ID A0A162SCA6_9CLOT Unreviewed; 613 AA.
AC A0A162SCA6;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Diol dehydratase-reactivating factor alpha subunit {ECO:0000313|EMBL:KZL91051.1};
GN Name=ddrA_2 {ECO:0000313|EMBL:KZL91051.1};
GN ORFNames=CLMAG_39620 {ECO:0000313|EMBL:KZL91051.1};
OS Clostridium magnum DSM 2767.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1121326 {ECO:0000313|EMBL:KZL91051.1, ECO:0000313|Proteomes:UP000076603};
RN [1] {ECO:0000313|EMBL:KZL91051.1, ECO:0000313|Proteomes:UP000076603}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2767 {ECO:0000313|EMBL:KZL91051.1,
RC ECO:0000313|Proteomes:UP000076603};
RA Poehlein A., Uhlig R., Fischer R., Bahl H., Daniel R.;
RT "Genome sequence of Clostridium magnum DSM 2767.";
RL Submitted (APR-2016) 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:KZL91051.1}.
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DR EMBL; LWAE01000004; KZL91051.1; -; Genomic_DNA.
DR RefSeq; WP_066626236.1; NZ_LWAE01000004.1.
DR AlphaFoldDB; A0A162SCA6; -.
DR STRING; 1121326.CLMAG_39620; -.
DR PATRIC; fig|1121326.3.peg.4009; -.
DR OrthoDB; 4676896at2; -.
DR Proteomes; UP000076603; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000076603}.
FT DOMAIN 92..258
FT /note="DD-reactivating factor swiveling"
FT /evidence="ECO:0000259|Pfam:PF18427"
FT DOMAIN 280..605
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 170
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR011502-1"
FT BINDING 187
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR011502-1"
FT BINDING 463..466
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR011502-2"
FT BINDING 561..562
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR011502-2"
FT BINDING 595
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR011502-2"
SQ SEQUENCE 613 AA; 65551 MW; 4A2ED0F7080762CE CRC64;
MRIIAGVDIG NATTEVALAR VDNDKIEFLS SGIVQTTGIK GTEENIQGVF SSLKRALYKV
SMELEDLQLV RINEAAPVIG DVAMETITET IITESTMIGH NPTTPGGIGL GIGQTIYIED
LDSLDIKSLT EENQFIVLIL SKVSFLEAAA RINAAVKRGI NITAAVVQRD DGVLINNRLD
KKIPIVDEVM LLEKVPIGMK AAVEVADQGG VVETLCNPYG IATVFGLTSE ETKLIVPISR
ALIGNRSAVV IKTPKGDVQE KRIPAGKIHI DGLKRKETAD VEDGAEKIME AVKLCVPVQD
IKGEAGTNAG GMLEKVRQVM AKLTNQKITD IKIQDLLAVD TFIPQKVKGG LAEEFSMENA
VGIAAMVKAD KLQMQMIADR LQEKLKVAVE VGGVEADMAI RGALTTPGSS TPLAILDMGA
GSTDASIINS QGQICSIHLA GAGNMVTMLI KSELGLEDFN LAEDIKKYPL AKVESLFHIR
HEDGTVEFFE NPLEPSVFAK VVILKDGMLI PIDGQNSLEK IKTIRRSAKE KVFVTNCLRA
LSIVSPTGNI RDIEFVVLVG GSSLDFEVPQ LVTDALAQYG VVAGRGNIRG VEGPRNAVAT
GLILAFNGNG EDN
//
