Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

C0MHJ2 (C0MHJ2_STRS7) Unreviewed, UniProtKB/TrEMBL

Last modified June 11, 2014. Version 37. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein attributes

Sequence length927 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 SAAS SAAS021135

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 site1381 By similarity HAMAP-Rule MF_00595
Active site5901 By similarity HAMAP-Rule MF_00595

Sequences

Sequence LengthMass (Da)Tools
C0MHJ2 [UniParc].

Last modified May 5, 2009. Version 1.
Checksum: E2D3E8B7EFDFFB8F

FASTA927105,120
        10         20         30         40         50         60 
MSVKKLESYN NQEIIAEEVA ILKEILESIT RRMIGDEAFA RIEEIIDLSE KQDYVLLEQL 

        70         80         90        100        110        120 
IAGISNKDME LISRYFSILP LLINISEDVD LAYEINRQNN TNQDYLGKLA LTIASVAEKE 

       130        140        150        160        170        180 
NAKELLEKVT VVPVLTAHPT QVQRKTVLEL TNSIHNLLRR YRDVKAGVMN QNKWYSELYR 

       190        200        210        220        230        240 
YIDILMQTDI IREKKLKVKN EITNVMQYYN SSLIQAITAL TSKYKTLAKD KGILLDNPKP 

       250        260        270        280        290        300 
INMGMWIGGD RDGNPFVTAE TLRLSATVQS EVILRFYIDK LSALYQTFSL SSALTKTSPE 

       310        320        330        340        350        360 
VERLASLSSD QSIYRENEPY RRAFHYIQVR LAKTLQELVG QPASDQLASR MPATVGSLQS 

       370        380        390        400        410        420 
GVTSIVTNSS DQQAPAYKTA AAFKADLVMI EQSLIAAGDS SLVEGDLQEV LQAVDIFGFF 

       430        440        450        460        470        480 
LASIDLRQDS SVQEACVAEL LKNAGMVENY SALSEEQKCE ILLKELTEDP RTLSSAAVEK 

       490        500        510        520        530        540 
SELLEKELAI YTAARELKDK LGEEVIKQHI ISHTESVSDM FELAIMLKEV GLIDQRQARV 

       550        560        570        580        590        600 
QIVPLFETIE DLDNARAIMT QYLSYDIVKS WIATNAGYQE IMLGYSDSNK DGGYLASGWT 

       610        620        630        640        650        660 
LYKAQNELTK IGEDNDVSIT FFHGRGGTVG RGGGPSYEAI TSQPFGSIKD RIRLTEQGEI 

       670        680        690        700        710        720 
IENKYGNQDV AYYNLEMLIS ASINRMVTRM LTNPDEIDGF RKIMDEIVED SKRIYRELVF 

       730        740        750        760        770        780 
DNPHFYDYFF EASPIKEVSS LNIGSRPAAR KTITDISGLR AIPWVFSWSQ NRIMLPGWYA 

       790        800        810        820        830        840 
VGSAFKRFID KEEGNLAKLQ HMYDKWPFFH SLLSNVDMVL SKSNMNIAFQ YAQLAESKEV 

       850        860        870        880        890        900 
CEVFHTILDE WQLTKNVILA IAQHDELLEE TPSLKQSLDF RLPYFNVLNY IQIELIKRLR 

       910        920 
HEQLDEDYEK LIHTTINGIA TGLRNSG 

« Hide

References

[1]"Genomic evidence for the evolution of Streptococcus equi: host restriction, increased virulence, and genetic exchange with human pathogens."
Holden M.T.G., Heather Z., Paillot R., Steward K.F., Webb K., Ainslie F., Jourdan T., Bason N.C., Holroyd N.E., Mungall K., Quail M.A., Sanders M., Simmonds M., Willey D., Brooks K., Aanensen D.M., Spratt B.G., Jolley K.A. expand/collapse author list , Maiden M.C.J., Kehoe M., Chanter N., Bentley S.D., Robinson C., Maskell D.J., Parkhill J., Waller A.S.
PLoS Pathog. 5:E1000346-E1000346(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: H70 EMBL CAW99736.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
FM204884 Genomic DNA. Translation: CAW99736.1.
RefSeqYP_002744768.1. NC_012470.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING553483.SZO_12420.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAW99736; CAW99736; SZO_12420.
GeneID7693806.
KEGGseq:SZO_12420.
PATRIC19652244. VBIStrEqu35012_1318.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2352.
HOGENOMHOG000238647.
KOK01595.
OMASILNCET.
OrthoDBEOG6TJ7T8.

Enzyme and pathway databases

BioCycSEQU40041:GC8B-1331-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 nameC0MHJ2_STRS7
AccessionPrimary (citable) accession number: C0MHJ2
Entry history
Integrated into UniProtKB/TrEMBL: May 5, 2009
Last sequence update: May 5, 2009
Last modified: June 11, 2014
This is version 37 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)