LDH_MYCGA
ID LDH_MYCGA Reviewed; 323 AA.
AC O52354;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 15-AUG-2003, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=L-lactate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00488};
DE Short=L-LDH {ECO:0000255|HAMAP-Rule:MF_00488};
DE EC=1.1.1.27 {ECO:0000255|HAMAP-Rule:MF_00488};
GN Name=ldh {ECO:0000255|HAMAP-Rule:MF_00488}; Synonyms=mdh;
GN OrderedLocusNames=MYCGA0730; ORFNames=MGA_0746;
OS Mycoplasma gallisepticum (strain R(low / passage 15 / clone 2))
OS (Mycoplasmoides gallisepticum).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=710127;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=A5969Var.B;
RX PubMed=10867916;
RA Skamrov A.V., Gol'dman M.A., Feoktistova E.S., Bibilashvili R.S.;
RT "Determination and analysis of the nucleotide sequence of a segment of a
RT Mycoplasma gallisepticum strain A5969 chromosome, containing operons S10
RT and rrn23-5.";
RL Mol. Biol. (Mosk.) 34:390-396(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R(low / passage 15 / clone 2);
RX PubMed=12949158; DOI=10.1099/mic.0.26427-0;
RA Papazisi L., Gorton T.S., Kutish G., Markham P.F., Browning G.F.,
RA Nguyen D.K., Swartzell S., Madan A., Mahairas G., Geary S.J.;
RT "The complete genome sequence of the avian pathogen Mycoplasma
RT gallisepticum strain R(low).";
RL Microbiology 149:2307-2316(2003).
CC -!- FUNCTION: Catalyzes the conversion of lactate to pyruvate.
CC {ECO:0000255|HAMAP-Rule:MF_00488}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-lactate + NAD(+) = H(+) + NADH + pyruvate;
CC Xref=Rhea:RHEA:23444, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16651, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.27;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00488};
CC -!- PATHWAY: Fermentation; pyruvate fermentation to lactate; (S)-lactate
CC from pyruvate: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00488}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00488}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00488}.
CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. LDH family.
CC {ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000305}.
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DR EMBL; AF036708; AAB95409.1; -; Genomic_DNA.
DR EMBL; AE015450; AAP56423.1; -; Genomic_DNA.
DR RefSeq; WP_011113302.1; NC_004829.2.
DR AlphaFoldDB; O52354; -.
DR SMR; O52354; -.
DR KEGG; mga:MGA_0746; -.
DR PATRIC; fig|233150.7.peg.77; -.
DR HOGENOM; CLU_045401_1_2_14; -.
DR OMA; ASCAEYI; -.
DR OrthoDB; 870724at2; -.
DR UniPathway; UPA00554; UER00611.
DR Proteomes; UP000001418; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004459; F:L-lactate dehydrogenase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.90.110.10; -; 1.
DR HAMAP; MF_00488; Lactate_dehydrog; 1.
DR InterPro; IPR001557; L-lactate/malate_DH.
DR InterPro; IPR011304; L-lactate_DH.
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 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; SSF51735; SSF51735; 1.
DR SUPFAM; SSF56327; SSF56327; 1.
PE 3: Inferred from homology;
KW Cytoplasm; NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..323
FT /note="L-lactate dehydrogenase"
FT /id="PRO_0000168367"
FT ACT_SITE 181
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT BINDING 12
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT BINDING 33
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT BINDING 65
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT BINDING 94
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT BINDING 126..129
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT BINDING 149
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT BINDING 154..157
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT BINDING 234
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT CONFLICT 218
FT /note="S -> P (in Ref. 1; AAB95409)"
FT /evidence="ECO:0000305"
FT CONFLICT 255
FT /note="T -> M (in Ref. 1; AAB95409)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 323 AA; 35372 MW; 6831D412F214C5E3 CRC64;
MKKIAVIGCG FVGSTYILDL LQQGVQADYL LVDKNTNLAD GHVRDLRDSK SLKSHNGSTF
NVGTYDDLKD ADVVAITASI PTVPTADGEV FTDRLQLMTA NVKILNEIAL ELKRVGFKGL
SIIPTNPCDV MAGVYQKVTG FDPHKIISTG CQLETMRTRK MISEALGVNS DSVEGFVVGE
HGSGAIVPWS VFRVGNVPMK QLIAEGKIKE EYVKDIFSRV VKEAFEIIKF KKATYFGIAE
SMSLITRAYI YNLNTVLGVG VQLDDKYVAS GIYFTVPAVV GKHGWKLHSK LQLSQEEQAA
FDKSALNIQK VTKDALDLIG FKN
