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Database: UniProt
Entry: A0A0F5ANA0_9GAMM
LinkDB: A0A0F5ANA0_9GAMM
Original site: A0A0F5ANA0_9GAMM 
ID   A0A0F5ANA0_9GAMM        Unreviewed;       228 AA.
AC   A0A0F5ANA0;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=D-lactate dehydratase {ECO:0000256|ARBA:ARBA00013134};
DE            EC=4.2.1.130 {ECO:0000256|ARBA:ARBA00013134};
GN   ORFNames=WN56_15000 {ECO:0000313|EMBL:KKA43658.1};
OS   Salinivibrio sp. KP-1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Salinivibrio.
OX   NCBI_TaxID=1406902 {ECO:0000313|EMBL:KKA43658.1, ECO:0000313|Proteomes:UP000033449};
RN   [1] {ECO:0000313|EMBL:KKA43658.1, ECO:0000313|Proteomes:UP000033449}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KP-1 {ECO:0000313|EMBL:KKA43658.1,
RC   ECO:0000313|Proteomes:UP000033449};
RA   Kaur G., Kumar A., Mathan Kumar R., Kumar N., Singh N.K., Arora A.,
RA   Kaur N., Bala M., Mayilraj S.;
RT   "Taxonomic description and genome sequence of Salinivibrio halophilus sp.
RT   nov., a novel halotolerant gammaproteobacterium isolated from marine
RT   sediment and emended description of the genus Salinivibrio.";
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + methylglyoxal = (R)-lactate + H(+);
CC         Xref=Rhea:RHEA:27754, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16004, ChEBI:CHEBI:17158; EC=4.2.1.130;
CC         Evidence={ECO:0000256|ARBA:ARBA00001524};
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:KKA43658.1}.
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DR   EMBL; LAQR01000048; KKA43658.1; -; Genomic_DNA.
DR   RefSeq; WP_046075760.1; NZ_LAQR01000048.1.
DR   AlphaFoldDB; A0A0F5ANA0; -.
DR   PATRIC; fig|1406902.3.peg.2998; -.
DR   OrthoDB; 9792284at2; -.
DR   Proteomes; UP000033449; Unassembled WGS sequence.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   CDD; cd03141; GATase1_Hsp31_like; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR002818; DJ-1/PfpI.
DR   PANTHER; PTHR48094:SF11; GLUTATHIONE-INDEPENDENT GLYOXALASE HSP31-RELATED; 1.
DR   PANTHER; PTHR48094; PROTEIN/NUCLEIC ACID DEGLYCASE DJ-1-RELATED; 1.
DR   Pfam; PF01965; DJ-1_PfpI; 1.
DR   SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000033449};
KW   Stress response {ECO:0000256|ARBA:ARBA00023016};
KW   Transferase {ECO:0000313|EMBL:KKA43658.1}.
FT   DOMAIN          27..224
FT                   /note="DJ-1/PfpI"
FT                   /evidence="ECO:0000259|Pfam:PF01965"
FT   REGION          49..72
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   228 AA;  24801 MW;  CC40397D1A080F04 CRC64;
     MQQHKILMVL TSHDAMGDTG HKTGFWLEEF TTPYYAFKDA GASIVVASPE GGAAPIDPNS
     EAEDAQSEST RRFDGDAELQ DMVNNTVKLS DVNAYEYDAI FYPGGHGPLW DLAEDPTSRQ
     LIETFYYQGK PVGAVCHGPA VFRHTRSDRD EPLVKGKRVT GFTNGEEAAV GLTEVVPFLV
     EDMLKENGGL YEKADDFTSY VVTDGNLVTG QNPVSSEACV NAVLALLK
//
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