GenomeNet

Database: UniProt
Entry: A0A0L6U0P1_9FIRM
LinkDB: A0A0L6U0P1_9FIRM
Original site: A0A0L6U0P1_9FIRM 
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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
//
DBGET integrated database retrieval system