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A8A2M8 (FCTA_ECOHS) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 39. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Formyl-coenzyme A transferase
Short name=Formyl-CoA transferase
EC=2.8.3.16
Gene names
Name:frc
Ordered Locus Names:EcHS_A2511
OrganismEscherichia coli O9:H4 (strain HS) [Complete proteome] [HAMAP]
Taxonomic identifier331112 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length416 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the transfer of the CoA moiety from formyl-CoA to oxalate By similarity. HAMAP-Rule MF_00742

Catalytic activity

Formyl-CoA + oxalate = formate + oxalyl-CoA. HAMAP-Rule MF_00742

Pathway

Metabolic intermediate degradation; oxalate degradation; CO(2) and formate from oxalate: step 1/2. HAMAP-Rule MF_00742

Subunit structure

Homodimer By similarity.

Sequence similarities

Belongs to the CaiB/BaiF CoA-transferase family.

Ontologies

Keywords
   Molecular functionTransferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processoxalate catabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_functionformyl-CoA transferase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 416416Formyl-coenzyme A transferase HAMAP-Rule MF_00742
PRO_1000062169

Sites

Active site1691Nucleophile By similarity
Binding site961Coenzyme A By similarity

Sequences

Sequence LengthMass (Da)Tools
A8A2M8 [UniParc].

Last modified October 23, 2007. Version 1.
Checksum: 97F7FA4001073301

FASTA41645,828
        10         20         30         40         50         60 
MSTPLQGIKV LDFTGVQSGP SCTQMLAWFG ADVIKIERPG VGDVTRHQLR DIPDIDALYF 

        70         80         90        100        110        120 
TMLNSNKRSI ELNTKTAEGK EVMEKLIREA DILVENFHPG AIDHMGFTWE HIQEINPRLI 

       130        140        150        160        170        180 
FGSIKGFDEC SPYVNVKAYE NVAQAAGGAA STTGFWDGPP LVSAAALGDS NTGMHLLIGL 

       190        200        210        220        230        240 
LAALLHREKT GRGQRVTMSM QDAVLNLCRV KLRDQQRLDK LGYLEEYPQY PNGTFGDAVP 

       250        260        270        280        290        300 
RGGNAGGGGQ PGWILKCKGW ETDPNAYIYF TIQEQNWENT CKAIGKPEWI TDPAYSTAHA 

       310        320        330        340        350        360 
RQPHIFDIFA EIEKYTVTID KHEAVAYLTQ FDIPCAPVLS MKEISLDPSL RQSGSVVEVE 

       370        380        390        400        410 
QPLRGKYLTV GCPMKFSAFT PDIKAAPLLG EHTAAVLQEL GYSDDEIAAM KQNHAI

« Hide

References

[1]"The pangenome structure of Escherichia coli: comparative genomic analysis of E. coli commensal and pathogenic isolates."
Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F., Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R., Henderson I.R., Sperandio V., Ravel J.
J. Bacteriol. 190:6881-6893(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: HS.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000802 Genomic DNA. Translation: ABV06782.1.
RefSeqYP_001459165.1. NC_009800.1.

3D structure databases

ProteinModelPortalA8A2M8.
SMRA8A2M8. Positions 2-416.
ModBaseSearch...

Protein-protein interaction databases

STRING331112.EcHS_A2511.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABV06782; ABV06782; EcHS_A2511.
GeneID5592503.
KEGGecx:EcHS_A2511.
PATRIC18315000. VBIEscCol77814_2461.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1804.
HOGENOMHOG000219745.
KOK07749.
OMAKFDIPCA.
ProtClustDBPRK05398.

Enzyme and pathway databases

BioCycECOL331112:GHHI-2593-MONOMER.
UniPathwayUPA00540; UER00598.

Family and domain databases

Gene3D3.40.50.10540. 2 hits.
HAMAPMF_00742. Formyl-CoA_transfer.
InterProIPR003673. CoA-Trfase_fam_III.
IPR023606. CoA-Trfase_III_dom.
IPR017659. Formyl-CoA_transferase.
[Graphical view]
PANTHERPTHR11837. PTHR11837. 1 hit.
PfamPF02515. CoA_transf_3. 1 hit.
[Graphical view]
SUPFAMSSF89796. CoA-Trfase_fam_III. 1 hit.
TIGRFAMsTIGR03253. oxalate_frc. 1 hit.
ProtoNetSearch...

Entry information

Entry nameFCTA_ECOHS
AccessionPrimary (citable) accession number: A8A2M8
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: October 23, 2007
Last modified: May 1, 2013
This is version 39 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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