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Database: UniProt
Entry: B2TKP7_CLOBB
LinkDB: B2TKP7_CLOBB
Original site: B2TKP7_CLOBB 
ID   B2TKP7_CLOBB            Unreviewed;       253 AA.
AC   B2TKP7; U4P2B1;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   27-MAR-2024, entry version 64.
DE   SubName: Full=2-hydroxyglutaryl-CoA dehydratase component A {ECO:0000313|EMBL:ACD24062.1};
GN   Name=hgdC {ECO:0000313|EMBL:ACD24062.1};
GN   OrderedLocusNames=CLL_A0649 {ECO:0000313|EMBL:ACD24062.1};
OS   Clostridium botulinum (strain Eklund 17B / Type B).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=935198 {ECO:0000313|EMBL:ACD24062.1, ECO:0000313|Proteomes:UP000001195};
RN   [1] {ECO:0000313|Proteomes:UP000001195}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Eklund 17B / Type B {ECO:0000313|Proteomes:UP000001195};
RA   Brinkac L.M., Brown J.L., Bruce D., Detter C., Munk C., Smith L.A.,
RA   Smith T.J., Sutton G., Brettin T.S.;
RT   "Complete sequence of Clostridium botulinum strain Eklund.";
RL   Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|ARBA:ARBA00001966};
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DR   EMBL; CP001056; ACD24062.1; -; Genomic_DNA.
DR   AlphaFoldDB; B2TKP7; -.
DR   KEGG; cbk:CLL_A0649; -.
DR   PATRIC; fig|935198.13.peg.596; -.
DR   HOGENOM; CLU_066597_0_0_9; -.
DR   Proteomes; UP000001195; Chromosome.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.420.40; -; 2.
DR   InterPro; IPR002731; ATPase_BadF.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR008275; CoA_E_activase_dom.
DR   NCBIfam; TIGR00241; CoA_E_activ; 1.
DR   PANTHER; PTHR32329; BIFUNCTIONAL PROTEIN [INCLUDES 2-HYDROXYACYL-COA DEHYDRATASE (N-TER) AND ITS ACTIVATOR DOMAIN (C_TERM)-RELATED; 1.
DR   PANTHER; PTHR32329:SF2; BIFUNCTIONAL PROTEIN [INCLUDES 2-HYDROXYACYL-COA DEHYDRATASE (N-TER) AND ITS ACTIVATOR DOMAIN (C_TERM)-RELATED; 1.
DR   Pfam; PF01869; BcrAD_BadFG; 1.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 1.
PE   4: Predicted;
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT   DOMAIN          6..246
FT                   /note="ATPase BadF/BadG/BcrA/BcrD type"
FT                   /evidence="ECO:0000259|Pfam:PF01869"
SQ   SEQUENCE   253 AA;  27641 MW;  0795ACCE78571941 CRC64;
     MSKYTLGIDS GSTTTKGVLF DGKTIVRTML VKTAAKPRES ISKIYNELYS NNVKYTITTG
     YGRDLLKEAD RTITEITCHA KGAAFLNPNI KGVIDIGGQD SKAILLDESL NVVDFLMNDK
     CAAGTGRFVE VMMRILEEDI TNIDEFVKDK KPVNITSMCT VFAESEIISL LAKDVHRGDI
     ALGIIHSICR RTANFAQKLN LKDEVFFSGG LASSEVFRAT LESYLKQKVS INELSQFAGA
     IGAATIGYVL AEC
//
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