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Q2S6D5 (Q2S6D5_SALRD) Unreviewed, UniProtKB/TrEMBL

Last modified July 9, 2014. Version 67. 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 attributes

Sequence length957 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Forms oxaloacetate, a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle By similarity. HAMAP-Rule MF_00595

Catalytic activity

Phosphate + oxaloacetate = H2O + phosphoenolpyruvate + HCO3-. HAMAP-Rule MF_00595 SAAS SAAS018129

Cofactor

Magnesium By similarity. HAMAP-Rule MF_00595 SAAS SAAS018129

Subunit structure

Homotetramer By similarity. HAMAP-Rule MF_00595

Sequence similarities

Belongs to the PEPCase type 1 family. HAMAP-Rule MF_00595

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Active site1721 By similarity HAMAP-Rule MF_00595
Active site6071 By similarity HAMAP-Rule MF_00595

Sequences

Sequence LengthMass (Da)Tools
Q2S6D5 [UniParc].

Last modified January 24, 2006. Version 1.
Checksum: 09EDFEE3C6EE3C4E

FASTA957107,032
        10         20         30         40         50         60 
MPRWDDLDLE TEGTGISKPL SRQVNLVGSM LGHIAEEQSG EALFEHVEGL RALCKAAEQE 

        70         80         90        100        110        120 
DAPEKREEAA ERIAALDQDT LERLLHVYTT FFHLVNQAEQ QEIIRINRER ARQSGPSEWP 

       130        140        150        160        170        180 
LGPGDGPGAD GAEPRPQSID AAVADLKAEG YTADEVVAFF RQLDIQPTLT AHPTEARRRS 

       190        200        210        220        230        240 
VLRKEQHIAD LLSTLRRPDA TPDERAETLD RLYSQVAFLL GTDEVRAERP TVREEVEQGH 

       250        260        270        280        290        300 
YFLHGSIWDT IPAIHRDVQQ ALRRHYDATA ELPAFLQYRS WIGSDRDGNP NVTADVTRWT 

       310        320        330        340        350        360 
VARQRRTTLE HYLDEIDELR DDLSISTRQL TVSDALEASL EADAEEIALP DDVRRQYQRE 

       370        380        390        400        410        420 
PYRLKLCYIE ERLRGLLDRI DATDVAAMAG AYAADDLLAD LDLIAESLQG HGFEDAAQSG 

       430        440        450        460        470        480 
QLHRLRSLVK TFGFHLAALD VRQHSRVHED TVAALLDAGD VVDDYGALSE EEKLEVLSRE 

       490        500        510        520        530        540 
LQNPRPLVSR HADLPADAAE LMEVFGVLRA MHAVDPDIVG SYVVSMTHTV SDLLEPMLLA 

       550        560        570        580        590        600 
KEAGLGAVVD GSYRCPLDVV PLFETIEDLD AADDRMETLF THPVYAAQLE GRDGFQEIML 

       610        620        630        640        650        660 
GYSDSNKDGG YWMANWALHK AIHALGVVCD EHDVDLRLFH GRGGTVGRGG GHTSQAIRAL 

       670        680        690        700        710        720 
PPVVHNGRIR MTEQGEIISF RYALPDIARR HVEQIVNATL TATARAQNTP APENPLLADK 

       730        740        750        760        770        780 
VSMESDVVAL MDRLAEEGMS AYREFIDDPE GWQWYTAATP IEHISRLPIA SRPVSRASEG 

       790        800        810        820        830        840 
EQVEFENLRA IPWVFAWTQT RYIAPGWYGT GQGLATLLEN EPDARDTLRD LYENWPFFRT 

       850        860        870        880        890        900 
VLDSAQREMA RARLPIAERY DALAEVETSF HAPIVDDYER AESAILEITD QAALFDGNPV 

       910        920        930        940        950 
LKKSIELRNP YTDVLNLIQI ELLKRYRAST DDAEQEALRE AIFLSINGVA AAMQSTG 

« Hide

References

[1]"The genome of Salinibacter ruber: convergence and gene exchange among hyperhalophilic bacteria and archaea."
Mongodin E.F., Nelson K.E., Daugherty S., Deboy R.T., Wister J., Khouri H., Weidman J., Walsh D.A., Papke R.T., Sanchez Perez G., Sharma A.K., Nesbo C.L., MacLeod D., Bapteste E., Doolittle W.F., Charlebois R.L., Legault B., Rodriguez-Valera F.
Proc. Natl. Acad. Sci. U.S.A. 102:18147-18152(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 13855 / M31.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000159 Genomic DNA. Translation: ABC43864.1.
RefSeqYP_444246.1. NC_007677.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING309807.SRU_0093.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABC43864; ABC43864; SRU_0093.
GeneID3851345.
KEGGsru:SRU_0093.
PATRIC23422501. VBISalRub86502_0102.

Phylogenomic databases

eggNOGCOG2352.
HOGENOMHOG000238647.
KOK01595.
OMAISCQHYR.
OrthoDBEOG6TJ7T8.
PhylomeDBQ2S6D5.

Enzyme and pathway databases

BioCycSRUB309807:GJJD-93-MONOMER.

Family and domain databases

HAMAPMF_00595. PEPcase_type1.
InterProIPR021135. PEP_COase.
IPR018129. PEP_COase_AS.
IPR022805. PEP_COase_bac/pln-type.
IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
[Graphical view]
PfamPF00311. PEPcase. 1 hit.
[Graphical view]
PRINTSPR00150. PEPCARBXLASE.
SUPFAMSSF51621. SSF51621. 1 hit.
PROSITEPS00781. PEPCASE_1. 1 hit.
PS00393. PEPCASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameQ2S6D5_SALRD
AccessionPrimary (citable) accession number: Q2S6D5
Entry history
Integrated into UniProtKB/TrEMBL: January 24, 2006
Last sequence update: January 24, 2006
Last modified: July 9, 2014
This is version 67 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)