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Database: UniProt
Entry: A0A6P1M938_9FIRM
LinkDB: A0A6P1M938_9FIRM
Original site: A0A6P1M938_9FIRM 
ID   A0A6P1M938_9FIRM        Unreviewed;       605 AA.
AC   A0A6P1M938;
DT   07-OCT-2020, integrated into UniProtKB/TrEMBL.
DT   07-OCT-2020, sequence version 1.
DT   02-APR-2025, entry version 15.
DE   SubName: Full=Diol dehydratase reactivase subunit alpha {ECO:0000313|EMBL:QHI71249.1};
GN   ORFNames=Ami3637_01530 {ECO:0000313|EMBL:QHI71249.1};
OS   Aminipila terrae.
OC   Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
OC   Anaerovoracaceae; Aminipila.
OX   NCBI_TaxID=2697030 {ECO:0000313|EMBL:QHI71249.1, ECO:0000313|Proteomes:UP000463883};
RN   [1] {ECO:0000313|EMBL:QHI71249.1, ECO:0000313|Proteomes:UP000463883}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBA3637 {ECO:0000313|EMBL:QHI71249.1,
RC   ECO:0000313|Proteomes:UP000463883};
RA   Kim Y.B., Roh S.W.;
RT   "Genomic analysis of Aminipila sp. CBA3637.";
RL   Submitted (JAN-2020) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP047591; QHI71249.1; -; Genomic_DNA.
DR   RefSeq; WP_162361024.1; NZ_CP047591.1.
DR   AlphaFoldDB; A0A6P1M938; -.
DR   KEGG; amic:Ami3637_01530; -.
DR   Proteomes; UP000463883; Chromosome.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000463883}.
FT   DOMAIN          92..252
FT                   /note="DD-reactivating factor swiveling"
FT                   /evidence="ECO:0000259|Pfam:PF18427"
FT   DOMAIN          273..599
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         164
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR011502-1"
FT   BINDING         181
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR011502-1"
FT   BINDING         457..460
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR011502-2"
FT   BINDING         555..556
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR011502-2"
FT   BINDING         589
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR011502-2"
SQ   SEQUENCE   605 AA;  64059 MW;  F87492D09D5BAEBE CRC64;
     MKIIAGIDIG NATTETAIGK IQNGKADFLA SGIVPTTGIK GTSANISGLF KSLTNALDEA
     GLKLEDLDEI RVNEAAPVIG DVAMETITET IITESTMIGH NPETPGGLGV GAGETVLITE
     LGRVTGGRNY IVVIPSSVDF EKAAEEINKF SGSKNITAAI VQKDDGVLIN NRLNKKIPIV
     DEVELVDKVP LGMFCAVEVA GAGSVVEVLS NPYGIATMFN LDSEETKQVV PIARALIGNR
     SAVVIKTPEG DIKERRIPAG TIEIISSHKS IKVDVDEGSE KIMEVVNTVP EVEDVKGEPG
     TNAGGMLERV RQVMSNLTGQ HPQSIKIRDL LAVDTFTPQK VQGGLANEFS QESAVGIAAM
     VKANKLQMEK IAAELTDKIN VPVKVGGVEA DMAIRGALTT PGTSEPLAIL DMGAGSTDAS
     IITPSGRITS IHLAGAGNMA TMLIQSEMGL QDFNTAEDIK KYPLAKVESL FHIRHEDGTV
     EFFEKPLDAN VFAKVVILKE GEMIPLEGNY SIEKIKLIRK AAKERVFVTN AIRALTKVSP
     TNNVRDIQFV VLVGGSALDF EIPQLVTDAL AQYRVVSGRA NIRGTEGPRN AVATGLVLSV
     AGKDG
//
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