ID   E3D9Q7_GARV3            Unreviewed;       307 AA.
AC   E3D9Q7;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   27-MAR-2024, entry version 64.
DE   SubName: Full=Lactate/malate dehydrogenase, NAD binding domain protein {ECO:0000313|EMBL:ADP38801.1};
GN   OrderedLocusNames=HMPREF0421_20719 {ECO:0000313|EMBL:ADP38801.1};
OS   Gardnerella vaginalis (strain ATCC 14019 / 317).
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Gardnerella.
OX   NCBI_TaxID=525284 {ECO:0000313|EMBL:ADP38801.1, ECO:0000313|Proteomes:UP000001453};
RN   [1] {ECO:0000313|EMBL:ADP38801.1, ECO:0000313|Proteomes:UP000001453}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14019 / 317 {ECO:0000313|Proteomes:UP000001453};
RX   PubMed=20865041; DOI=10.1371/journal.pone.0012411;
RA   Yeoman C.J., Yildirim S., Thomas S.M., Durkin A.S., Torralba M., Sutton G.,
RA   Buhay C.J., Ding Y., Dugan-Rocha S.P., Muzny D.M., Qin X., Gibbs R.A.,
RA   Leigh S.R., Stumpf R., White B.A., Highlander S.K., Nelson K.E.,
RA   Wilson B.A.;
RT   "Comparative genomics of Gardnerella vaginalis strains reveals substantial
RT   differences in metabolic and virulence potential.";
RL   PLoS ONE 5:E12411-E12411(2010).
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily.
CC       {ECO:0000256|RuleBase:RU003369}.
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DR   EMBL; CP002104; ADP38801.1; -; Genomic_DNA.
DR   RefSeq; YP_003985824.1; NC_014644.1.
DR   AlphaFoldDB; E3D9Q7; -.
DR   KEGG; gvg:HMPREF0421_20719; -.
DR   PATRIC; fig|525284.18.peg.714; -.
DR   HOGENOM; CLU_045401_1_2_11; -.
DR   OrthoDB; 9802969at2; -.
DR   Proteomes; UP000001453; Chromosome.
DR   GO; GO:0004459; F:L-lactate dehydrogenase activity; IEA:InterPro.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR   CDD; cd05291; HicDH_like; 1.
DR   Gene3D; 3.90.110.10; Lactate dehydrogenase/glycoside hydrolase, family 4, C-terminal; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR001557; L-lactate/malate_DH.
DR   InterPro; IPR018177; L-lactate_DH_AS.
DR   InterPro; IPR022383; Lactate/malate_DH_C.
DR   InterPro; IPR001236; Lactate/malate_DH_N.
DR   InterPro; IPR015955; Lactate_DH/Glyco_Ohase_4_C.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR43128; L-2-HYDROXYCARBOXYLATE DEHYDROGENASE (NAD(P)(+)); 1.
DR   PANTHER; PTHR43128:SF34; L-LACTATE DEHYDROGENASE; 1.
DR   Pfam; PF02866; Ldh_1_C; 1.
DR   Pfam; PF00056; Ldh_1_N; 1.
DR   PIRSF; PIRSF000102; Lac_mal_DH; 1.
DR   PRINTS; PR00086; LLDHDRGNASE.
DR   SUPFAM; SSF56327; LDH C-terminal domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00064; L_LDH; 1.
PE   3: Inferred from homology;
KW   NAD {ECO:0000256|PIRSR:PIRSR000102-3};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003369}.
FT   DOMAIN          6..147
FT                   /note="Lactate/malate dehydrogenase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00056"
FT   DOMAIN          150..302
FT                   /note="Lactate/malate dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02866"
FT   ACT_SITE        180
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-1"
FT   BINDING         11..16
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         36
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         100
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         123..125
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
SQ   SEQUENCE   307 AA;  33950 MW;  B655C6E44508EF37 CRC64;
     MFHMRKVAVI GMGNVGAAVA HQLIIGGHVD DLYLYDSNEA KVKADALDFE DSMDNVPFNV
     NITVNDYEAL KDVEVIVSAL GHIKLLDVPH PDRFAELKYN RKEVAEVGAK IKASGFHGVL
     IDITNPCDAI CQLYKEATGL PYERVIGTGT LLDSARLHRA VGKFFGVHPK AVKGYSLGEH
     GDSQFVAWST VKVLEQPITD PAEEKNIDLD AVDDETREGG FTVFYGKKYT NYGIAAAAVR
     LVNAVMTDSR EQMPVSNYRE EYHSYLSYPA IVGRDGIIEQ CKLDLTEEEL QKLQHSADTI
     LSKAQME
//