ID LDH6B_MACFA Reviewed; 381 AA.
AC Q4R816;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 24-JAN-2024, entry version 89.
DE RecName: Full=L-lactate dehydrogenase A-like 6B;
DE EC=1.1.1.27;
GN Name=LDHAL6B; ORFNames=QtsA-13749;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
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 -!- PATHWAY: Fermentation; pyruvate fermentation to lactate; (S)-lactate
CC from pyruvate: step 1/1.
CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. LDH family.
CC {ECO:0000305}.
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DR EMBL; AB168645; BAE00756.1; -; mRNA.
DR RefSeq; NP_001271721.1; NM_001284792.1.
DR AlphaFoldDB; Q4R816; -.
DR SMR; Q4R816; -.
DR STRING; 9541.ENSMFAP00000005854; -.
DR eggNOG; KOG1495; Eukaryota.
DR OrthoDB; 5344346at2759; -.
DR UniPathway; UPA00554; UER00611.
DR Proteomes; UP000233100; Unplaced.
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 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 2: Evidence at transcript level;
KW NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..381
FT /note="L-lactate dehydrogenase A-like 6B"
FT /id="PRO_0000261002"
FT ACT_SITE 242
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 101..106
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 148
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 155
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 187
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 187
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 218
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 297
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 381 AA; 42049 MW; 9D394077C58B634F CRC64;
MSWTVPLVRA SQRVSSVGAN FLCLKMALCP RQAARIPLKG AWRFTSVSKM ATVKSELIER
FTSEEPVHHS KVSIIGTGSV GMACAISILL KGLIDELALV DLDEGKLKGE TMDLQHGSSF
TKMPNIVCSK DYFVTANSNL VIITAGARQE KGETRLNLVQ RNVALFKLMI SNIVQHSPHC
KLIIVSNPVD ILSYVAWKLS AFPKNRVIGS GCNLDTARFR FLIGQKLGIH SESCHGWILG
EHGDSSVPVW SGVNIAGVPL KDLNSDIGTD KDPEQWKNVH EEVIATAYEI IKMKGYTSWA
IGLSVADLTE SILKNLRRTH PVSTIIKGLY GIDEEVFLSI PCILGENGIT HLIKIKLTPE
EEDRLKKSAK TLWEIQKELK I
//
