Q9KLR4 (NAPA_VIBCH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Periplasmic nitrate reductase
EC=1.7.99.4

Gene names

Name:	napA
Ordered Locus Names:	VC_A0678

Organism

Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961) [Reference proteome] [HAMAP]

Taxonomic identifier

243277 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Vibrionales › Vibrionaceae › Vibrio › Vibrio cholerae › Vibrio cholerae O1 › Vibrio cholerae O1 biovar El Tor

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. HAMAP-Rule MF_01630
Catalytic activity	Nitrite + acceptor = nitrate + reduced acceptor. HAMAP-Rule MF_01630
Cofactor	Binds 1 4Fe-4S cluster By similarity. HAMAP-Rule MF_01630 Binds 1 molybdenum ion per subunit By similarity. HAMAP-Rule MF_01630 Binds 2 molybdopterin guanine dinucleotide (MGD) groups per subunit By similarity.
Subunit structure	Interacts with NapB By similarity. HAMAP-Rule MF_01630
Subcellular location	Periplasm By similarity HAMAP-Rule MF_01630.
Post-translational modification	Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven. HAMAP-Rule MF_01630
Sequence similarities	Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. NasA/NapA/NarB subfamily. Contains 1 4Fe-4S Mo/W bis-MGD-type domain.

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 Reference 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
Cellular_component	nitrate reductase complex Inferred from sequence or structural similarity Ref.1. Source: TIGR periplasmic space Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW 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 sequence or structural similarity Ref.1. Source: TIGR
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 HAMAP-Rule MF_01630		PRO_0000046009
Regions
	Domain	41 – 97	57	4Fe-4S Mo/W bis-MGD-type
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)
	Q9KLR4 [UniParc]. Last modified October 1, 2000. 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]

"DNA sequence of both chromosomes of the cholera pathogen Vibrio cholerae." Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L., Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R., Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D., Vamathevan J.J., Bass S. , Qin H., Dragoi I., Sellers P., McDonald L.A., Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L., Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M. Nature 406:477-483(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 39315 / El Tor Inaba N16961.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE003853 Genomic DNA. Translation: AAF96578.1.
PIR	D82430.
RefSeq	NP_233066.1. NC_002506.1.
3D structure databases
ProteinModelPortal	Q9KLR4.
SMR	Q9KLR4. Positions 40-827.
ModBase	Search...
Protein-protein interaction databases
STRING	243277.VCA0678.
Protocols and materials databases
DNASU	2612423.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAF96578; AAF96578; VC_A0678.
GeneID	2612423.
KEGG	vch:VCA0678.
PATRIC	20085904. VBIVibCho83274_3302.
Phylogenomic databases
eggNOG	COG0243.
KO	K02567.
OMA	IISAPYE.
ProtClustDB	PRK13532.
Family and domain databases
Gene3D	2.40.40.20. 1 hit.
HAMAP	MF_01630. Nitrate_reduct.
InterPro	IPR009010. Asp_de-COase-like_dom. IPR006657. MoPterin_dinucl-bd_dom. IPR006656. Mopterin_OxRdtase. IPR006963. Mopterin_OxRdtase_4Fe-4S_dom. IPR027467. MopterinOxRdtase_cofactor_BS. IPR010051. Periplasm_NO3_reductase_lsu. IPR006311. TAT_signal. [Graphical view]
Pfam	PF04879. Molybdop_Fe4S4. 1 hit. PF00384. Molybdopterin. 1 hit. PF01568. Molydop_binding. 1 hit. [Graphical view]
SMART	SM00926. Molybdop_Fe4S4. 1 hit. [Graphical view]
SUPFAM	SSF50692. Asp_decarb_fold. 1 hit.
TIGRFAMs	TIGR01706. NAPA. 1 hit.
PROSITE	PS51669. 4FE4S_MOW_BIS_MGD. 1 hit. 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_VIBCH

Accession

Primary (citable) accession number: Q9KLR4

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 7, 2006
Last sequence update:	October 1, 2000
Last modified:	May 29, 2013
This is version 77 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program