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Protein

Formyl-CoA:oxalate CoA-transferase

Gene

frc

Organism
Escherichia coli O9:H4 (strain HS)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Involved in the catabolism of oxalate and in the adapatation to low pH via the induction of the oxalate-dependent acid tolerance response (ATR). Catalyzes the transfer of the CoA moiety from formyl-CoA to oxalate (By similarity).By similarity

Catalytic activityi

Formyl-CoA + oxalate = formate + oxalyl-CoA.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei38 – 381Coenzyme AUniRule annotation
Binding sitei104 – 1041Coenzyme AUniRule annotation
Active sitei169 – 1691NucleophileUniRule annotation

GO - Molecular functioni

  1. formyl-CoA transferase activity Source: UniProtKB-EC

GO - Biological processi

  1. oxalate catabolic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Enzyme and pathway databases

BioCyciECOL331112:GHHI-2497-MONOMER.
UniPathwayiUPA00540; UER00598.

Names & Taxonomyi

Protein namesi
Recommended name:
Formyl-CoA:oxalate CoA-transferase (EC:2.8.3.16UniRule annotation)
Short name:
FCOCT
Alternative name(s):
Formyl-coenzyme A transferaseUniRule annotation
Short name:
Formyl-CoA transferaseUniRule annotation
Gene namesi
Name:frcUniRule annotation
Ordered Locus Names:EcHS_A2511
OrganismiEscherichia coli O9:H4 (strain HS)
Taxonomic identifieri331112 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000001123 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 416416Formyl-CoA:oxalate CoA-transferasePRO_1000062169Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi331112.EcHS_A2511.

Structurei

3D structure databases

ProteinModelPortaliA8A2M8.
SMRiA8A2M8. Positions 2-416.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni17 – 182Coenzyme A bindingBy similarity
Regioni72 – 754Coenzyme A bindingBy similarity
Regioni96 – 983Coenzyme A bindingBy similarity
Regioni137 – 1404Coenzyme A bindingBy similarity
Regioni248 – 2503Substrate bindingBy similarity
Regioni273 – 2753Coenzyme A bindingBy similarity

Sequence similaritiesi

Belongs to the CaiB/BaiF CoA-transferase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG1804.
HOGENOMiHOG000219745.
KOiK07749.
OMAiKFDIPCA.
OrthoDBiEOG6C8MWH.

Family and domain databases

Gene3Di3.40.50.10540. 2 hits.
HAMAPiMF_00742. Formyl_CoA_transfer.
InterProiIPR003673. CoA-Trfase_fam_III.
IPR023606. CoA-Trfase_III_dom.
IPR017659. Formyl_CoA_transfer.
[Graphical view]
PANTHERiPTHR11837. PTHR11837. 1 hit.
PfamiPF02515. CoA_transf_3. 1 hit.
[Graphical view]
SUPFAMiSSF89796. SSF89796. 1 hit.
TIGRFAMsiTIGR03253. oxalate_frc. 1 hit.

Sequencei

Sequence statusi: Complete.

A8A2M8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTPLQGIKV LDFTGVQSGP SCTQMLAWFG ADVIKIERPG VGDVTRHQLR
60 70 80 90 100
DIPDIDALYF TMLNSNKRSI ELNTKTAEGK EVMEKLIREA DILVENFHPG
110 120 130 140 150
AIDHMGFTWE HIQEINPRLI FGSIKGFDEC SPYVNVKAYE NVAQAAGGAA
160 170 180 190 200
STTGFWDGPP LVSAAALGDS NTGMHLLIGL LAALLHREKT GRGQRVTMSM
210 220 230 240 250
QDAVLNLCRV KLRDQQRLDK LGYLEEYPQY PNGTFGDAVP RGGNAGGGGQ
260 270 280 290 300
PGWILKCKGW ETDPNAYIYF TIQEQNWENT CKAIGKPEWI TDPAYSTAHA
310 320 330 340 350
RQPHIFDIFA EIEKYTVTID KHEAVAYLTQ FDIPCAPVLS MKEISLDPSL
360 370 380 390 400
RQSGSVVEVE QPLRGKYLTV GCPMKFSAFT PDIKAAPLLG EHTAAVLQEL
410
GYSDDEIAAM KQNHAI
Length:416
Mass (Da):45,828
Last modified:October 23, 2007 - v1
Checksum:i97F7FA4001073301
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000802 Genomic DNA. Translation: ABV06782.1.
RefSeqiYP_001459165.1. NC_009800.1.

Genome annotation databases

EnsemblBacteriaiABV06782; ABV06782; EcHS_A2511.
GeneIDi5592503.
KEGGiecx:EcHS_A2511.
PATRICi18315000. VBIEscCol77814_2461.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000802 Genomic DNA. Translation: ABV06782.1.
RefSeqiYP_001459165.1. NC_009800.1.

3D structure databases

ProteinModelPortaliA8A2M8.
SMRiA8A2M8. Positions 2-416.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi331112.EcHS_A2511.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABV06782; ABV06782; EcHS_A2511.
GeneIDi5592503.
KEGGiecx:EcHS_A2511.
PATRICi18315000. VBIEscCol77814_2461.

Phylogenomic databases

eggNOGiCOG1804.
HOGENOMiHOG000219745.
KOiK07749.
OMAiKFDIPCA.
OrthoDBiEOG6C8MWH.

Enzyme and pathway databases

UniPathwayiUPA00540; UER00598.
BioCyciECOL331112:GHHI-2497-MONOMER.

Family and domain databases

Gene3Di3.40.50.10540. 2 hits.
HAMAPiMF_00742. Formyl_CoA_transfer.
InterProiIPR003673. CoA-Trfase_fam_III.
IPR023606. CoA-Trfase_III_dom.
IPR017659. Formyl_CoA_transfer.
[Graphical view]
PANTHERiPTHR11837. PTHR11837. 1 hit.
PfamiPF02515. CoA_transf_3. 1 hit.
[Graphical view]
SUPFAMiSSF89796. SSF89796. 1 hit.
TIGRFAMsiTIGR03253. oxalate_frc. 1 hit.
ProtoNetiSearch...

Publicationsi

  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.

Entry informationi

Entry nameiFCTA_ECOHS
AccessioniPrimary (citable) accession number: A8A2M8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: October 23, 2007
Last modified: April 29, 2015
This is version 50 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.