ID   LLDD_MYCTO              Reviewed;         414 AA.
AC   P9WND4; L0T848; P95143; Q7D7V5;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 37.
DE   RecName: Full=Putative L-lactate dehydrogenase;
DE            EC=1.1.-.-;
GN   Name=lldD; Synonyms=lldD2; OrderedLocusNames=MT1921;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-lactate + A = AH2 + pyruvate; Xref=Rhea:RHEA:45816,
CC         ChEBI:CHEBI:13193, ChEBI:CHEBI:15361, ChEBI:CHEBI:16651,
CC         ChEBI:CHEBI:17499;
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU00683};
CC   -!- SIMILARITY: Belongs to the FMN-dependent alpha-hydroxy acid
CC       dehydrogenase family. {ECO:0000255|PROSITE-ProRule:PRU00683}.
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DR   EMBL; AE000516; AAK46192.1; -; Genomic_DNA.
DR   PIR; H70667; H70667.
DR   RefSeq; WP_003899057.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WND4; -.
DR   SMR; P9WND4; -.
DR   EnsemblBacteria; AAK46192; AAK46192; MT1921.
DR   KEGG; mtc:MT1921; -.
DR   PATRIC; fig|83331.31.peg.2067; -.
DR   HOGENOM; CLU_020639_6_1_11; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   CDD; cd02809; alpha_hydroxyacid_oxid_FMN; 1.
DR   Gene3D; 3.20.20.70; -; 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   Pfam; PF01070; FMN_dh; 1.
DR   PIRSF; PIRSF000138; Al-hdrx_acd_dh; 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; FMN; Oxidoreductase.
FT   CHAIN           1..414
FT                   /note="Putative L-lactate dehydrogenase"
FT                   /id="PRO_0000427146"
FT   DOMAIN          29..406
FT                   /note="FMN hydroxy acid dehydrogenase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00683"
FT   ACT_SITE        301
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00683"
FT   BINDING         55
FT                   /ligand="a 2-oxocarboxylate"
FT                   /ligand_id="ChEBI:CHEBI:35179"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00683"
FT   BINDING         137
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00683"
FT   BINDING         159
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00683"
FT   BINDING         161
FT                   /ligand="a 2-oxocarboxylate"
FT                   /ligand_id="ChEBI:CHEBI:35179"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00683"
FT   BINDING         187
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00683"
FT   BINDING         196
FT                   /ligand="a 2-oxocarboxylate"
FT                   /ligand_id="ChEBI:CHEBI:35179"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00683"
FT   BINDING         277
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00683"
FT   BINDING         304
FT                   /ligand="a 2-oxocarboxylate"
FT                   /ligand_id="ChEBI:CHEBI:35179"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00683"
FT   BINDING         332..336
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00683"
FT   BINDING         355..356
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00683"
SQ   SEQUENCE   414 AA;  45342 MW;  2EA6FA4B2B89C366 CRC64;
     MAVNRRVPRV RDLAPLLQFN RPQFDTSKRR LGAALTIQDL RRIAKRRTPR AAFDYADGGA
     EDELSIARAR QGFRDIEFHP TILRDVTTVC AGWNVLGQPT VLPFGIAPTG FTRLMHTEGE
     IAGARAAAAA GIPFSLSTLA TCAIEDLVIA VPQGRKWFQL YMWRDRDRSM ALVRRVAAAG
     FDTMLVTVDV PVAGARLRDV RNGMSIPPAL TLRTVLDAMG HPRWWFDLLT TEPLAFASLD
     RWPGTVGEYL NTVFDPSLTF DDLAWIKSQW PGKLVVKGIQ TLDDARAVVD RGVDGIVLSN
     HGGRQLDRAP VPFHLLPHVA RELGKHTEIL VDTGIMSGAD IVAAIALGAR CTLIGRAYLY
     GLMAGGEAGV NRAIEILQTG VIRTMRLLGV TCLEELSPRH VTQLRRLGPI GAPT