Reviewed, UniProtKB/Swiss-Prot Q3HS05 (NAPA_PSEST)

Names and origin

Protein names

Recommended name:
    Periplasmic nitrate reductase
    EC=1.7.99.4

Gene names

Name:

napA

Organism

Pseudomonas stutzeri (Pseudomonas perfectomarina)

Taxonomic identifier

316 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas

Protein attributes

Sequence length	834 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Catalytic subunit of the periplasmic nitrate reductase (NAP). Only expressed at high levels during aerobic growth. NapAB complex receives electrons from the membrane-anchored tetraheme protein napC, thus allowing electron flow between membrane and periplasm. Essential function for nitrate assimilation and may have a role in anaerobic metabolism By similarity.
Catalytic activity	Nitrite + acceptor = nitrate + reduced acceptor.
Cofactor	Binds 1 4Fe-4S cluster By similarity. Binds 1 molybdenum ion per subunit By similarity. Binds 2 molybdopterin guanine dinucleotide (MGD) groups per subunit By similarity.
Subunit structure	Interacts with napB By similarity.
Subcellular location	PeriplasmBy similarity.
Post-translational modification	Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven.
Sequence similarities	Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. NasA/napA/narB subfamily.

Ontologies

Keywords
Biological process	Electron transport Nitrate assimilation Transport
Cellular component	Periplasm
Domain	Signal
Ligand	4Fe-4S Iron Iron-sulfur Metal-binding Molybdenum
Molecular function	Oxidoreductase
Gene Ontology (GO)
Biological process	Mo-molybdopterin cofactor biosynthetic process Inferred from electronic annotation. Source: HAMAP electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW nitrate assimilation Inferred from electronic annotation. Source: HAMAP transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	periplasmic space Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: InterPro electron carrier activity Inferred from electronic annotation. Source: HAMAP iron ion binding Inferred from electronic annotation. Source: HAMAP molybdenum ion binding Inferred from electronic annotation. Source: InterPro nitrate reductase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 29	29	Tat-type signal Potential
	Chain	30 – 834	805	Periplasmic nitrate reductase		PRO_0000045996
Sites
	Metal binding	48	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	51	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	55	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	83	1	Iron-sulfur (4Fe-4S) By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q3HS05-1 [UniParc]. Last modified November 8, 2005. Version 1. Checksum: 7621B1EF0FDE3B4D	FASTA	834	93,752
	10 20 30 40 50 60 MSLTRRQFAK ANAAAIAATV AGMPIASTAS NLVTEADATN LKWDKAPCRF CGTGCGVMVA 70 80 90 100 110 120 TRENRVVATH GDVKADVNRG INCVKGYFLS KIMYGTDRLT QPLLRMKDGK FDKQGEFQPV 130 140 150 160 170 180 TWDQAFDIME EKYKAALKAG GPEAIGMFGS GQWTIWEGYA ANKLMKAGFR SNNIDPNARH 190 200 210 220 230 240 CMASAAFGFM RTFGMDEPMG CYEDIEAADA FVLWGSNMAE MHPVLWTRLT DRRLSAPHVK 250 260 270 280 290 300 VAVMSTFEHR SFELADIPMI FNPQTDLVIL NYIANHIIQS GAVNKEFIDK HTRFAKGATN 310 320 330 340 350 360 IGYGLRPTDP LELKAENAAV ANTWTDIGYE DYVEFLKPYT LEHAAKESGV PAERLKALAE 370 380 390 400 410 420 LYADPKVKVM SFWTMGFNQH TRGVWANNMI YNIHLLTGKI SEPGNSPFSL TGQPSACGTA 430 440 450 460 470 480 REVGTFSHRL PADMAVTNPK HRAITEKIWK LPEGTIQEKP GFHAVDQSRK LKDGVLKVYW 490 500 510 520 530 540 TQVTNNMQAG PNVMQEILPG WRNPETFVIV SDVYPTVSAQ AADLILPSAM WVEKEGAYGN 550 560 570 580 590 600 AERRTQFWHQ LVTAPGEARS DLWQLVEFSK RFRVDEVWPA ELLSKAPEFK DKTLFDVLFK 610 620 630 640 650 660 NGQVDRFSND EIAEGYANYE AEAFGFYLQK GLFEEYAEFG RGHAHDLAAF DVYHRERGLR 670 680 690 700 710 720 WPVVDEKETQ WRYREGYDPY VEAGSGVQFY GNADKKAIIF ALPYEVPAEV PDEEYPFWLS 730 740 750 760 770 780 TGRVLEHWHT GSMTQRVDEL HKAVPDALVY MHPEDARKLN VRRGSVVKIV SRRGEMQGRV 790 800 810 820 830 ETRGRNKPPM GLVYVPFFDA NKLINKVTLD ATDPISKQTD FKKCAVKIEV VSIA

References

[1]	"Nitrate reduction in Pseudomonas stutzeri A15 and its contribution to rice and wheat rhizosphere fitness." Rediers H., Vanderleyden J., De Mot R. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: A15.

Cross-references

Sequence databases
EMBLGenBankDDBJ	DQ200356 Genomic DNA. Translation: ABA42173.1.
3D structure databases
SMR	Q3HS05. Positions 41-829.
ModBase	Search...
Family and domain databases
HAMAP	MF_01630. [Tree]
InterPro	IPR009010. Asp_de-COase-like_fold. IPR006656. Mopterin_OxRdtase. IPR006963. Mopterin_OxRdtase_Fe4S4. IPR006655. Mopterin_OxRdtase_prok_CS. IPR006657. MPT_dinuc_bd. IPR010051. NO3_reductase_lsu_periplasm. IPR006311. Tat. [Graphical view]
Gene3D	G3DSA:2.40.40.20. Asp_decarboxylase-like_fold. 1 hit.
Pfam	PF04879. Molybdop_Fe4S4. 1 hit. PF00384. Molybdopterin. 1 hit. PF01568. Molydop_binding. 1 hit. [Graphical view]
TIGRFAMs	TIGR01706. NAPA. 1 hit. TIGR01409. TAT_signal_seq. 1 hit.
PROSITE	PS00551. MOLYBDOPTERIN_PROK_1. 1 hit. PS00490. MOLYBDOPTERIN_PROK_2. False negative. PS00932. MOLYBDOPTERIN_PROK_3. False negative. PS51318. TAT. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

NAPA_PSEST

Accession

Primary (citable) accession number: Q3HS05

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 7, 2006
Last sequence update:	November 8, 2005
Last modified:	November 25, 2008
This is version 22 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)