNCWFRV KVNVCRPRHG 490 500 510 520 530 540 EKAGLAFEHP VRTNQPGGWM AQQKHLETAE RTSAATSTTN QQFTMSEVRK HASQDSAWIV 550 560 570 580 590 600 VHGHVYDCTA FLKDHPGGAD SILINAGTDC TEEFDAIHSD KAKELLDTYR IGDLVTTGGA 610 620 630 640 650 660 EQRSPLELAP SPPIRHEGPA APVIALSNPR EKVPCQLVAR TVLSRDVRLF RFALPSSGQV 670 680 690 700 710 720 LGLPVGKHIF VCASIDGKLC MRAYTPTSSV DEVGHFDLLV KVYFRNENTK FPDGGRMTQY 730 740 750 760 770 780 LDSLPVGAHV DVKGPLGHVE YVGRGGFVID GKPRKAGRLA MVAGGSGITP IYQVIQAVLR 790 800 810 820 830 840 DQPEDKTEMH LVYANRTEDD ILLRAELDRW AAEYPERLKV WYVVSQVKRL DEWKYSVGIV 850 860 870 880 TEAVLRDDVP EARDGTLALL CGPPSMIQSP ILPNLEKMKH QLDDSVVSF

References

[1]	Campbell W.H., Redinbaugh M.G., Ingemarsson B., Doughtery E.S., Campbell E.R. Submitted (JAN-1995) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: cv. B73. Tissue: Seedling.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U20450 Genomic DNA. Translation: AAA62316.1.
PIR	T02240.
3D structure databases
HSSP	HSSP built from PDB template 2CND based on UniProtKB P17571.
SMR	P49102. Positions 632-889.
ModBase	Search...
Organism-specific databases
Gramene	P49102.
MaizeGDB	30041.
Family and domain databases
InterPro	IPR001199. Cyt_B5. IPR001834. Cyt_B5_reductase. IPR001709. FPN_cyt_redctse. IPR005066. MoCF_OxRdtse_dimer. IPR008335. Mopterin_OxRdtase_euk. IPR012137. Nitr_rd_NADH. 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]
PIRSF	PIRSF000233. Nitr_rd_NADH. 1 hit.
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. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

NIA3_MAIZE

Accession

Primary (citable) accession number: P49102

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	February 1, 1996
Last modified:	November 25, 2008
This is version 64 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)