Reviewed, UniProtKB/Swiss-Prot P17569 (NIA_CUCMA)

Names and origin

Protein names	Recommended name:     Nitrate reductase [NADH]       Short name=NR     EC=1.7.1.1
Organism	Cucurbita maxima (Pumpkin) (Winter squash)
Taxonomic identifier	3661 [NCBI]
Taxonomic lineage	Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids I › Cucurbitales › Cucurbitaceae › Cucurbita

Protein attributes

Sequence length	918 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
Induction	By nitrate.
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 – 918	918	Nitrate reductase [NADH]		PRO_0000166055
Regions
	Domain	543 – 618	76	Cytochrome b5 heme-binding
	Domain	661 – 774	114	FAD-binding FR-type
Sites
	Metal binding	195	1	Molybdenum-pterin Potential
	Metal binding	249	1	Molybdenum-pterin Potential
	Metal binding	578	1	Iron (heme axial ligand) By similarity
	Metal binding	601	1	Iron (heme axial ligand) By similarity
Amino acid modifications
	Disulfide bond	434		Interchain Potential

Sequences

	Sequence		Length	Mass (Da)
	P17569-1 [UniParc]. Last modified August 1, 1990. Version 1. Checksum: A2CAFDDADEA1B2D1	FASTA	918	103,384
	10 20 30 40 50 60 MAASVDNRQY GPLQPPLSGV VRSFKNGPNH RADSPVRGCN FPNSNVDYNN NRPLKSSVKI 70 80 90 100 110 120 QEAAAEEMED SCSEDENENE FRDLIVKGNR ELEPSILDHR DEGTADNWIE RNASMVRLTG 130 140 150 160 170 180 KHPFNSEPPL NRLMHHGFIT PVPLHYVRNH GVVPKAKWAD WTVEVCGLVK RPAKFTMDQL 190 200 210 220 230 240 LNEFRFREFP ATLVCAGNRR KEQNMVKQSI GFNWGAAGVS TSVWRRVPLC DLLKRCGILS 250 260 270 280 290 300 RKKGALNVCF EGAEDLPGGG GSKYGTSIKK ELAMDPARDI ILAYMQNGEQ LAPDHGFPVR 310 320 330 340 350 360 MIIPGFIGGR MVKWLKRIIV TTKESENYYH FKDNRVLPSH VDADVANAEA WWYKPEHIIN 370 380 390 400 410 420 ELNINSVITT PCHEEILPIN AWTTQRPYTL RGYSYSGGGK KVTRVEVTMD SGETWQVCTL 430 440 450 460 470 480 DHPEKANKYG KYWCWCFWSL EVEVLDLLSA KEIAVRAWDE THNTQPEKLI WNLMGMMNNC 490 500 510 520 530 540 WFRVKTNMCK PHKGEIGIVF EHPTQPGNQS GGWMDRERHL EISTESNQTL KKSVSTPFMN 550 560 570 580 590 600 TASNTYTLSE VKKHNSPQSA WIIVHGHVYD CTRFLKDHPG GSDSILINAG TDCTEEFDAI 610 620 630 640 650 660 HSDKAKKMLE DYRIGELITT GYASDSSSNS PNNSTHGASN FSHLAPIREA PVSRRVALAP 670 680 690 700 710 720 NEKIPCKLIS KTSISHDVRV FRFALPGGQD QALGLPVGKH IFICATVDGK LCMRAYTPTS 730 740 750 760 770 780 SIDEMGFFEL VVKVYFKGVH PKFPNGGIMS QYLDSMEVGS TLDVKGPLGH IEYTGRGNFM 790 800 810 820 830 840 VHGKPRFARR LAMLAGGTGI TPIYQVVQAI LKDPEDETEM YVVYANRTED DILLRDELDT 850 860 870 880 890 900 WAKKNQRLKV WYVVQESIRE GWEYSVGFIT ENILREHIPA AAEDTLALAC GPPAMIQFAV 910 QPNLEKMNYD TKNSLLVF

References

[1]	"Nitrate reductase from squash: cDNA cloning and nitrate regulation." Crawford N.M., Campbell W.H., Davis R. Proc. Natl. Acad. Sci. U.S.A. 83:8073-8076(1986) [PubMed: 16593773] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"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: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Seedling.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M33154 mRNA. Translation: AAA33114.1.
PIR	A41667.
3D structure databases
HSSP	HSSP built from PDB template 2CND based on UniProtKB P17571.
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.7.1.1. 2176.
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_CUCMA

Accession

Primary (citable) accession number: P17569

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1990
Last sequence update:	August 1, 1990
Last modified:	June 16, 2009
This is version 74 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)