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P11568

- HGDC_ACIFV

UniProt

P11568 - HGDC_ACIFV

Protein

Activator of (R)-2-hydroxyglutaryl-CoA dehydratase

Gene

hgdC

Organism
Acidaminococcus fermentans (strain ATCC 25085 / DSM 20731 / VR4)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 91 (01 Oct 2014)
      Sequence version 2 (01 Nov 1997)
      Previous versions | rss
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    Functioni

    Required for the activation of (R)-2-hydroxyglutaryl-CoA dehydratase. This protein is extremely sensitive towards oxygen.

    Cofactori

    Binds 1 4Fe-4S cluster per dimer.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi127 – 1271Iron-sulfur (4Fe-4S); shared with dimeric partner
    Metal bindingi166 – 1661Iron-sulfur (4Fe-4S); shared with dimeric partner

    GO - Molecular functioni

    1. 4 iron, 4 sulfur cluster binding Source: UniProtKB-KW
    2. metal ion binding Source: UniProtKB-KW

    Keywords - Ligandi

    4Fe-4S, Iron, Iron-sulfur, Metal-binding

    Enzyme and pathway databases

    BioCyciAFER591001:GHUL-1889-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Activator of (R)-2-hydroxyglutaryl-CoA dehydratase
    Alternative name(s):
    2-hydroxyglutaryl-CoA dehydratase component A
    Gene namesi
    Name:hgdC
    Ordered Locus Names:Acfer_1816
    OrganismiAcidaminococcus fermentans (strain ATCC 25085 / DSM 20731 / VR4)
    Taxonomic identifieri591001 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesNegativicutesSelenomonadalesAcidaminococcaceaeAcidaminococcus
    ProteomesiUP000001902: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 260260Activator of (R)-2-hydroxyglutaryl-CoA dehydratasePRO_0000083965Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.

    Structurei

    Secondary structure

    1
    260
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 107
    Beta strandi12 – 2110
    Turni22 – 243
    Beta strandi25 – 339
    Helixi40 – 5213
    Helixi56 – 583
    Beta strandi60 – 667
    Turni67 – 759
    Beta strandi77 – 804
    Helixi82 – 9312
    Beta strandi99 – 1046
    Beta strandi107 – 1148
    Beta strandi117 – 12610
    Helixi132 – 14211
    Turni146 – 1483
    Helixi149 – 1535
    Helixi167 – 17913
    Helixi184 – 20421
    Beta strandi210 – 2167
    Helixi217 – 2204
    Helixi222 – 23211
    Helixi240 – 2445
    Helixi245 – 25713

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1HUXX-ray3.00A/B1-260[»]
    ProteinModelPortaliP11568.
    SMRiP11568. Positions 2-249.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP11568.

    Family & Domainsi

    Sequence similaritiesi

    To E.coli YjiL and M.jannaschii MJ0004 and MJ0800.Curated

    Phylogenomic databases

    HOGENOMiHOG000282733.
    OMAiQETEMIA.

    Family and domain databases

    InterProiIPR002731. ATPase_BadF.
    IPR008275. CoA_E_activase.
    [Graphical view]
    PfamiPF01869. BcrAD_BadFG. 1 hit.
    [Graphical view]
    TIGRFAMsiTIGR00241. CoA_E_activ. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P11568-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSIYTLGIDV GSTASKCIIL KDGKEIVAKS LVAVGTGTSG PARSISEVLE    50
    NAHMKKEDMA FTLATGYGRN SLEGIADKQM SELSCHAMGA SFIWPNVHTV 100
    IDIGGQDVKV IHVENGTMTN FQMNDKCAAG TGRFLDVMAN ILEVKVSDLA 150
    ELGAKSTKRV AISSTCTVFA ESEVISQLSK GTDKIDIIAG IHRSVASRVI 200
    GLANRVGIVK DVVMTGGVAQ NYGVRGALEE GLGVEIKTSP LAQYNGALGA 250
    ALYAYKKAAK 260
    Length:260
    Mass (Da):27,269
    Last modified:November 1, 1997 - v2
    Checksum:i7E97044DB6E805AC
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti196 – 1961A → P in CAA32464. (PubMed:2659350)Curated
    Sequence conflicti209 – 2091V → L in CAA32464. (PubMed:2659350)Curated
    Sequence conflicti214 – 22411MTGGVAQNYGV → HDRRCSPELWL in CAA32464. (PubMed:2659350)CuratedAdd
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X59645 Genomic DNA. Translation: CAA42196.1.
    CP001859 Genomic DNA. Translation: ADB48170.1.
    X14252 Genomic DNA. Translation: CAA32464.1.
    PIRiS36105.
    RefSeqiWP_012939153.1. NC_013740.1.
    YP_003399485.1. NC_013740.1.

    Genome annotation databases

    EnsemblBacteriaiADB48170; ADB48170; Acfer_1816.
    GeneIDi8738319.
    KEGGiafn:Acfer_1816.
    PATRICi31910223. VBIAciFer109666_1807.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X59645 Genomic DNA. Translation: CAA42196.1 .
    CP001859 Genomic DNA. Translation: ADB48170.1 .
    X14252 Genomic DNA. Translation: CAA32464.1 .
    PIRi S36105.
    RefSeqi WP_012939153.1. NC_013740.1.
    YP_003399485.1. NC_013740.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1HUX X-ray 3.00 A/B 1-260 [» ]
    ProteinModelPortali P11568.
    SMRi P11568. Positions 2-249.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ADB48170 ; ADB48170 ; Acfer_1816 .
    GeneIDi 8738319.
    KEGGi afn:Acfer_1816.
    PATRICi 31910223. VBIAciFer109666_1807.

    Phylogenomic databases

    HOGENOMi HOG000282733.
    OMAi QETEMIA.

    Enzyme and pathway databases

    BioCyci AFER591001:GHUL-1889-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P11568.

    Family and domain databases

    InterProi IPR002731. ATPase_BadF.
    IPR008275. CoA_E_activase.
    [Graphical view ]
    Pfami PF01869. BcrAD_BadFG. 1 hit.
    [Graphical view ]
    TIGRFAMsi TIGR00241. CoA_E_activ. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Identification of the gene encoding the activator of (R)-2-hydroxyglutaryl-CoA dehydratase from Acidaminococcus fermentans by gene expression in Escherichia coli."
      Bendrat K., Mueller U., Klees A.-G., Buckel W.
      FEBS Lett. 329:329-331(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 25085 / DSM 20731 / VR4.
    3. "Cloning and sequencing of the genes of 2-hydoxyglutaryl-CoA dehydratase from Acidaminococcus fermentans."
      Dutscho R., Wohlfarth G., Buckel P., Buckel W.
      Eur. J. Biochem. 181:741-746(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 129-260.
    4. "Activation of (R)-2-hydroxyglutaryl-CoA dehydratase from Acidaminococcus fermentans."
      Mueller U., Buckel W.
      Eur. J. Biochem. 230:698-704(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    5. "The iron-sulfur clusters in 2-hydroxyglutaryl-CoA dehydratase from Acidaminococcus fermentans. Biochemical and spectroscopic investigations."
      Hans M., Buckel W., Bill E.
      Eur. J. Biochem. 267:7082-7093(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    6. "Crystal structure of the Acidaminococcus fermentans 2-hydroxyglutaryl-CoA dehydratase component A."
      Locher K.P., Hans M., Yeh A.P., Schmid B., Buckel W., Rees D.C.
      J. Mol. Biol. 307:297-308(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).

    Entry informationi

    Entry nameiHGDC_ACIFV
    AccessioniPrimary (citable) accession number: P11568
    Secondary accession number(s): D2RM68, Q44042
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1989
    Last sequence update: November 1, 1997
    Last modified: October 1, 2014
    This is version 91 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references

    External Data

    Dasty 3