Reviewed, UniProtKB/Swiss-Prot A9N5G2 (NAPA_SALPB)

Names and origin

Protein names

Recommended name:
    Periplasmic nitrate reductase
    EC=1.7.99.4

Gene names

Name:	napA
Ordered Locus Names:	SPAB_00733

Organism

Salmonella paratyphi B (strain ATCC BAA-1250 / SPB7) [Complete proteome] [HAMAP]

Taxonomic identifier

272994 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella › Salmonella enterica subsp. enterica serovar Paratyphi B

Protein attributes

Sequence length	828 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
Technical term	Complete proteome
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 – 31	31	Tat-type signal Potential
	Chain	32 – 828	797	Periplasmic nitrate reductase		PRO_1000088119
Sites
	Metal binding	46	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	49	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	53	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	81	1	Iron-sulfur (4Fe-4S) By similarity

Sequences

	Sequence		Length	Mass (Da)
	A9N5G2-1 [UniParc]. Last modified February 5, 2008. Version 1. Checksum: 81739A3FECE5D836	FASTA	828	92,858
	10 20 30 40 50 60 MKLSRRSFMK ANAVAAAAAA AGLSVPGVAR AVVGQQEAIK WDKAPCRFCG TGCGVLVGTQ 70 80 90 100 110 120 QGRVVACQGD PDAPVNRGLN CIKGYFLPKI MYGKDRLTQP MLRMKDGSYH KDGEFTPVSW 130 140 150 160 170 180 EQAFDVMEEK FKTALKEKGP EAIGMFGSGQ WTIWEGYAAA KLFKAGFRSN NIDPNARHCM 190 200 210 220 230 240 ASAVVGFMRT FGMDEPMGCY DDIEQADAFV LWGSNMAEMH PILWSRITNR RLSDPNVKVA 250 260 270 280 290 300 VLSTFQHRSF ELADNGIVFT PQSDLVILNY IANYIIQNNA VNQDFFTKHV NLRKGATDIG 310 320 330 340 350 360 YGLRPTHPLE KAAKNPGSDA SEPMSFDEYK AFVAEYTLDK TAEMTGVPKD QLEQLAQLYA 370 380 390 400 410 420 DPNKRVISYW TMGFNQHTRG VWANNLVYNL HLLTGKISQP GCGPFSLTGQ PSACGTAREV 430 440 450 460 470 480 GTFSHRLPAD MVVTNEKHRD ICEKHWQIPA GTIPAKVGLH AVAQDRALKD GKLNVYWVMC 490 500 510 520 530 540 NNNMQAGPNI NEDRMPGWRD PRNFIIVSDP YPTVSALSAD LILPTAMWVE KEGAYGNAER 550 560 570 580 590 600 RTQFWRQQIK APGEAKSDLW QLVQFSRRFK TEEVWPEALL AQKPELRGKT LYDVLFATPA 610 620 630 640 650 660 VSKFPLSELK EDQLNDESRE LGFYLQKGLF EEYAWFGRGH GHDLAPFDDY HNARGLRWPV 670 680 690 700 710 720 VEGKETQWRY SEGNDPYVKA GEGYKFYGKP DGKAVIFALP FEPAAESPDN EYDLWLSTGR 730 740 750 760 770 780 VLEHWHTGSM TRRVPELHRA FPEAVVFIHP LDAKARDLRR GDKVKVSSRR GEVISIVETR 790 800 810 820 GRNRPPQGLV YMPFFDAAQL VNNLTLDATD PLSKETDFKK CAVKLAKV

References

[1]	McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S., Fulton R., Cordes M., Wollam A., Shah N., Pepin K., Bhonagiri V., Nash W., Johnson M., Thiruvilangam P., Wilson R. Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000886 Genomic DNA. Translation: ABX66158.1.
RefSeq	YP_001586991.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	5781787.
GenomeReviews	Gene locus SPAB_00733 in contig CP000886_GR.
KEGG	spq:SPAB_00733.
Organism-specific databases
CMR	Search...
Family and domain databases
HAMAP	MF_01630. [Tree]
InterPro	IPR009010. Asp_de-COase-like_fold. IPR006655. Mopterin_OxRdtase_prok_CS. IPR010051. NO3_reductase_lsu_periplasm. IPR006311. Tat. [Graphical view]
Gene3D	G3DSA:2.40.40.20. Asp_decarboxylase-like_fold. 1 hit.
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_SALPB

Accession

Primary (citable) accession number: A9N5G2

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 20, 2008
Last sequence update:	February 5, 2008
Last modified:	November 25, 2008
This is version 9 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)