ID   A0A1M6HUR3_9CLOT        Unreviewed;       606 AA.
AC   A0A1M6HUR3;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   SubName: Full=Diol dehydratase reactivase alpha subunit {ECO:0000313|EMBL:SHJ25887.1};
GN   ORFNames=SAMN02745975_01649 {ECO:0000313|EMBL:SHJ25887.1};
OS   Geosporobacter subterraneus DSM 17957.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Geosporobacter.
OX   NCBI_TaxID=1121919 {ECO:0000313|EMBL:SHJ25887.1, ECO:0000313|Proteomes:UP000184536};
RN   [1] {ECO:0000313|EMBL:SHJ25887.1, ECO:0000313|Proteomes:UP000184536}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17957 {ECO:0000313|EMBL:SHJ25887.1,
RC   ECO:0000313|Proteomes:UP000184536};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FQZV01000018; SHJ25887.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1M6HUR3; -.
DR   STRING; 1121919.SAMN02745975_01649; -.
DR   OrthoDB; 4676896at2; -.
DR   Proteomes; UP000184536; 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   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}.
FT   DOMAIN          93..254
FT                   /note="DD-reactivating factor swiveling"
FT                   /evidence="ECO:0000259|Pfam:PF18427"
FT   DOMAIN          275..601
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         105
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR011502-1"
FT   BINDING         166
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR011502-1"
FT   BINDING         183
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR011502-1"
FT   BINDING         459..462
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR011502-2"
FT   BINDING         557..558
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR011502-2"
FT   BINDING         591
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR011502-2"
SQ   SEQUENCE   606 AA;  64939 MW;  619917C588045802 CRC64;
     MKLVAGVDIG NATTEVALAQ ITDQNEIKFL SGGIVNTTGI KGTRQNIHGV FASLKQALDK
     TNFKMEDLDL IRINEAAPVI GDVAMETITE TIITESTMIG HNPSTPGGLG LGVGTTIHID
     HLNARSGEEA MIVLIPKNVD FMHAAQEINR FTDLGFNIQG AVAQRDDGVL INNRLKKPIP
     IVDEVLLLEK VPVNMKAAIE VASPGGVVEI LSNPYGIATV FGLTSEETKQ IVPIARALIG
     NRSAVVIKTP KGDVQERRIP AGQIYIIGEK RRATVDVDDG AERIMKILKI SAPIKDIKGE
     PGTNAGGMLE KVRQVMSDLT KQHPNSIKIQ DLLAVDTFVP QKVKGGLAEE FSMENAVGIA
     AMVKADKLQM DMIAEELKAE IAVPVEVGGV EADMAIRGAL TTPGSSTPLA ILDMGAGSTD
     ASVINKNGEI RSIHLAGAGN MVTLLIRSEL GLEDTEMAED IKKYPLAKVE SLFHIRHEDG
     TVQFYEKPLD PNVFAKVVIL KDNNMIPIPD HNSVEKIKLI RRSAKEKVFV TNAIRALSMV
     CPTGNVRDIE FVVLVGGSAL DFEVPQLVTD ALSQYGVVAG RGNIRGSEGP RNAVATGLIL
     AMKGRQ
//