Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

A5EZX9

- NAPA_VIBC3

UniProt

A5EZX9 - NAPA_VIBC3

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Periplasmic nitrate reductase

Gene

napA

Organism
Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 / O395)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi

Functioni

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.UniRule annotation

Catalytic activityi

Nitrite + acceptor = nitrate + reduced acceptor.UniRule annotation

Cofactori

Protein has several cofactor binding sites:
  • [4Fe-4S] clusterUniRule annotationNote: Binds 1 [4Fe-4S] cluster.UniRule annotation
  • Mo-bis(molybdopterin guanine dinucleotide)UniRule annotationNote: Binds 1 molybdenum-bis(molybdopterin guanine dinucleotide) (Mo-bis-MGD) cofactor per subunit.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi48 – 481Iron-sulfur (4Fe-4S)UniRule annotation
Metal bindingi51 – 511Iron-sulfur (4Fe-4S)UniRule annotation
Metal bindingi55 – 551Iron-sulfur (4Fe-4S)UniRule annotation
Metal bindingi83 – 831Iron-sulfur (4Fe-4S)UniRule annotation

GO - Molecular functioni

  1. 4 iron, 4 sulfur cluster binding Source: UniProtKB-HAMAP
  2. electron carrier activity Source: UniProtKB-HAMAP
  3. iron ion binding Source: UniProtKB-HAMAP
  4. molybdenum ion binding Source: InterPro
  5. nitrate reductase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. Mo-molybdopterin cofactor biosynthetic process Source: UniProtKB-HAMAP
  2. nitrate assimilation Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Electron transport, Nitrate assimilation, Transport

Keywords - Ligandi

4Fe-4S, Iron, Iron-sulfur, Metal-binding, Molybdenum

Names & Taxonomyi

Protein namesi
Recommended name:
Periplasmic nitrate reductaseUniRule annotation (EC:1.7.99.4UniRule annotation)
Gene namesi
Name:napAUniRule annotation
Ordered Locus Names:VC0395_0617, VC395_A0634
OrganismiVibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 / O395)
Taxonomic identifieri345073 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio
ProteomesiUP000000249: Chromosome 1, UP000001630: Chromosome II

Subcellular locationi

Periplasm UniRule annotation

GO - Cellular componenti

  1. periplasmic space Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Cellular componenti

Periplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2929Tat-type signalUniRule annotationAdd
BLAST
Chaini30 – 829800Periplasmic nitrate reductasePRO_1000073642Add
BLAST

Post-translational modificationi

Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven.

Interactioni

Subunit structurei

Interacts with NapB.UniRule annotation

Protein-protein interaction databases

STRINGi345073.VC0395_0617.

Structurei

3D structure databases

ProteinModelPortaliA5EZX9.
SMRiA5EZX9. Positions 40-827.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini41 – 97574Fe-4S Mo/W bis-MGD-typeUniRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. NasA/NapA/NarB subfamily.UniRule annotation
Contains 1 4Fe-4S Mo/W bis-MGD-type domain.UniRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG0243.
HOGENOMiHOG000031441.
KOiK02567.
OMAiAGKMHDS.

Family and domain databases

HAMAPiMF_01630. Nitrate_reduct.
InterProiIPR009010. 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]
PfamiPF04879. Molybdop_Fe4S4. 1 hit.
PF00384. Molybdopterin. 1 hit.
PF01568. Molydop_binding. 1 hit.
[Graphical view]
SMARTiSM00926. Molybdop_Fe4S4. 1 hit.
[Graphical view]
SUPFAMiSSF50692. SSF50692. 1 hit.
TIGRFAMsiTIGR01706. NAPA. 1 hit.
PROSITEiPS51669. 4FE4S_MOW_BIS_MGD. 1 hit.
PS00551. MOLYBDOPTERIN_PROK_1. 1 hit.
PS51318. TAT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

A5EZX9-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKMTRRAFVK ANAAASAAAV AGITLPASAT NLIASSDQTA IHWDKAPCRF
60 70 80 90 100
CGTGCSVLVG TQDGRVVATQ GDPEAPVNKG LNCIKGYFLS KIMYGQDRLK
110 120 130 140 150
TPLLRMKDGQ YHKDGEFTPV SWDTAFDVMA EKWKASLKTK GPTSVGMFGS
160 170 180 190 200
GQWTVMEGYA AVKLMKAGFR SNNIDPNARH CMASAVVGFM RTFGIDEPMG
210 220 230 240 250
CYDDFEHADA FVLWGSNMAE MHPVLWTRIT DRRLSHPHVK VNVLSTYYHR
260 270 280 290 300
SFELADHGYI FHPQSDLAIA NFIANYIIQN DAVNWDFVNK HTHFKQAVTD
310 320 330 340 350
IGYGLRDDHP LQKKAKNANS GDVSDISFEE YKKSVAPYTV EKASEISGVS
360 370 380 390 400
PDKLITLAKQ YADPNTKVMS LWTMGMNQHT RGVWMQSLVY NLHLLTGKIA
410 420 430 440 450
TPGNSPFSLT GQPSACGTAR EVGTFAHRLP ADMVVANPKH RAIAEKVWKL
460 470 480 490 500
PEGTIPEKPG FHAVQQDRML KDGVLNCYWV QCNNNMQAGP NINEERLPGY
510 520 530 540 550
RNPENFIVVS DAYPTVTAQA ADLVLPTAMW VEKEGAYGNA ERRTQVWYQQ
560 570 580 590 600
VKTVGESHSD SWQVIEFSKR FKVEDVWPEE LLAKAPQYRG KTLYDVLFKN
610 620 630 640 650
GQVDKFPLSE ARELNDDAHH FGFYIQKGLF EEYAEFGRGH GHDLAPYDVY
660 670 680 690 700
HQVRGLRWPV VDGKETKWRF KEGSDPYAKA GSGWDFYGKP DGKAWIISSP
710 720 730 740 750
YEAPPEMPNE EYDLWLCTGR VLEHWHTGTM TRRVPELYKA VPDALCFMHH
760 770 780 790 800
EDAQARGLRR GDEVLISNSR GEVRVRVETR GRNKPPKGLV FVPFFDARIL
810 820
VNKLILDATD PLSKQTDFKK CPVKITKVA
Length:829
Mass (Da):93,106
Last modified:June 12, 2007 - v1
Checksum:i6B9BEE7A10D99975
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000626 Genomic DNA. Translation: ABQ18717.1.
CP001236 Genomic DNA. Translation: ACP11468.1.
RefSeqiYP_001215456.1. NC_009456.1.
YP_002821704.1. NC_012583.1.

Genome annotation databases

EnsemblBacteriaiABQ18717; ABQ18717; VC0395_0617.
ACP11468; ACP11468; VC395_A0634.
GeneIDi5134168.
7777698.
KEGGivco:VC0395_0617.
vcr:VC395_A0634.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000626 Genomic DNA. Translation: ABQ18717.1 .
CP001236 Genomic DNA. Translation: ACP11468.1 .
RefSeqi YP_001215456.1. NC_009456.1.
YP_002821704.1. NC_012583.1.

3D structure databases

ProteinModelPortali A5EZX9.
SMRi A5EZX9. Positions 40-827.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 345073.VC0395_0617.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABQ18717 ; ABQ18717 ; VC0395_0617 .
ACP11468 ; ACP11468 ; VC395_A0634 .
GeneIDi 5134168.
7777698.
KEGGi vco:VC0395_0617.
vcr:VC395_A0634.

Phylogenomic databases

eggNOGi COG0243.
HOGENOMi HOG000031441.
KOi K02567.
OMAi AGKMHDS.

Family and domain databases

HAMAPi MF_01630. Nitrate_reduct.
InterProi 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 ]
Pfami PF04879. Molybdop_Fe4S4. 1 hit.
PF00384. Molybdopterin. 1 hit.
PF01568. Molydop_binding. 1 hit.
[Graphical view ]
SMARTi SM00926. Molybdop_Fe4S4. 1 hit.
[Graphical view ]
SUPFAMi SSF50692. SSF50692. 1 hit.
TIGRFAMsi TIGR01706. NAPA. 1 hit.
PROSITEi PS51669. 4FE4S_MOW_BIS_MGD. 1 hit.
PS00551. MOLYBDOPTERIN_PROK_1. 1 hit.
PS51318. TAT. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. Heidelberg J.
    Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 39541 / Classical Ogawa 395 / O395.
  2. "A recalibrated molecular clock and independent origins for the cholera pandemic clones."
    Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J., Wang W., Wang J., Qian W., Li D., Wang L.
    PLoS ONE 3:E4053-E4053(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 39541 / Classical Ogawa 395 / O395.

Entry informationi

Entry nameiNAPA_VIBC3
AccessioniPrimary (citable) accession number: A5EZX9
Secondary accession number(s): C3M5Q5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: June 12, 2007
Last modified: November 26, 2014
This is version 55 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3