ID A0A0R1XEN2_9LACO Unreviewed; 616 AA.
AC A0A0R1XEN2;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 08-OCT-2025, entry version 38.
DE SubName: Full=Propanediol dehydratase, large subunit {ECO:0000313|EMBL:KRM28607.1};
GN ORFNames=FD32_GL001709 {ECO:0000313|EMBL:KRM28607.1};
OS Limosilactobacillus panis DSM 6035.
OC Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Limosilactobacillus.
OX NCBI_TaxID=1423782 {ECO:0000313|EMBL:KRM28607.1, ECO:0000313|Proteomes:UP000051412};
RN [1] {ECO:0000313|EMBL:KRM28607.1, ECO:0000313|Proteomes:UP000051412}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6035 {ECO:0000313|EMBL:KRM28607.1,
RC ECO:0000313|Proteomes:UP000051412};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Genome Announc. 6:8322-8322(2015).
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:KRM28607.1}.
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DR EMBL; AZGM01000040; KRM28607.1; -; Genomic_DNA.
DR RefSeq; WP_047767751.1; NZ_AZGM01000040.1.
DR AlphaFoldDB; A0A0R1XEN2; -.
DR STRING; 1423782.FD32_GL001709; -.
DR PATRIC; fig|1423782.4.peg.1781; -.
DR OrthoDB; 4676896at2; -.
DR Proteomes; UP000051412; 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:UP000051412}.
FT DOMAIN 95..257
FT /note="DD-reactivating factor swiveling"
FT /evidence="ECO:0000259|Pfam:PF18427"
FT DOMAIN 279..606
FT /note="Diol dehydratase reactivase ATPase-like"
FT /evidence="ECO:0000259|Pfam:PF08841"
FT BINDING 13..15
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR011502-2"
FT BINDING 107
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR011502-1"
FT BINDING 169
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR011502-1"
FT BINDING 186
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 616 AA; 65620 MW; 58DD1BFD1DCD8CBA CRC64;
MATEKVIGVD IGNSSTEVAL ADVADNGDVN VINSGIAATT GIKGTKQNLV GIRNSINQVL
KKSNLSIDDI DLIRINEATP VIGDVAMETI TETIVTESTM IGHNPDTPGG RGTGAGYTVP
LLELANKTDK SKPYIVVVPK QVDFEDAAKL INAYVAAGYK ITAAILQNDD GVLIDNRLNK
MIPIVDEVAM IDKVPLNMLA AVEVAGPGQV ISQLSNPYGI ATLFSLTPEE TKNIVPISRA
LIGNRSAVVI KTPAGDVKAR VIPAGKINIT GTNGEHEDVD VAAGSDKIMD TVSDFRSIQD
ITGESGTNVG GMLEKVRQTM ADLTGKQNKD IAIQDLLAVD TQVPVKVRGG LAGEFSNESA
VGIAAMVKSD HLQMEMIAKL IEQEFHTKVE IGGAEVESAI RGALTTPGTT KPIAILDLGA
GSTDASIINK ENKTVAIHLA GAGDMVTMII NSELGLEDPY LAEDIKRYPL AKVENLFQIR
HEDGSVQFFD KPLDSGLFAR VVVIKPEGYE PIPGNPSIEK VKMIRQSAKK RVFVTNAIRA
LRIVSPTGNI RDIPYVVIVG GSALDFEIPQ LVTDELAHYN LVAGRGNVRG VEGPRNAVAT
GLVLRYGEER RKQHEN
//
