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F9ZP62 (F9ZP62_ACICS) Unreviewed, UniProtKB/TrEMBL

Last modified June 11, 2014. Version 11. 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 namesRecommended name:
Phosphoenolpyruvate carboxylase HAMAP-Rule MF_00595

Short name=PEPC HAMAP-Rule MF_00595
Short name=PEPCase HAMAP-Rule MF_00595
EC=4.1.1.31 HAMAP-Rule MF_00595
Gene names
Name:ppc HAMAP-Rule MF_00595
Ordered Locus Names:Atc_1791 EMBL AEK58439.1
OrganismAcidithiobacillus caldus (strain SM-1) [Complete proteome] [HAMAP] EMBL AEK58439.1
Taxonomic identifier990288 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAcidithiobacillalesAcidithiobacillaceaeAcidithiobacillus

Protein attributes

Sequence length930 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 site1471 By similarity HAMAP-Rule MF_00595
Active site5871 By similarity HAMAP-Rule MF_00595

Sequences

Sequence LengthMass (Da)Tools
F9ZP62 [UniParc].

Last modified October 19, 2011. Version 1.
Checksum: FCC4B6B1DC3072E8

FASTA930106,485
        10         20         30         40         50         60 
MENKKVPNDR ALRARVKRLG NLLGEVLKEQ AGDRVFNAVE QLRQGYIRLH RREDPKLRKR 

        70         80         90        100        110        120 
LARFIDALPQ DDLVLVIRAF NTYFSLVNIA EEEFQHLQRR RLLQRSEALW VGSFEETFRA 

       130        140        150        160        170        180 
LQQQGIHSGQ LQYLLGQIRY LPVFTAHPTE SKRRTVLHGL RRIFLTSKML DDPSLSQEEE 

       190        200        210        220        230        240 
NDVLRQLKAQ IQILWETEEV RSNRPQVQDE VENGLFYFRD SLFNAVPMCY HAARRAVRRV 

       250        260        270        280        290        300 
YGNPNVDIPA FIRFGSWIGG DRDGNPNVTA AITGWALRTQ SMEVLREYQR RLADLYQLLG 

       310        320        330        340        350        360 
HSSRFCAVSP VLLASLERDA DDFPELAEWV NQRFPSEPYR RKLRYMMTRL DLRLRQLENG 

       370        380        390        400        410        420 
QILNEAAGPG YSSASEFLED LLLVRDSLRG HRDHYIAEHD VQNLVWLLET FGFHLAALDI 

       430        440        450        460        470        480 
RQESTVHGQT IAELFRDVAG FANYLEQPEE QRLLTLAEAL RRPGCLVTET PELSPLAAET 

       490        500        510        520        530        540 
CAMFRCIAQL RREVSPEAFG SYVISMTHEA SHILEVLLLA KEFGLAGWSR EGLYSEIAVT 

       550        560        570        580        590        600 
PLFETIHDLE RMEAVMSRLL DDPVYAEILR SQGNLQEVML GYSDSCKDGG ILSSSWSLYQ 

       610        620        630        640        650        660 
AQIRLAELAD RRRIQIRVFH GRGGSVGRGG GPTYEAIMAQ PPDTVRGQIK ITEQGEVLSF 

       670        680        690        700        710        720 
KYANLETAVY ELTVGVAGLI RASVGLVRRV ELDRPDYLQV MSELVEIGEA VYRDLTEHTP 

       730        740        750        760        770        780 
GFMDYFYEAT PLNEIAHMNI GSRPSHRHRG DRSMASIRAI PWVFAWAQSR HVLPAWYGLG 

       790        800        810        820        830        840 
SALARWRGDD PDRLNTLRDM AKHWPFFRAL LGNISMAMAK THLDLAREYA GLPQDQECAQ 

       850        860        870        880        890        900 
KIFAKIRAEY ELSLAELLTA LDLPAPLADN PTLAFSLQRR NVYMEPLNHI QLALLRRYRN 

       910        920        930 
EDTPQEFRET WLDPLLRTIN AIAAGQRNTG 

« Hide

References

[1]"Unraveling the Acidithiobacillus caldus complete genome and its central metabolisms for carbon assimilation."
You X.Y., Guo X., Zheng H.J., Zhang M.J., Liu L.J., Zhu Y.Q., Zhu B., Wang S.Y., Zhao G.P., Poetsch A., Jiang C.Y., Liu S.J.
J. Genet. Genomics 38:243-252(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SM-1 EMBL AEK58439.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP002573 Genomic DNA. Translation: AEK58439.1.
RefSeqYP_004749140.1. NC_015850.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAEK58439; AEK58439; Atc_1791.
GeneID10989576.
KEGGacu:Atc_1791.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK01595.

Enzyme and pathway databases

BioCycACAL990288:GJBS-1817-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 nameF9ZP62_ACICS
AccessionPrimary (citable) accession number: F9ZP62
Entry history
Integrated into UniProtKB/TrEMBL: October 19, 2011
Last sequence update: October 19, 2011
Last modified: June 11, 2014
This is version 11 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)