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A1RG51 (A1RG51_SHESW) Unreviewed, UniProtKB/TrEMBL

Last modified June 11, 2014. Version 61. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Periplasmic nitrate reductase HAMAP-Rule MF_01630

EC=1.7.99.4 HAMAP-Rule MF_01630
Gene names
Name:napA HAMAP-Rule MF_01630
Ordered Locus Names:Sputw3181_0795 EMBL ABM23646.1
OrganismShewanella sp. (strain W3-18-1) [Complete proteome] [HAMAP] EMBL ABM23646.1
Taxonomic identifier351745 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella

Protein attributes

Sequence length826 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred 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. SAAS SAAS010051 HAMAP-Rule MF_01630

Cofactor

Binds 1 4Fe-4S cluster By similarity. SAAS SAAS010051 HAMAP-Rule MF_01630

Binds 1 molybdenum-bis(molybdopterin guanine dinucleotide) (Mo-bis-MGD) cofactor per subunit By similarity. HAMAP-Rule MF_01630 SAAS SAAS010051

Subunit structure

Interacts with NapB By similarity. HAMAP-Rule MF_01630 SAAS SAAS019546

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 By similarity. HAMAP-Rule MF_01630

Sequence similarities

Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. NasA/NapA/NarB subfamily. HAMAP-Rule MF_01630

Contains 1 4Fe-4S Mo/W bis-MGD-type domain. HAMAP-Rule MF_01630

Contains 4Fe-4S Mo/W bis-MGD-type domain. SAAS SAAS010051

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3333 Potential EMBL ABM23646.1
Signal peptide1 – 3232Tat-type signal By similarity HAMAP-Rule MF_01630
Chain34 – 826793 Potential EMBL ABM23646.1
PRO_5000203760

Regions

Domain38 – 94574Fe-4S Mo/W bis-MGD-type By similarity HAMAP-Rule MF_01630

Sites

Metal binding451Iron-sulfur (4Fe-4S) By similarity HAMAP-Rule MF_01630
Metal binding481Iron-sulfur (4Fe-4S) By similarity HAMAP-Rule MF_01630
Metal binding521Iron-sulfur (4Fe-4S) By similarity HAMAP-Rule MF_01630
Metal binding801Iron-sulfur (4Fe-4S) By similarity HAMAP-Rule MF_01630

Sequences

Sequence LengthMass (Da)Tools
A1RG51 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: EA75ECD77474B12E

FASTA82692,335
        10         20         30         40         50         60 
MSISRREFLK ANAALAAATA VGVTLPVKMV EAAESDNIKW DKAPCRFCGV GCSVLVGTKA 

        70         80         90        100        110        120 
GKVVATKGDP ESPVNRGLNC IKGYFLSKIM YGKDRLTTPL LRMKDGKYHK EGEFTPVSWD 

       130        140        150        160        170        180 
VALDTMAAKW KHSIATKGPT SVGMFGSGQW TIWEGYAASK LHKAGFLTNN IDPNARHCMA 

       190        200        210        220        230        240 
SAVVGFMRTF GIDEPMGCYD DLEAADHFVL WGANMAEMHP ILWARLSDRR LSSPSCRVHV 

       250        260        270        280        290        300 
LSTFENRSFD LADNPMVFHP QSDLVILNYI ANYIIQNKAV NTDFVTKHTQ FALGVDDIGY 

       310        320        330        340        350        360 
GLRPDHPLEK KAKNPGNGKS TPISFDEYAK FVSTYTLEYA AKMSGVEPEK LETLAKAYAD 

       370        380        390        400        410        420 
PKVKVMSLWT MGINQHVRGV WANNMLYNLH LLTGKIATPG NSPFSLTGQP SACGTAREVG 

       430        440        450        460        470        480 
TFAHRLPADM VVDNDKHRAI TEKMWQVPEG TIPPKPGYHA VLQSRMLKDG KLNCYWTMCT 

       490        500        510        520        530        540 
NNMQAGPNIN EEMYPGFRNP ENFIVVSDPY PTVTAMAADL ILPTAMWVEK EGAYGNAERR 

       550        560        570        580        590        600 
THMWHQQVKA PEGAKSDLWQ LMEFAKRFNV SEVWPAELIA KQPEYADKTL FEVLFANGVI 

       610        620        630        640        650        660 
NKFPTTDCKA ELNDESQHFG FYVQKGIFEE YAAFGRGHAH DLADFDRYHE TRGLRWPVVN 

       670        680        690        700        710        720 
GKETLRRFVE GSDPYVKAGE GFKFYGKPDG KAVIFALPYE PAAEEPNSEY DLWMSTGRVL 

       730        740        750        760        770        780 
EHWHTGSMTA RVPELYRAYP DAQIFMHPED AKARGLQRGD EVVVASPRGE VKTRVETKGR 

       790        800        810        820 
NKPPRGVVFM PFFDARQLVN KLILDATDPL SKETDFKKCP VKVMKA 

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References

[1]"Complete sequence of Shewanella sp. W3-18-1."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Lykidis A., Tiedje J., Richardson P.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: W3-18-1 EMBL ABM23646.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000503 Genomic DNA. Translation: ABM23646.1.
RefSeqYP_962200.1. NC_008750.1.

3D structure databases

ProteinModelPortalA1RG51.
SMRA1RG51. Positions 38-825.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING351745.Sputw3181_0795.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABM23646; ABM23646; Sputw3181_0795.
GeneID4659879.
KEGGshw:Sputw3181_0795.
PATRIC23595035. VBISheSp103602_0822.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0243.
HOGENOMHOG000031441.
KOK02567.
OMARRLSHKD.
OrthoDBEOG6CVV7G.

Enzyme and pathway databases

BioCycSSP351745:GCOY-815-MONOMER.

Family and domain databases

HAMAPMF_01630. Nitrate_reduct.
InterProIPR009010. 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]
PfamPF04879. Molybdop_Fe4S4. 1 hit.
PF00384. Molybdopterin. 1 hit.
PF01568. Molydop_binding. 1 hit.
[Graphical view]
SMARTSM00926. Molybdop_Fe4S4. 1 hit.
[Graphical view]
SUPFAMSSF50692. SSF50692. 1 hit.
TIGRFAMsTIGR01706. NAPA. 1 hit.
TIGR01409. TAT_signal_seq. 1 hit.
PROSITEPS51669. 4FE4S_MOW_BIS_MGD. 1 hit.
PS51318. TAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameA1RG51_SHESW
AccessionPrimary (citable) accession number: A1RG51
Entry history
Integrated into UniProtKB/TrEMBL: February 6, 2007
Last sequence update: February 6, 2007
Last modified: June 11, 2014
This is version 61 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)