P23312 (NIA_SPIOL) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Gene names

Name:

NIA

Organism

Spinacia oleracea (Spinach)

Taxonomic identifier

3562 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › Caryophyllales › Amaranthaceae › Spinacia

Protein attributes

Sequence length	926 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript 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 per subunit. Binds 1 heme group per subunit. Binds 1 molybdenum-pterin group per subunit.
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
Gene Ontology (GO)
Biological process	nitrate assimilation Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	electron carrier activity Inferred from electronic annotation. Source: InterPro flavin adenine dinucleotide binding Inferred from electronic annotation. Source: InterPro heme 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 – 926	926	Nitrate reductase [NADH]		PRO_0000166071
Regions
	Domain	551 – 626	76	Cytochrome b5 heme-binding
	Domain	670 – 782	113	FAD-binding FR-type
Sites
	Metal binding	204	1	Molybdenum-pterin Potential
	Metal binding	258	1	Molybdenum-pterin Potential
	Metal binding	586	1	Iron (heme axial ligand) By similarity
	Metal binding	609	1	Iron (heme axial ligand) By similarity
Amino acid modifications
	Disulfide bond	443		Interchain Potential
Experimental info
	Sequence conflict	303	1	D → A in BAA13047. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P23312 [UniParc]. Last modified November 1, 1991. Version 1. Checksum: FF21DF01963F1AFC	FASTA	926	103,971
	10 20 30 40 50 60 MAASVDRQYH PAPMSGVVRT PFSNHHRSDS PVRNGYTFSN PPSSNGVVKP GEKIKLVDNN 70 80 90 100 110 120 SNSNNGSNNN NNRYDSDSEE DDDENEMNVW NEMIKKGNSE LEPSSVDSRD EGTADQWIER 130 140 150 160 170 180 NPSMIRLTGK HPFNSEPPLT RLMHHGFLTP VPLHYVRNHG PVPNAKWEDW TVEVTGLVKR 190 200 210 220 230 240 PIRFTMDQLV NDFQSREFPV TLVCAGNRRK EQNMTKQSIG FNWGSAAVST SVWRGVPLRD 250 260 270 280 290 300 VLKRCGVMSS LKGALNVCFE GAEDLPGGGG SKYGTSVKRE FAMDPARDII LAYMQNGEKL 310 320 330 340 350 360 SPDHGYPVRM IIPGFIGGRM VKWLKRIIVT TTESDNYYHY KDNRVLPSHV DAELANSEAW 370 380 390 400 410 420 WYKQEYIINE LNVNSVITSP CHEEILPINA WTTQRPYTMR GYAYSGGGRK VTRVEVTMDG 430 440 450 460 470 480 GDTWDICELD HQERGSKYGK FWCWCFWSLE VEVLDLLGAK EIGVRAWDES LNTQPEKLIW 490 500 510 520 530 540 NVMGMMNNCW FRVKTNVCKP HKGEIGIVFE HPTQPGNKSG GWMARERHLE ISDSGPTLKR 550 560 570 580 590 600 TASTPFMNTT SKMYSMSEVK KHNTADSAWI VVHGNVYNAT RFLKDHPGGS DSILINAGTD 610 620 630 640 650 660 CTEEFDAIHS DKAKRLLEDF RIGELISTGY TSDSSSPGNS VHGGSVYSGL AGLAPITEAV 670 680 690 700 710 720 PLRNVALNPR VKIPCKLIEK VSLSHDVRRF RFGLPSEDQV LGLPVGKHIF LCANVDDKLC 730 740 750 760 770 780 MRAYTPSSTI DVVGYFDLVV KVYFKDVHPR FPNGGVMSQH LDSLSLGSIV DVKGPLGHIE 790 800 810 820 830 840 YLGKGNFTVH GKPKFAKKLA MISGGTGITP IYQVMQAILK DPEDKTEMHV VYANRTEEDI 850 860 870 880 890 900 LLREELDKWA DEFRDRVKVW YVVEKAEEGW KYDTGFISEK ILRDHVPAVG DDVLALTCGP 910 920 PPMIQFAVQP NLDKMGFDIK EQLLIF

References

[1]	"Nucleotide sequence of a spinach nitrate reductase cDNA." Prosser I.M., Lazarus C.M. Plant Mol. Biol. 15:187-190(1990) [PubMed: 2103436] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"The nitrate reductase gene isolated from DNA of cultured spinach cells." Tamura N., Takahashi H., Takeba G., Satoi T., Nakagawa H. Biochim. Biophys. Acta 1338:151-155(1997) [PubMed: 9128133] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: cv. Hoyo.
[3]	"Sequence analysis of cloned cDNA and proteolytic fragments for nitrate reductase from Spinacia oleracea L." Shiraishi N., Kubo Y., Takeba K., Kiyota S., Sakano K., Nakagawa H. Plant Cell Physiol. 32:1031-1038(1991) Cited for: NUCLEOTIDE SEQUENCE OF 287-926. Strain: cv. Hoyo.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M32600 mRNA. Translation: AAA34033.1. D86226 Genomic DNA. Translation: BAA13047.1. U08029 mRNA. Translation: AAA18377.1.
PIR	RDSPNH. S11868.
3D structure databases
ProteinModelPortal	P23312.
SMR	P23312. Positions 672-926.
ModBase	Search...
Protein-protein interaction databases
IntAct	P23312. 1 interaction.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
InterPro	IPR001199. Cyt_B5. IPR018506. Cyt_B5_heme-BS. IPR017927. Fd_Rdtase_FAD-bd. IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase. IPR014756. Ig_E-set. IPR005066. MoCF_OxRdtse_dimer. IPR008335. Mopterin_OxRdtase_euk. IPR001834. NADH-Cyt_B5_reductase. IPR012137. Nitr_rd_NADH. IPR008333. OxRdtase_FAD-bd_dom. IPR001433. OxRdtase_FAD/NAD-bd. IPR000572. OxRdtase_Mopterin-bd_dom. IPR022407. OxRdtase_Mopterin_BS. IPR017938. Riboflavin_synthase-like_b-brl. [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.
SUPFAM	SSF55856. Cyt_B5. 1 hit. SSF81296. Ig_E-set. 1 hit. SSF56524. Oxidored_molyb. 1 hit. SSF63380. Riboflavin_synthase_like_b-brl. 1 hit.
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_SPIOL

Accession

Primary (citable) accession number: P23312
Secondary accession number(s): Q41377

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1991
Last sequence update:	November 1, 1991
Last modified:	October 19, 2011
This is version 82 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program