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Q59111

- GCTA_ACIFV

UniProt

Q59111 - GCTA_ACIFV

Protein

Glutaconate CoA-transferase subunit A

Gene

gctA

Organism
Acidaminococcus fermentans (strain ATCC 25085 / DSM 20731 / VR4)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 91 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Catalyzes the transfer of the CoA moiety from acetyl-CoA to (R)-2-hydroxyglutarate and related compounds like glutaconate.

    Catalytic activityi

    Acetyl-CoA + (E)-glutaconate = acetate + glutaconyl-1-CoA.

    Pathwayi

    GO - Molecular functioni

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

    GO - Biological processi

    1. glutamate catabolic process via 2-hydroxyglutarate Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Transferase

    Enzyme and pathway databases

    BioCyciAFER591001:GHUL-1892-MONOMER.
    MetaCyc:MONOMER-1028.
    SABIO-RKQ59111.
    UniPathwayiUPA00533; UER00686.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutaconate CoA-transferase subunit A (EC:2.8.3.12)
    Alternative name(s):
    GCT large subunit
    Gene namesi
    Name:gctA
    Ordered Locus Names:Acfer_1819
    OrganismiAcidaminococcus fermentans (strain ATCC 25085 / DSM 20731 / VR4)
    Taxonomic identifieri591001 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesNegativicutesSelenomonadalesAcidaminococcaceaeAcidaminococcus
    ProteomesiUP000001902: Chromosome

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 320319Glutaconate CoA-transferase subunit APRO_0000157927Add
    BLAST

    Interactioni

    Subunit structurei

    Heterooctamer of four A and four B subunits.

    Protein-protein interaction databases

    DIPiDIP-6200N.
    IntActiQ59111. 1 interaction.

    Structurei

    Secondary structure

    1
    320
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi7 – 148
    Beta strandi20 – 234
    Helixi33 – 419
    Beta strandi47 – 504
    Beta strandi52 – 543
    Helixi56 – 638
    Beta strandi67 – 759
    Turni78 – 803
    Beta strandi81 – 833
    Helixi85 – 939
    Beta strandi96 – 1005
    Helixi103 – 11513
    Beta strandi118 – 1236
    Helixi129 – 1324
    Helixi138 – 1425
    Beta strandi153 – 1575
    Beta strandi160 – 16910
    Beta strandi174 – 18310
    Helixi198 – 2047
    Beta strandi205 – 21511
    Helixi218 – 2225
    Helixi225 – 2273
    Helixi232 – 2343
    Beta strandi237 – 2404
    Turni242 – 2476
    Beta strandi248 – 2503
    Turni251 – 2533
    Helixi258 – 26710
    Helixi271 – 28111
    Turni282 – 2843
    Helixi288 – 2958
    Helixi297 – 3015
    Turni307 – 3093
    Helixi315 – 3173

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1POIX-ray2.50A/C2-318[»]
    ProteinModelPortaliQ59111.
    SMRiQ59111. Positions 2-318.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ59111.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    HOGENOMiHOG000011749.
    KOiK01039.
    OMAiTHLIPFA.

    Family and domain databases

    InterProiIPR004165. CoA_trans_fam_I.
    [Graphical view]
    PANTHERiPTHR13707. PTHR13707. 1 hit.
    PfamiPF01144. CoA_trans. 1 hit.
    [Graphical view]
    SMARTiSM00882. CoA_trans. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q59111-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSKVMTLKDA IAKYVHSGDH IALGGFTTDR KPYAAVFEIL RQGITDLTGL    50
    GGAAGGDWDM LIGNGRVKAY INCYTANSGV TNVSRRFRKW FEAGKLTMED 100
    YSQDVIYMMW HAAALGLPFL PVTLMQGSGL TDEWGISKEV RKTLDKVPDD 150
    KFKYIDNPFK PGEKVVAVPV PQVDVAIIHA QQASPDGTVR IWGGKFQDVD 200
    IAEAAKYTIV TCEEIISDEE IRRDPTKNDI PGMCVDAVVL APYGAHPSQC 250
    YGLYDYDNPF LKVYDKVSKT QEDFDAFCKE WVFDLKDHDE YLNKLGATRL 300
    INLKVVPGLG YHIDMTKEDK 320
    Length:320
    Mass (Da):35,722
    Last modified:January 23, 2007 - v3
    Checksum:iC51B214FE17FEB46
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X81440 Genomic DNA. Translation: CAA57199.1.
    CP001859 Genomic DNA. Translation: ADB48173.1.
    PIRiS51051.
    RefSeqiWP_012939156.1. NC_013740.1.
    YP_003399488.1. NC_013740.1.

    Genome annotation databases

    EnsemblBacteriaiADB48173; ADB48173; Acfer_1819.
    GeneIDi8738322.
    KEGGiafn:Acfer_1819.
    PATRICi31910229. VBIAciFer109666_1810.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X81440 Genomic DNA. Translation: CAA57199.1 .
    CP001859 Genomic DNA. Translation: ADB48173.1 .
    PIRi S51051.
    RefSeqi WP_012939156.1. NC_013740.1.
    YP_003399488.1. NC_013740.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1POI X-ray 2.50 A/C 2-318 [» ]
    ProteinModelPortali Q59111.
    SMRi Q59111. Positions 2-318.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-6200N.
    IntActi Q59111. 1 interaction.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ADB48173 ; ADB48173 ; Acfer_1819 .
    GeneIDi 8738322.
    KEGGi afn:Acfer_1819.
    PATRICi 31910229. VBIAciFer109666_1810.

    Phylogenomic databases

    HOGENOMi HOG000011749.
    KOi K01039.
    OMAi THLIPFA.

    Enzyme and pathway databases

    UniPathwayi UPA00533 ; UER00686 .
    BioCyci AFER591001:GHUL-1892-MONOMER.
    MetaCyc:MONOMER-1028.
    SABIO-RK Q59111.

    Miscellaneous databases

    EvolutionaryTracei Q59111.

    Family and domain databases

    InterProi IPR004165. CoA_trans_fam_I.
    [Graphical view ]
    PANTHERi PTHR13707. PTHR13707. 1 hit.
    Pfami PF01144. CoA_trans. 1 hit.
    [Graphical view ]
    SMARTi SM00882. CoA_trans. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Location of the two genes encoding glutaconate coenzyme A-transferase at the beginning of the hydroxyglutarate operon in Acidaminococcus fermentans."
      Mack M., Bendrat K., Zelder O., Eckel E., Linder D., Buckel W.
      Eur. J. Biochem. 226:41-51(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-13.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 25085 / DSM 20731 / VR4.
    3. "Glutaconate CoA-transferase from Acidaminococcus fermentans: the crystal structure reveals homology with other CoA-transferases."
      Jacob U., Mack M., Clausen T., Huber R., Buckel W., Messerschmidt A.
      Structure 5:415-426(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS).

    Entry informationi

    Entry nameiGCTA_ACIFV
    AccessioniPrimary (citable) accession number: Q59111
    Secondary accession number(s): D2RM71
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 91 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3