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Database: UniProt
Entry: I0HSG8_RUBGI
LinkDB: I0HSG8_RUBGI
Original site: I0HSG8_RUBGI 
ID   I0HSG8_RUBGI            Unreviewed;       303 AA.
AC   I0HSG8;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   24-JAN-2024, entry version 55.
DE   RecName: Full=L-lactate dehydrogenase {ECO:0000256|ARBA:ARBA00012967};
DE            EC=1.1.1.27 {ECO:0000256|ARBA:ARBA00012967};
GN   Name=ldh {ECO:0000313|EMBL:BAL95955.1};
GN   OrderedLocusNames=RGE_26160 {ECO:0000313|EMBL:BAL95955.1};
OS   Rubrivivax gelatinosus (strain NBRC 100245 / IL144).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Sphaerotilaceae; Rubrivivax.
OX   NCBI_TaxID=983917 {ECO:0000313|EMBL:BAL95955.1, ECO:0000313|Proteomes:UP000007883};
RN   [1] {ECO:0000313|EMBL:BAL95955.1, ECO:0000313|Proteomes:UP000007883}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 100245 / IL144 {ECO:0000313|Proteomes:UP000007883};
RX   PubMed=22689232; DOI=10.1128/JB.00511-12;
RA   Nagashima S., Kamimura A., Shimizu T., Nakamura-isaki S., Aono E.,
RA   Sakamoto K., Ichikawa N., Nakazawa H., Sekine M., Yamazaki S., Fujita N.,
RA   Shimada K., Hanada S., Nagashima K.V.P.;
RT   "Complete genome sequence of phototrophic betaproteobacterium Rubrivivax
RT   gelatinosus IL144.";
RL   J. Bacteriol. 194:3541-3542(2012).
CC   -!- FUNCTION: Catalyzes the reversible oxidation of malate to oxaloacetate.
CC       {ECO:0000256|ARBA:ARBA00003966}.
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:0000256|ARBA:ARBA00001763};
CC   -!- PATHWAY: Fermentation; pyruvate fermentation to lactate; (S)-lactate
CC       from pyruvate: step 1/1. {ECO:0000256|ARBA:ARBA00004843}.
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily. LDH family.
CC       {ECO:0000256|ARBA:ARBA00006054}.
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DR   EMBL; AP012320; BAL95955.1; -; Genomic_DNA.
DR   RefSeq; WP_014428817.1; NC_017075.1.
DR   AlphaFoldDB; I0HSG8; -.
DR   STRING; 983917.RGE_26160; -.
DR   KEGG; rge:RGE_26160; -.
DR   PATRIC; fig|983917.3.peg.2539; -.
DR   eggNOG; COG0039; Bacteria.
DR   HOGENOM; CLU_045401_2_2_4; -.
DR   OMA; ASCAEYI; -.
DR   UniPathway; UPA00554; UER00611.
DR   Proteomes; UP000007883; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0004459; F:L-lactate dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
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; 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   NCBIfam; TIGR01771; L-LDH-NAD; 1.
DR   PANTHER; PTHR43128; L-2-HYDROXYCARBOXYLATE DEHYDROGENASE (NAD(P)(+)); 1.
DR   PANTHER; PTHR43128:SF16; 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|ARBA:ARBA00023027, ECO:0000256|PIRSR:PIRSR000102-3};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003369};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007883}.
FT   DOMAIN          1..137
FT                   /note="Lactate/malate dehydrogenase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00056"
FT   DOMAIN          140..296
FT                   /note="Lactate/malate dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02866"
FT   ACT_SITE        170
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-1"
FT   BINDING         7..12
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         32
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         92
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         113..115
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
SQ   SEQUENCE   303 AA;  32397 MW;  32F2998C1C94F1A1 CRC64;
     MKVGIIGVGY VGASVAVSLL HGGVTRELLL HDRDAARAEG EAMDLAQGAP YYPRATVRAV
     DLDEVSRCDV VVFAAGRNGR PGESRLQLLA DNFRVASEVG RVVGQHAGII VAISNPVDVL
     TRVLQQSSGL PPERVFGTGT MLDTARLRQA LAERLAVDSR SVHAQVLGEH GDSEIVQWSG
     AQVGGRPLRD WPGWTREDEQ RLGHEVKRAA YEIIQRKGVT NHAIGLVTAD LVRAIVRDEH
     RVLTVTRCHT GEGLDGVALS LPAIVGRNGA TTVIPPSLDD DEAQALAHSA QVLRDAWSQL
     APA
//
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