Reviewed, UniProtKB/Swiss-Prot P39869 (NIA_LOTJA)

Names and origin

Protein names

Recommended name:
    Nitrate reductase [NADH]
      Short name=NR
    EC=1.7.1.1

Gene names

Name:

NIA

Organism

Lotus japonicus

Taxonomic identifier

34305 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids I › Fabales › Fabaceae › Papilionoideae › Loteae › Lotus

Protein attributes

Sequence length	900 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+ + 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 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
PTM	Disulfide bond
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	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 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 – 900	900	Nitrate reductase [NADH]		PRO_0000166059
Regions
	Domain	521 – 596	76	Cytochrome b5 heme-binding
	Domain	644 – 756	113	FAD-binding FR-type
Sites
	Metal binding	172	1	Molybdenum-pterin Potential
	Metal binding	226	1	Molybdenum-pterin Potential
	Metal binding	556	1	Iron (heme axial ligand) By similarity
	Metal binding	579	1	Iron (heme axial ligand) By similarity
Amino acid modifications
	Disulfide bond	411		Interchain Potential

Sequences

	Sequence		Length	Mass (Da)
	P39869-1 [UniParc]. Last modified February 1, 1995. Version 1. Checksum: 547C25388DD13535	FASTA	900	101,420
	10 20 30 40 50 60 MAASVDNRQY STLNGVVRSF TPNNTYLHDP KPSFPAVNLD LDASSSDDDD EKDDASILKD 70 80 90 100 110 120 LIRKGNAEIE SSVLDPRDQG TADNWISRNS SMVRLTGKHP FNSEPPLPRL MHHGFITPVP 130 140 150 160 170 180 LHYVRNHGPV PKARWDDWTV EVTGLVKTPT RFSMDRLVRD FPSRELPVTL VCAGNRRKEQ 190 200 210 220 230 240 NMVRQSIGFN WGSAGVSTSV WRGVSLRHIL RRCRIQTRSR GALHVCFEGD EDLPGGGGSK 250 260 270 280 290 300 YSTSIRREVA MDPSRDVILA YMQNGEVLAP DHGFPVRVII PGFIGGRMVK WLKRIVVTEE 310 320 330 340 350 360 ECDGHYHYKD NRVLPSHVDA ELANEEGWWY KPEYIINELN INSVITTPCH DEILPINAWT 370 380 390 400 410 420 TQRPYTLRGY SYSGGGRKVT RVEVTLDGGE TWFVCALDQQ EKPNKYGKYW CWCFWSLEVE 430 440 450 460 470 480 VLDLLGTKEI AVRAWDEALN TQPENLIWNV MGMMNNCWFR VKTNVCKPHK GEIGIVFEHP 490 500 510 520 530 540 TQPGNQPGGW MAKEKHLEIS QQDSRPILKK SVSSPFMNTF TKMYSLSEVK KHNSPDSAWI 550 560 570 580 590 600 IVHGHVYDCT RFLKDHPGGA DSILINAGTD CTEEFEAIHS DKAKKMLEDY RVGELITTGY 610 620 630 640 650 660 TSDSSSPNNS LHGNSEFKHL APIKEITTMS LPPLPRRKVA LIPREKIPCK LISRTSISHD 670 680 690 700 710 720 VRVFRFALPS EDQQLGLPVG KHIFLCATVD GKLCMRAYTP TSGVDEVGYF ELVVKVYFKG 730 740 750 760 770 780 VHPKFPNGGA MSQHLDSLPI GSDLDVKGPL GHIEYTGRGN FLVHGKHRFA KKLAMLAGGT 790 800 810 820 830 840 GITPIYQVAQ AILKDPEDHT KMYVVYANRT EDDILLREEL DTWAKKYEDR FKVWYVVETA 850 860 870 880 890 900 KEGWGYSVGF VTEGVMREHL PEAGDDALAL ACGPPPMIQF AVNPNLEKMG YDVKNDLLVF

References

[1]	Waterhouse R.N., Smyth A.J., Prosser I.M., Forde B.G., Clarkson D.T. Submitted (JUL-1994) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: cv. Gifu / B-129.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X80670 Genomic DNA. Translation: CAA56696.1.
PIR	S47029.
3D structure databases
HSSP	HSSP built from PDB template 2CND based on UniProtKB P17571.
SMR	P39869. Positions 646-900.
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.7.1.1. 977.
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. 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

NIA_LOTJA

Accession

Primary (citable) accession number: P39869

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
Last modified:	June 16, 2009
This is version 63 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)