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Protein

Periplasmic nitrate reductase

Gene

napA

Organism
Shewanella sp. (strain W3-18-1)
Status
Unreviewed-Annotation score: 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 annotationSAAS annotation

Cofactori

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi45 – 451Iron-sulfur (4Fe-4S)UniRule annotation
Metal bindingi48 – 481Iron-sulfur (4Fe-4S)UniRule annotation
Metal bindingi52 – 521Iron-sulfur (4Fe-4S)UniRule annotation
Metal bindingi80 – 801Iron-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

OxidoreductaseUniRule annotationSAAS annotation

Keywords - Biological processi

Electron transportUniRule annotationSAAS annotation, Nitrate assimilationUniRule annotationSAAS annotation, Transport

Keywords - Ligandi

4Fe-4SUniRule annotationSAAS annotation, Iron, Iron-sulfur, Metal-binding, MolybdenumUniRule annotationSAAS annotation

Enzyme and pathway databases

BioCyciSSP351745:GCOY-815-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Periplasmic nitrate reductaseUniRule annotation (EC:1.7.99.4UniRule annotation)
Gene namesi
Name:napAUniRule annotation
Ordered Locus Names:Sputw3181_0795Imported
OrganismiShewanella sp. (strain W3-18-1)Imported
Taxonomic identifieri351745 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella
ProteomesiUP000002597: Chromosome

Subcellular locationi

Periplasm UniRule annotation

GO - Cellular componenti

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

Keywords - Cellular componenti

PeriplasmUniRule annotation

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3333 PotentialImportedAdd
BLAST
Signal peptidei1 – 3232Tat-type signalUniRule annotationAdd
BLAST
Chaini34 – 826793 PotentialImportedPRO_5000203760Add
BLAST

Post-translational modificationi

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

Interactioni

Subunit structurei

Interacts with NapB.UniRule annotationSAAS annotation

Protein-protein interaction databases

STRINGi351745.Sputw3181_0795.

Structurei

3D structure databases

ProteinModelPortaliA1RG51.
SMRiA1RG51. Positions 38-825.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini38 – 94574Fe-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
Contains 4Fe-4S Mo/W bis-MGD-type domain.SAAS annotation

Keywords - Domaini

SignalUniRule annotationImported

Phylogenomic databases

eggNOGiCOG0243.
HOGENOMiHOG000031441.
KOiK02567.
OMAiESPVNKG.
OrthoDBiEOG6CVV7G.

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.
IPR010051. Periplasm_NO3_reductase_lsu.
IPR006311. TAT_signal.
IPR019546. TAT_signal_bac_arc.
[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.
TIGR01409. TAT_signal_seq. 1 hit.
PROSITEiPS51669. 4FE4S_MOW_BIS_MGD. 1 hit.
PS51318. TAT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

A1RG51-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSISRREFLK ANAALAAATA VGVTLPVKMV EAAESDNIKW DKAPCRFCGV
60 70 80 90 100
GCSVLVGTKA GKVVATKGDP ESPVNRGLNC IKGYFLSKIM YGKDRLTTPL
110 120 130 140 150
LRMKDGKYHK EGEFTPVSWD VALDTMAAKW KHSIATKGPT SVGMFGSGQW
160 170 180 190 200
TIWEGYAASK LHKAGFLTNN IDPNARHCMA SAVVGFMRTF GIDEPMGCYD
210 220 230 240 250
DLEAADHFVL WGANMAEMHP ILWARLSDRR LSSPSCRVHV LSTFENRSFD
260 270 280 290 300
LADNPMVFHP QSDLVILNYI ANYIIQNKAV NTDFVTKHTQ FALGVDDIGY
310 320 330 340 350
GLRPDHPLEK KAKNPGNGKS TPISFDEYAK FVSTYTLEYA AKMSGVEPEK
360 370 380 390 400
LETLAKAYAD PKVKVMSLWT MGINQHVRGV WANNMLYNLH LLTGKIATPG
410 420 430 440 450
NSPFSLTGQP SACGTAREVG TFAHRLPADM VVDNDKHRAI TEKMWQVPEG
460 470 480 490 500
TIPPKPGYHA VLQSRMLKDG KLNCYWTMCT NNMQAGPNIN EEMYPGFRNP
510 520 530 540 550
ENFIVVSDPY PTVTAMAADL ILPTAMWVEK EGAYGNAERR THMWHQQVKA
560 570 580 590 600
PEGAKSDLWQ LMEFAKRFNV SEVWPAELIA KQPEYADKTL FEVLFANGVI
610 620 630 640 650
NKFPTTDCKA ELNDESQHFG FYVQKGIFEE YAAFGRGHAH DLADFDRYHE
660 670 680 690 700
TRGLRWPVVN GKETLRRFVE GSDPYVKAGE GFKFYGKPDG KAVIFALPYE
710 720 730 740 750
PAAEEPNSEY DLWMSTGRVL EHWHTGSMTA RVPELYRAYP DAQIFMHPED
760 770 780 790 800
AKARGLQRGD EVVVASPRGE VKTRVETKGR NKPPRGVVFM PFFDARQLVN
810 820
KLILDATDPL SKETDFKKCP VKVMKA
Length:826
Mass (Da):92,335
Last modified:February 6, 2007 - v1
Checksum:iEA75ECD77474B12E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000503 Genomic DNA. Translation: ABM23646.1.
RefSeqiYP_962200.1. NC_008750.1.

Genome annotation databases

EnsemblBacteriaiABM23646; ABM23646; Sputw3181_0795.
GeneIDi4659879.
KEGGishw:Sputw3181_0795.
PATRICi23595035. VBISheSp103602_0822.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000503 Genomic DNA. Translation: ABM23646.1.
RefSeqiYP_962200.1. NC_008750.1.

3D structure databases

ProteinModelPortaliA1RG51.
SMRiA1RG51. Positions 38-825.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi351745.Sputw3181_0795.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABM23646; ABM23646; Sputw3181_0795.
GeneIDi4659879.
KEGGishw:Sputw3181_0795.
PATRICi23595035. VBISheSp103602_0822.

Phylogenomic databases

eggNOGiCOG0243.
HOGENOMiHOG000031441.
KOiK02567.
OMAiESPVNKG.
OrthoDBiEOG6CVV7G.

Enzyme and pathway databases

BioCyciSSP351745:GCOY-815-MONOMER.

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.
IPR010051. Periplasm_NO3_reductase_lsu.
IPR006311. TAT_signal.
IPR019546. TAT_signal_bac_arc.
[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.
TIGR01409. TAT_signal_seq. 1 hit.
PROSITEiPS51669. 4FE4S_MOW_BIS_MGD. 1 hit.
PS51318. TAT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: W3-18-1Imported.

Entry informationi

Entry nameiA1RG51_SHESW
AccessioniPrimary (citable) accession number: A1RG51
Entry historyi
Integrated into UniProtKB/TrEMBL: February 6, 2007
Last sequence update: February 6, 2007
Last modified: February 4, 2015
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteomeImported

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.