Reviewed, UniProtKB/Swiss-Prot A5EZX9 (NAPA_VIBC3)

Names and origin

Protein names

Recommended name:
    Periplasmic nitrate reductase
    EC=1.7.99.4

Gene names

Name:	napA
Ordered Locus Names:	VC0395_0617

Organism

Vibrio cholerae serotype O1 (strain ATCC 39541 / Ogawa 395 / O395) [Complete proteome] [HAMAP]

Taxonomic identifier

345073 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Vibrionales › Vibrionaceae › Vibrio

Protein attributes

Sequence length	829 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 – 29	29	Tat-type signal Potential
	Chain	30 – 829	800	Periplasmic nitrate reductase		PRO_1000073642
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)
	A5EZX9-1 [UniParc]. Last modified June 12, 2007. Version 1. Checksum: 6B9BEE7A10D99975	FASTA	829	93,106
	10 20 30 40 50 60 MKMTRRAFVK ANAAASAAAV AGITLPASAT NLIASSDQTA IHWDKAPCRF CGTGCSVLVG 70 80 90 100 110 120 TQDGRVVATQ GDPEAPVNKG LNCIKGYFLS KIMYGQDRLK TPLLRMKDGQ YHKDGEFTPV 130 140 150 160 170 180 SWDTAFDVMA EKWKASLKTK GPTSVGMFGS GQWTVMEGYA AVKLMKAGFR SNNIDPNARH 190 200 210 220 230 240 CMASAVVGFM RTFGIDEPMG CYDDFEHADA FVLWGSNMAE MHPVLWTRIT DRRLSHPHVK 250 260 270 280 290 300 VNVLSTYYHR SFELADHGYI FHPQSDLAIA NFIANYIIQN DAVNWDFVNK HTHFKQAVTD 310 320 330 340 350 360 IGYGLRDDHP LQKKAKNANS GDVSDISFEE YKKSVAPYTV EKASEISGVS PDKLITLAKQ 370 380 390 400 410 420 YADPNTKVMS LWTMGMNQHT RGVWMQSLVY NLHLLTGKIA TPGNSPFSLT GQPSACGTAR 430 440 450 460 470 480 EVGTFAHRLP ADMVVANPKH RAIAEKVWKL PEGTIPEKPG FHAVQQDRML KDGVLNCYWV 490 500 510 520 530 540 QCNNNMQAGP NINEERLPGY RNPENFIVVS DAYPTVTAQA ADLVLPTAMW VEKEGAYGNA 550 560 570 580 590 600 ERRTQVWYQQ VKTVGESHSD SWQVIEFSKR FKVEDVWPEE LLAKAPQYRG KTLYDVLFKN 610 620 630 640 650 660 GQVDKFPLSE ARELNDDAHH FGFYIQKGLF EEYAEFGRGH GHDLAPYDVY HQVRGLRWPV 670 680 690 700 710 720 VDGKETKWRF KEGSDPYAKA GSGWDFYGKP DGKAWIISSP YEAPPEMPNE EYDLWLCTGR 730 740 750 760 770 780 VLEHWHTGTM TRRVPELYKA VPDALCFMHH EDAQARGLRR GDEVLISNSR GEVRVRVETR 790 800 810 820 GRNKPPKGLV FVPFFDARIL VNKLILDATD PLSKQTDFKK CPVKITKVA

References

[1]	Heidelberg J. Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000626 Genomic DNA. Translation: ABQ18717.1.
RefSeq	YP_001215456.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	5134168.
GenomeReviews	Gene locus VC0395_0617 in contig CP000626_GR.
KEGG	vco:VC0395_0617.
Organism-specific databases
CMR	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_VIBC3

Accession

Primary (citable) accession number: A5EZX9

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 26, 2008
Last sequence update:	June 12, 2007
Last modified:	November 25, 2008
This is version 15 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)