ID   A0A1G8AI55_9VIBR        Unreviewed;       626 AA.
AC   A0A1G8AI55;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   SubName: Full=Propanediol dehydratase reactivation factor, large subunit {ECO:0000313|EMBL:SDH20638.1};
GN   ORFNames=SAMN04488136_110142 {ECO:0000313|EMBL:SDH20638.1};
OS   Vibrio xiamenensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=861298 {ECO:0000313|EMBL:SDH20638.1, ECO:0000313|Proteomes:UP000198854};
RN   [1] {ECO:0000313|EMBL:SDH20638.1, ECO:0000313|Proteomes:UP000198854}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.10228 {ECO:0000313|EMBL:SDH20638.1,
RC   ECO:0000313|Proteomes:UP000198854};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FNDD01000010; SDH20638.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G8AI55; -.
DR   STRING; 861298.SAMN04488136_110142; -.
DR   OrthoDB; 4676896at2; -.
DR   Proteomes; UP000198854; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd00012; NBD_sugar-kinase_HSP70_actin; 1.
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   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.
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:UP000198854}.
FT   DOMAIN          92..253
FT                   /note="DD-reactivating factor swiveling"
FT                   /evidence="ECO:0000259|Pfam:PF18427"
FT   DOMAIN          274..614
FT                   /note="Diol dehydratase reactivase ATPase-like"
FT                   /evidence="ECO:0000259|Pfam:PF08841"
FT   BINDING         11..13
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         569..570
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR011502-2"
FT   BINDING         603
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR011502-2"
SQ   SEQUENCE   626 AA;  66356 MW;  8B2345D16DA1378F CRC64;
     MAYIVGIDIG NSSTEVALAN VQGSDVRFMA SAITETTGIK GTKRNLFGIY QALDMVVENA
     SLSRGDISLI RINEATPVIG DVAMETITET IITESTMIGH NPKTPGGVGL GVGLTINCED
     LLKRDNDQPY ILVVPGEFDF ADVATMVNAA TEAGYQIQAL ILQKDDGVLV SNRLSRTLPI
     VDEVSYIDRI PLGMLAAVEV APPGQVISTL SNPYGIATVF ELSSDETKNI VPVARALIGT
     RSAVVVKTPA GDVKARTIPA GHLTLYCQGR SHSIDVAEGS EKIMQGVEAC SALDNVTGEA
     GSNIGGMLEN VRQTMAKLTD KPSSEIFIQD LLAVDTLVPV NVVGGLAGEF SLEHAVGIAS
     MVKSDHLQMA RIAQEIQATL NVKVQIGGAE AEAAILGALT TPGTQTPLAI LDLGAGSTDA
     SIINHNGEIV ATHLAGAGDM VTMIIASELG LDDRYLAEDI KKYPLAKVES LFHLRHEDGT
     VQFFDQPLPS EIFARVVVVK NPPQGDSKDD DPAQPRFVPL PGEHTIERVK LVRQSAKQRV
     FVTNALRALK SVSPTGNIRD IPFVVLVGGS SLDFEVPQLV TDALSHYNLV AGRGNVRGCQ
     GPRNAVATGL ILAYQQGRQA QEEPLQ
//