ID H2NND7_PONAB Unreviewed; 381 AA.
AC H2NND7; A0A2J8VCE5; A0A6D2XFN4;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=L-lactate dehydrogenase {ECO:0000256|ARBA:ARBA00012967, ECO:0000256|RuleBase:RU000496};
DE EC=1.1.1.27 {ECO:0000256|ARBA:ARBA00012967, ECO:0000256|RuleBase:RU000496};
GN Name=LDHAL6B {ECO:0000313|Ensembl:ENSPPYP00000007393.1};
GN ORFNames=CR201_G0020330 {ECO:0000313|EMBL:PNJ55188.1};
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601 {ECO:0000313|Ensembl:ENSPPYP00000007393.1, ECO:0000313|Proteomes:UP000001595};
RN [1] {ECO:0000313|Ensembl:ENSPPYP00000007393.1, ECO:0000313|Proteomes:UP000001595}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Wilson R.K., Mardis E.;
RT "A 6x draft sequence assembly of the Pongo pygmaeus abelii genome.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PNJ55188.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Susie {ECO:0000313|EMBL:PNJ55188.1};
RA Pollen A., Hastie A., Hormozdiari F., Dougherty M., Liu R., Chaisson M.,
RA Hoppe E., Hill C., Pang A., Hillier L., Baker C., Armstrong J.,
RA Shendure J., Paten B., Wilson R., Chao H., Schneider V., Ventura M.,
RA Kronenberg Z., Murali S., Gordon D., Cantsilieris S., Munson K., Nelson B.,
RA Raja A., Underwood J., Diekhans M., Fiddes I., Haussler D., Eichler E.;
RT "High-resolution comparative analysis of great ape genomes.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSPPYP00000007393.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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|RuleBase:RU000496};
CC -!- PATHWAY: Fermentation; pyruvate fermentation to lactate; (S)-lactate
CC from pyruvate: step 1/1. {ECO:0000256|ARBA:ARBA00004843,
CC ECO:0000256|RuleBase:RU000496}.
CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. LDH family.
CC {ECO:0000256|ARBA:ARBA00006054}.
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DR EMBL; NDHI03003424; PNJ55188.1; -; Genomic_DNA.
DR RefSeq; XP_002825550.1; XM_002825504.3.
DR STRING; 9601.ENSPPYP00000007393; -.
DR Ensembl; ENSPPYT00000007697.2; ENSPPYP00000007393.1; ENSPPYG00000006520.2.
DR GeneID; 100439283; -.
DR KEGG; pon:100439283; -.
DR CTD; 92483; -.
DR eggNOG; KOG1495; Eukaryota.
DR GeneTree; ENSGT00940000163242; -.
DR HOGENOM; CLU_045401_0_2_1; -.
DR OMA; RVIGNGC; -.
DR OrthoDB; 5344346at2759; -.
DR TreeFam; TF314963; -.
DR UniPathway; UPA00554; UER00611.
DR Proteomes; UP000001595; Chromosome 15.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0004459; F:L-lactate dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0006089; P:lactate metabolic process; IEA:Ensembl.
DR GO; GO:0006090; P:pyruvate metabolic process; IEA:Ensembl.
DR CDD; cd05293; LDH_1; 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 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 NCBIfam; TIGR01771; L-LDH-NAD; 1.
DR PANTHER; PTHR43128; L-2-HYDROXYCARBOXYLATE DEHYDROGENASE (NAD(P)(+)); 1.
DR PANTHER; PTHR43128:SF8; L-LACTATE DEHYDROGENASE A-LIKE 6B; 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|RuleBase:RU000496};
KW Reference proteome {ECO:0000313|Proteomes:UP000001595}.
FT DOMAIN 71..209
FT /note="Lactate/malate dehydrogenase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00056"
FT DOMAIN 213..377
FT /note="Lactate/malate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02866"
FT ACT_SITE 242
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-1"
FT BINDING 76..81
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 101
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 162
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 185..187
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
SQ SEQUENCE 381 AA; 41835 MW; 03E9A7B80ACD053D CRC64;
MSWTVPAVRA SQRVSSVGAN FLCLGTALCP RQAARIPLKG AWLFTPVSKM ATVKSELIER
FTSEEPVHHS KVSIIGTGSV GMACAISILL KGLSDELALV DLDEDKLKGE TVDLQHGSPF
TKMPNIVCSK DYFVTANSNL VIITAGARQE KGETRLNLVQ RNVAIFKLMI SSIVQYSPHC
KLIIVSNPVD ILTYVAWKLS AFPKNRIIGS GCNLDTARFR FLIGQKLGIH SESCHGWILG
EHGDSSVPVW SGVNIAGVPL KDLNSDIGTD KDPEQWKNVH KEVIATAYEI IKMKGYTSWA
IGLSVADLTE SILKNLRRIH PVSTIIKGLY GIDEEVFLSI PCILGENGIT NLIKIKLTPE
EEAHLKKSAK TLWEIQKELK L
//
