ID   A0PSD6_MYCUA            Unreviewed;       414 AA.
AC   A0PSD6;
DT   09-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2007, sequence version 1.
DT   02-SEP-2026, entry version 108.
DE   RecName: Full=Putative L-lactate dehydrogenase {ECO:0000256|ARBA:ARBA00071405};
GN   Name=lldD2 {ECO:0000313|EMBL:ABL05255.1};
GN   OrderedLocusNames=MUL_3002 {ECO:0000313|EMBL:ABL05255.1};
OS   Mycobacterium ulcerans (strain Agy99).
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Mycobacteriaceae; Mycobacterium; Mycobacterium ulcerans group.
OX   NCBI_TaxID=362242 {ECO:0000313|EMBL:ABL05255.1, ECO:0000313|Proteomes:UP000000765};
RN   [1] {ECO:0000313|EMBL:ABL05255.1, ECO:0000313|Proteomes:UP000000765}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Agy99 {ECO:0000313|EMBL:ABL05255.1,
RC   ECO:0000313|Proteomes:UP000000765};
RX   PubMed=17210928; DOI=10.1101/gr.5942807;
RA   Stinear T.P., Seemann T., Pidot S., Frigui W., Reysset G., Garnier T.,
RA   Meurice G., Simon D., Bouchier C., Ma L., Tichit M., Porter J.L., Ryan J.,
RA   Johnson P.D., Davies J.K., Jenkin G.A., Small P.L., Jones L.M., Tekaia F.,
RA   Laval F., Daffe M., Parkhill J., Cole S.T.;
RT   "Reductive evolution and niche adaptation inferred from the genome of
RT   Mycobacterium ulcerans, the causative agent of Buruli ulcer.";
RL   Genome Res. 17:192-200(2007).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-lactate + A = pyruvate + AH2; Xref=Rhea:RHEA:45816,
CC         ChEBI:CHEBI:13193, ChEBI:CHEBI:15361, ChEBI:CHEBI:16651,
CC         ChEBI:CHEBI:17499; Evidence={ECO:0000256|ARBA:ARBA00050153};
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000256|ARBA:ARBA00001917, ECO:0000256|PROSITE-
CC         ProRule:PRU00683};
CC   -!- SIMILARITY: Belongs to the FMN-dependent alpha-hydroxy acid
CC       dehydrogenase family. {ECO:0000256|ARBA:ARBA00024042,
CC       ECO:0000256|PROSITE-ProRule:PRU00683}.
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DR   EMBL; CP000325; ABL05255.1; -; Genomic_DNA.
DR   RefSeq; WP_011740867.1; NC_008611.1.
DR   AlphaFoldDB; A0PSD6; -.
DR   KEGG; mul:MUL_3002; -.
DR   eggNOG; COG1304; Bacteria.
DR   HOGENOM; CLU_020639_6_1_11; -.
DR   Proteomes; UP000000765; Chromosome.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   CDD; cd02809; alpha_hydroxyacid_oxid_FMN; 1.
DR   FunFam; 3.20.20.70:FF:000261; L-lactate dehydrogenase (Cytochrome); 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR012133; Alpha-hydoxy_acid_DH_FMN.
DR   InterPro; IPR000262; FMN-dep_DH.
DR   InterPro; IPR037396; FMN_HAD.
DR   InterPro; IPR008259; FMN_hydac_DH_AS.
DR   PANTHER; PTHR10578:SF107; 2-HYDROXYACID OXIDASE 1; 1.
DR   PANTHER; PTHR10578; S -2-HYDROXY-ACID OXIDASE-RELATED; 1.
DR   Pfam; PF01070; FMN_dh; 1.
DR   PIRSF; PIRSF000138; Al-hdrx_acd_dh; 1.
DR   SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
DR   PROSITE; PS00557; FMN_HYDROXY_ACID_DH_1; 1.
DR   PROSITE; PS51349; FMN_HYDROXY_ACID_DH_2; 1.
PE   3: Inferred from homology;
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630, ECO:0000256|PIRSR:PIRSR000138-
KW   2}; FMN {ECO:0000256|ARBA:ARBA00022643, ECO:0000256|PIRSR:PIRSR000138-2};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000765}.
FT   DOMAIN          29..406
FT                   /note="FMN hydroxy acid dehydrogenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51349"
FT   ACT_SITE        301
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU00683"
FT   BINDING         55
FT                   /ligand="a 2-oxocarboxylate"
FT                   /ligand_id="ChEBI:CHEBI:35179"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00683"
FT   BINDING         55
FT                   /ligand="glyoxylate"
FT                   /ligand_id="ChEBI:CHEBI:36655"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT   BINDING         108..110
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT   BINDING         137
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2,
FT                   ECO:0000256|PROSITE-ProRule:PRU00683"
FT   BINDING         159
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2,
FT                   ECO:0000256|PROSITE-ProRule:PRU00683"
FT   BINDING         161
FT                   /ligand="a 2-oxocarboxylate"
FT                   /ligand_id="ChEBI:CHEBI:35179"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00683"
FT   BINDING         161
FT                   /ligand="glyoxylate"
FT                   /ligand_id="ChEBI:CHEBI:36655"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT   BINDING         187
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2,
FT                   ECO:0000256|PROSITE-ProRule:PRU00683"
FT   BINDING         196
FT                   /ligand="a 2-oxocarboxylate"
FT                   /ligand_id="ChEBI:CHEBI:35179"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00683"
FT   BINDING         196
FT                   /ligand="glyoxylate"
FT                   /ligand_id="ChEBI:CHEBI:36655"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT   BINDING         277
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2,
FT                   ECO:0000256|PROSITE-ProRule:PRU00683"
FT   BINDING         299
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT   BINDING         301
FT                   /ligand="glyoxylate"
FT                   /ligand_id="ChEBI:CHEBI:36655"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT   BINDING         304
FT                   /ligand="a 2-oxocarboxylate"
FT                   /ligand_id="ChEBI:CHEBI:35179"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00683"
FT   BINDING         304
FT                   /ligand="glyoxylate"
FT                   /ligand_id="ChEBI:CHEBI:36655"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT   BINDING         332..336
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00683"
FT   BINDING         355..356
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2,
FT                   ECO:0000256|PROSITE-ProRule:PRU00683"
SQ   SEQUENCE   414 AA;  45574 MW;  3A6A793FDD46C753 CRC64;
     MAVDRRLPRV GDLAPLMQFK RPQFNRTKRR LETALTIEDL RRVAKRRTPR AAFDYTDGAA
     EDELSIERAR QAFRDIEFHP TILRDVTSVR TGWDVFGKPV ALPFGIAPTG FTRLMHTEGE
     IAGARAAAEA GIPFSMSTLA TCAIEDLQAA VPQGRKWFQL YMWRDRDRSM ALVKRAADAG
     FDTMLVTVDV PVAGARLRDV RNGMSIPPAL TLRTVLDALP HPHWWFDLLT TEPLAFASLD
     RWSGTVGEYL NTMFDPSVTF DDLEWMKAQW PGKLVVKGIQ TLDDARAVVE RGADGIVLSN
     HGGRQLDRAP APFHLLPLVA RELGKDTEIV VDTGIMSGAD IVAAIALGAR CTLIGRAYLY
     GLMAGGEAGV KRAIEILSAG VSRTMRLLGV TCLEELSAKH VTQLQRLGPI PLPT
//