Reviewed, UniProtKB/Swiss-Prot P39864 (NIA_PHYIN)

Names and origin

Protein names

Recommended name:
    Nitrate reductase [NADPH]
      Short name=NR
    EC=1.7.1.3

Gene names

Name:

NIAA

Organism

Phytophthora infestans (Potato late blight fungus)

Taxonomic identifier

4787 [NCBI]

Taxonomic lineage

Eukaryota › stramenopiles › Oomycetes › Peronosporales › Phytophthora

Protein attributes

Sequence length	902 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 + NADP(+) + H(2)O = nitrate + NADPH.
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 NADP
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 (NADPH) 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 – 902	902	Nitrate reductase [NADPH]		PRO_0000166047
Regions
	Domain	537 – 612	76	Cytochrome b5 heme-binding
	Domain	637 – 751	115	FAD-binding FR-type
	Nucleotide binding	872 – 879	8	NADP By similarity
Sites
	Metal binding	182	1	Molybdenum-pterin Potential
	Metal binding	234	1	Molybdenum-pterin Potential
	Metal binding	572	1	Iron (heme axial ligand) By similarity
	Metal binding	595	1	Iron (heme axial ligand) By similarity
Amino acid modifications
	Disulfide bond	419		Interchain Potential

Sequences

	Sequence		Length	Mass (Da)
	P39864-1 [UniParc]. Last modified February 1, 1995. Version 1. Checksum: 05B9F4E1A381BBE6	FASTA	902	101,074
	10 20 30 40 50 60 MTRLRSAAST ITNRSTPALA LTASHAGSHP AVIVPIQPLL LTLERRPSCP HRVSYPEIEA 70 80 90 100 110 120 YRGISSSLRS HNAIVRASDI MAQIDPRDVG TPDEWVPRHP ELIRLTGRHP FNSEPPLKYA 130 140 150 160 170 180 STFITPMALH YVRNHGPVPR LEWDTHTFSI DGLVKKPRTF GMNELVTTFE QETVTFPVLL 190 200 210 220 230 240 VCAGNRRKEQ NMIKKTIGFS WGAAGCSTAE WTGVPLHVLL TACGVDREKA QWVWFEGIED 250 260 270 280 290 300 LPHDKYGTCI RASTELDPEC DVLVAWKANG ELLGPDHGFP VRLIVPGHIG GRMVKWLERI 310 320 330 340 350 360 HVSDHESSNH HHIMDNRVLP SHVTAETATA EGWWSKSPYA IMELNVNAVV ILPNHDDLLA 370 380 390 400 410 420 LGEDTTFNDI ETYTIKGYAY SGGGRRVIRV EVTLDDGASW QLARIIYHER PSKYGKMWCW 430 440 450 460 470 480 VHYELAAPMS SLLCAREVCV RAWDSSMNLM PAFPTWNVMG MMNNPWYRVK IHHEQDTNSL 490 500 510 520 530 540 RFEHPTQAGN QKGGWMTKER IMTNDVDSIK MLQVEPLDTS SAATPKPGLT ADELSELPLI 550 560 570 580 590 600 FADEVAKHNS KKSCWFICRD LVYDATPFLD EHPGGATSIL LCGGTDCTDE FESIHSTKAW 610 620 630 640 650 660 QMLKKYCIGR CSSTEDDTGT SDTSSDHEET DVALKGRTKV PIVLISREVV SHDARIFKFA 670 680 690 700 710 720 LPAKDLRLGL PIGNHVFLYA KINGKTAVRA YTPISSENDE DRGFVSFLIK VYFAGDNPVH 730 740 750 760 770 780 PEGGLFSQYL DGLHLGQQIQ IKGPLGHFTY YGDGNFSLET TNFHAYKFGF VAGGTGITPV 790 800 810 820 830 840 YQVMRAILED AKDQTKVALI YCVRSQRDLL LRKELETLQK LRPGQCRIFY TLSDMELLDR 850 860 870 880 890 900 NDPIVRGWAY GKSRLNFAMV KNIIGSDAED VCMCGPEGMI EYACKPALLK LNYDLKTQTT VF

References

[1]

"NiaA, the structural nitrate reductase gene of Phytophthora infestans: isolation, characterization and expression analysis in Aspergillus nidulans." Pieterse C.M.J., van 't Klooster J., van den Berg-Velthuis G.C.M., Govers F. Curr. Genet. 27:359-366(1995) [PubMed: 7614559] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: Isolate 88069.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U14405 Genomic DNA. Translation: AAA86681.1.
PIR	S57199.
3D structure databases
HSSP	HSSP built from PDB template 1EUE based on UniProtKB P04166.
ModBase	Search...
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. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

NIA_PHYIN

Accession

Primary (citable) accession number: P39864

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
Last modified:	November 25, 2008
This is version 62 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)