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D9PXG9 (D9PXG9_METTM) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 18. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Protein attributes

Sequence length483 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the irreversible beta-carboxylation of phosphoenolpyruvate (PEP) to form oxaloacetate (OAA), a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle By similarity. HAMAP-Rule MF_01904

Catalytic activity

Phosphate + oxaloacetate = H2O + phosphoenolpyruvate + HCO3-. HAMAP-Rule MF_01904

Cofactor

Magnesium By similarity. HAMAP-Rule MF_01904

Subunit structure

Homotetramer By similarity. HAMAP-Rule MF_01904

Sequence similarities

Belongs to the PEPCase type 2 family. HAMAP-Rule MF_01904

Sequences

Sequence LengthMass (Da)Tools
D9PXG9 [UniParc].

Last modified October 5, 2010. Version 1.
Checksum: B8F3CC940A4BCCD8

FASTA48354,888
        10         20         30         40         50         60 
MKVPRCMSTQ HPDNVNPPFF AEEPELGGED EIREAYYVFS HLGCDEQMWD CEGKEVDNYV 

        70         80         90        100        110        120 
VKKLLTKYQA FFRDHVLGED LRLTLRVPNP TVERAEAKIL LETLESIPRS YDTASLFYGM 

       130        140        150        160        170        180 
DAAPVFEVIL PMTSSSSCLN RIHSYYLDFV KGKERLQLAD GVTVKEWIGE FRPDEINVIP 

       190        200        210        220        230        240 
LFEDHEGMLN AAKITGEYLD GKDIPEQRVF LARSDPAMNY GMISATLLNR IALSDFRDLE 

       250        260        270        280        290        300 
EESGVKLYPI IGMGSAPFRG NLRPDNVEDV TGEYRGAYTF TVQSSFKYDH EPSDVIRGIK 

       310        320        330        340        350        360 
ELRSVKPGRA AEIEREGVLE ILSAYCREYR RQVMDLVDII NRVARYVPGR RKRKLHIGLF 

       370        380        390        400        410        420 
GYSRSMGNVS LPRAITFTAA LYSLGVPPEL LGFNALSSGD LEFIEEVYPG LGRDLHDAAR 

       430        440        450        460        470        480 
YANPESPFLS PEVKSSFEEY LEPEYDEGHM KTTEEIIRAL RINRTANLQE LILEAASQRK 


FLG

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References

« Hide 'large scale' references
[1]"The genome sequence of Methanothermobacter marburgensis."
Kaster A., Seedorf H., Goenrich M., Wiezer A., Liesegang H., Thauer R., Gottschalk G.
Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: Marburg.
[2]"Complete genome sequence of Methanothermobacter marburgensis, a methanoarchaeon model organism."
Liesegang H., Kaster A.K., Wiezer A., Goenrich M., Wollherr A., Seedorf H., Gottschalk G., Thauer R.K.
J. Bacteriol. 192:5850-5851(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 2133 / 14651 / NBRC 100331 / OCM 82 / Marburg.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP001710 Genomic DNA. Translation: ADL58917.1.
RefSeqYP_003850230.1. NC_014408.1.

3D structure databases

ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADL58917; ADL58917; MTBMA_c13290.
GeneID9705037.
KEGGmmg:MTBMA_c13290.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000038601.
KOK01595.
OMAMCTQHPD.

Enzyme and pathway databases

BioCycMMAR79929:GH5J-1336-MONOMER.

Family and domain databases

HAMAPMF_01904. PEPcase_type2.
InterProIPR007566. PEP_COase_arc-type.
IPR015813. Pyrv/PenolPyrv_Kinase.
[Graphical view]
PIRSFPIRSF006677. UCP006677. 1 hit.
SUPFAMSSF51621. Pyrv/PenolPyrv_Kinase_cat. 1 hit.
TIGRFAMsTIGR02751. PEPCase_arch. 1 hit.
ProtoNetSearch...

Entry information

Entry nameD9PXG9_METTM
AccessionPrimary (citable) accession number: D9PXG9
Entry history
Integrated into UniProtKB/TrEMBL: October 5, 2010
Last sequence update: October 5, 2010
Last modified: May 1, 2013
This is version 18 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
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