LDH_STAHJ
ID LDH_STAHJ Reviewed; 318 AA.
AC Q4L941;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 131.
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}; OrderedLocusNames=SH0525;
OS Staphylococcus haemolyticus (strain JCSC1435).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=279808;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCSC1435;
RX PubMed=16237012; DOI=10.1128/jb.187.21.7292-7308.2005;
RA Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y.,
RA Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C.,
RA Hiramatsu K.;
RT "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the
RT extreme plasticity of its genome and the evolution of human-colonizing
RT staphylococcal species.";
RL J. Bacteriol. 187:7292-7308(2005).
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}.
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DR EMBL; AP006716; BAE03834.1; -; Genomic_DNA.
DR RefSeq; WP_011274850.1; NC_007168.1.
DR AlphaFoldDB; Q4L941; -.
DR SMR; Q4L941; -.
DR STRING; 279808.SH0525; -.
DR EnsemblBacteria; BAE03834; BAE03834; SH0525.
DR GeneID; 58063282; -.
DR KEGG; sha:SH0525; -.
DR eggNOG; COG0039; Bacteria.
DR HOGENOM; CLU_045401_1_1_9; -.
DR OMA; AWSHVTI; -.
DR OrthoDB; 870724at2; -.
DR UniPathway; UPA00554; UER00611.
DR Proteomes; UP000000543; 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; 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 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.
DR TIGRFAMs; TIGR01771; L-LDH-NAD; 1.
DR PROSITE; PS00064; L_LDH; 1.
PE 3: Inferred from homology;
KW Cytoplasm; NAD; Oxidoreductase; Phosphoprotein.
FT CHAIN 1..318
FT /note="L-lactate dehydrogenase"
FT /id="PRO_0000237561"
FT ACT_SITE 176
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT BINDING 14
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT BINDING 35
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT BINDING 40
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT BINDING 66
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT BINDING 89
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT BINDING 121..124
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT BINDING 144
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT BINDING 149..152
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT BINDING 229
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT MOD_RES 220
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
SQ SEQUENCE 318 AA; 35101 MW; CDBFB085705FE926 CRC64;
MARHKIVLIG SGYVGSAFAH AIVAKGLVDE MAIIDIDEDK AKADVWDLNH ATPFGDNFVN
VHVGQYEDFK DADIVVICAS AKLAKGETRL KLLEDNVDIF VPMIQRIVDS GFDGYFVLPS
NPVDIMSYVV KRVSNFPKNK IIGSGTSLDT ARFQFFLSRE FDVAPNQVYA PIIGEHGDSQ
VAVWSHAQIA GEPVLDLLPS NTNLEAFKTS ISNRTTQIGY DIYVRKGTTN FGISLSLVRI
VEAILFNKNI IMNVSSYVEG EYGLSDVYIG VPTVINRNGA DRIIELALSK EELSQLHHSA
DIILDYQRQA DAIIDQMC
