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A8A2M8

- FCTA_ECOHS

UniProt

A8A2M8 - FCTA_ECOHS

Protein

Formyl-CoA:oxalate CoA-transferase

Gene

frc

Organism
Escherichia coli O9:H4 (strain HS)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 48 (01 Oct 2014)
      Sequence version 1 (23 Oct 2007)
      Previous versions | rss
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    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

    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: 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.
    OMAiFATIEDW.
    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_transferase.
    [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

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    MSTPLQGIKV LDFTGVQSGP SCTQMLAWFG ADVIKIERPG VGDVTRHQLR    50
    DIPDIDALYF TMLNSNKRSI ELNTKTAEGK EVMEKLIREA DILVENFHPG 100
    AIDHMGFTWE HIQEINPRLI FGSIKGFDEC SPYVNVKAYE NVAQAAGGAA 150
    STTGFWDGPP LVSAAALGDS NTGMHLLIGL LAALLHREKT GRGQRVTMSM 200
    QDAVLNLCRV KLRDQQRLDK LGYLEEYPQY PNGTFGDAVP RGGNAGGGGQ 250
    PGWILKCKGW ETDPNAYIYF TIQEQNWENT CKAIGKPEWI TDPAYSTAHA 300
    RQPHIFDIFA EIEKYTVTID KHEAVAYLTQ FDIPCAPVLS MKEISLDPSL 350
    RQSGSVVEVE QPLRGKYLTV GCPMKFSAFT PDIKAAPLLG EHTAAVLQEL 400
    GYSDDEIAAM KQNHAI 416
    Length:416
    Mass (Da):45,828
    Last modified:October 23, 2007 - v1
    Checksum:i97F7FA4001073301
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000802 Genomic DNA. Translation: ABV06782.1 .
    RefSeqi YP_001459165.1. NC_009800.1.

    3D structure databases

    ProteinModelPortali A8A2M8.
    SMRi A8A2M8. Positions 2-416.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 331112.EcHS_A2511.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABV06782 ; ABV06782 ; EcHS_A2511 .
    GeneIDi 5592503.
    KEGGi ecx:EcHS_A2511.
    PATRICi 18315000. VBIEscCol77814_2461.

    Phylogenomic databases

    eggNOGi COG1804.
    HOGENOMi HOG000219745.
    KOi K07749.
    OMAi FATIEDW.
    OrthoDBi EOG6C8MWH.

    Enzyme and pathway databases

    UniPathwayi UPA00540 ; UER00598 .
    BioCyci ECOL331112:GHHI-2497-MONOMER.

    Family and domain databases

    Gene3Di 3.40.50.10540. 2 hits.
    HAMAPi MF_00742. Formyl_CoA_transfer.
    InterProi IPR003673. CoA-Trfase_fam_III.
    IPR023606. CoA-Trfase_III_dom.
    IPR017659. Formyl-CoA_transferase.
    [Graphical view ]
    PANTHERi PTHR11837. PTHR11837. 1 hit.
    Pfami PF02515. CoA_transf_3. 1 hit.
    [Graphical view ]
    SUPFAMi SSF89796. SSF89796. 1 hit.
    TIGRFAMsi TIGR03253. oxalate_frc. 1 hit.
    ProtoNeti Search...

    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: October 1, 2014
    This is version 48 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