ID A0A0L6U0P1_9FIRM Unreviewed; 605 AA.
AC A0A0L6U0P1;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Glycerol dehydratase {ECO:0000313|EMBL:KNZ41360.1};
GN ORFNames=AKG39_12105 {ECO:0000313|EMBL:KNZ41360.1};
OS Acetobacterium bakii.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC Acetobacterium.
OX NCBI_TaxID=52689 {ECO:0000313|EMBL:KNZ41360.1, ECO:0000313|Proteomes:UP000036873};
RN [1] {ECO:0000313|Proteomes:UP000036873}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 8239 {ECO:0000313|Proteomes:UP000036873};
RA Song Y., Hwang S., Cho B.-K.;
RT "Draft genome sequence of Acetobacterium bakii DSM 8293, a potential
RT psychrophilic chemical producer through syngas fermentation.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KNZ41360.1}.
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DR EMBL; LGYO01000031; KNZ41360.1; -; Genomic_DNA.
DR RefSeq; WP_050740662.1; NZ_UOGO01000001.1.
DR AlphaFoldDB; A0A0L6U0P1; -.
DR STRING; 52689.AKG39_12105; -.
DR PATRIC; fig|52689.4.peg.1767; -.
DR OrthoDB; 4676896at2; -.
DR Proteomes; UP000036873; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.30.420.40; -; 2.
DR Gene3D; 3.90.470.30; -; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR Gene3D; 3.50.30.70; Swiveling domain of dehydratase reactivase alpha subunit; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR030994; DDR_dom.
DR InterPro; IPR040916; DDR_swiveling.
DR InterPro; IPR009191; DDRA.
DR InterPro; IPR028975; DDRA_swiveling_dom_sf.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR016039; Thiolase-like.
DR NCBIfam; TIGR04491; reactive_PduG; 1.
DR Pfam; PF08841; DDR; 1.
DR Pfam; PF18427; DDR_swiveling; 1.
DR PIRSF; PIRSF011502; DdrA_PduG; 1.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR SUPFAM; SSF82317; Swiveling domain of dehydratase reactivase alpha subunit; 1.
DR SUPFAM; SSF53901; Thiolase-like; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PIRSR:PIRSR011502-2};
KW Magnesium {ECO:0000256|PIRSR:PIRSR011502-1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR011502-1};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR011502-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000036873}.
FT DOMAIN 92..253
FT /note="DD-reactivating factor swiveling"
FT /evidence="ECO:0000259|Pfam:PF18427"
FT DOMAIN 274..601
FT /note="Diol dehydratase reactivase ATPase-like"
FT /evidence="ECO:0000259|Pfam:PF08841"
FT BINDING 10..12
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR011502-2"
FT BINDING 104
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR011502-1"
FT BINDING 165
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR011502-1"
FT BINDING 182
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR011502-1"
FT BINDING 458..461
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR011502-2"
FT BINDING 556..557
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR011502-2"
FT BINDING 590
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR011502-2"
SQ SEQUENCE 605 AA; 64697 MW; 42CB0543117A590A CRC64;
MIIAGIDIGN ATTETAVARF NNQEKPEFLS SGIYDTSGMK GTRQNIHGIF ASLKIALDKA
HLTVDDIDLI RINEAAPVIG DVAMETITET IITESTMIGH NPSTPGGLGI GVGVTVEIRD
VHNVEKGSSI IVIIPREVDF EDSSRIINNT VKNGIFVNGA IVQRDDGVLI NNRLDKKIPI
VDEVSLIEKV PLNMRAAIEV AAPGSVVEQL SNPYGIATVF DLTSDETKLV VPVSRALIGN
RSAVIIKTPA GDVKERKIPA GKIIIQGATK KAEINVDDGA ERIMEAIRSV APVEDIKGEP
GTNAGGMLEK VRQVMSNLTE QLPATIKIQD LLAVDTFVPQ VVKGGMAEEF SMENAVGIAA
MVKADKLQMN MIAEELEKEL GIKVEVGGVE ANMAVRGALT TPGSNKPLAI IDMGAGSTDA
AIINRAGEIK SIHLAGAGNM VTMLIGSELG FEDMGISEDI KKYPLAKVES LFHIRHEDGT
VQFFDKPLDP QTFARVVILT PNRMVPIPGN YSLDRIRTVR REAKTKVFVV NAIRSLERVS
PTGNVRDIEF VTLVGGSALD FEIPQLVTDA LSKYSIVAGR ANIRAIEGPR NAVATGLVLA
YGVGD
//