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Database: UniProt
Entry: Q47L13_THEFY
LinkDB: Q47L13_THEFY
Original site: Q47L13_THEFY 
ID   Q47L13_THEFY            Unreviewed;       227 AA.
AC   Q47L13;
DT   13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2005, sequence version 1.
DT   27-MAR-2024, entry version 98.
DE   RecName: Full=D-lactate dehydratase {ECO:0000256|ARBA:ARBA00013134};
DE            EC=4.2.1.130 {ECO:0000256|ARBA:ARBA00013134};
GN   OrderedLocusNames=Tfu_2826 {ECO:0000313|EMBL:AAZ56859.1};
OS   Thermobifida fusca (strain YX).
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Nocardiopsaceae; Thermobifida.
OX   NCBI_TaxID=269800 {ECO:0000313|EMBL:AAZ56859.1};
RN   [1] {ECO:0000313|EMBL:AAZ56859.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=YX {ECO:0000313|EMBL:AAZ56859.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Di Bartolo G., Chain P., Schmutz J.,
RA   Larimer F., Land M., Lykidis A., Richardson P.;
RT   "Complete sequence of Thermobifida fusca YX.";
RL   Submitted (JUL-2005) 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};
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DR   EMBL; CP000088; AAZ56859.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q47L13; -.
DR   STRING; 269800.Tfu_2826; -.
DR   KEGG; tfu:Tfu_2826; -.
DR   eggNOG; COG0693; Bacteria.
DR   HOGENOM; CLU_070319_1_1_11; -.
DR   OrthoDB; 9792284at2; -.
DR   GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; 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   Hydrolase {ECO:0000313|EMBL:AAZ56859.1};
KW   Protease {ECO:0000313|EMBL:AAZ56859.1};
KW   Stress response {ECO:0000256|ARBA:ARBA00023016}.
FT   DOMAIN          31..222
FT                   /note="DJ-1/PfpI"
FT                   /evidence="ECO:0000259|Pfam:PF01965"
SQ   SEQUENCE   227 AA;  24179 MW;  3D36B9A293BA92F3 CRC64;
     MPNLPKRVLL ALTSHGSLGD TGKPTGYYVP EAAHPWEVFR KAGYEVSFVS VKGGQPPATG
     YNAEDEVQRE FLEDPEVKKA LADTPTADSL NPADYAAVYF VGGHGTMWDF PDAADLAALA
     RDIYEAGGVV AAVCHGPAGL VNLKLSDGRY LVEGKEFASF TNEEEDAVNL SGVVPFLLQS
     KLEERGGIHV KKPKFESCVV VSERLVTGQN PASASGVAEE TVKLLAD
//
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