ID A0A2I2YN53_GORGO Unreviewed; 332 AA.
AC A0A2I2YN53;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=L-lactate dehydrogenase {ECO:0000256|RuleBase:RU000496};
DE EC=1.1.1.27 {ECO:0000256|RuleBase:RU000496};
GN Name=LDHC {ECO:0000313|Ensembl:ENSGGOP00000036371.1};
OS Gorilla gorilla gorilla (Western lowland gorilla).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Gorilla.
OX NCBI_TaxID=9595 {ECO:0000313|Ensembl:ENSGGOP00000036371.1, ECO:0000313|Proteomes:UP000001519};
RN [1] {ECO:0000313|Ensembl:ENSGGOP00000036371.1, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Scally A.;
RT "Insights into the evolution of the great apes provided by the gorilla
RT genome.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGGOP00000036371.1, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22398555; DOI=10.1038/nature10842;
RA Scally A., Dutheil J.Y., Hillier L.W., Jordan G.E., Goodhead I.,
RA Herrero J., Hobolth A., Lappalainen T., Mailund T., Marques-Bonet T.,
RA McCarthy S., Montgomery S.H., Schwalie P.C., Tang Y.A., Ward M.C., Xue Y.,
RA Yngvadottir B., Alkan C., Andersen L.N., Ayub Q., Ball E.V., Beal K.,
RA Bradley B.J., Chen Y., Clee C.M., Fitzgerald S., Graves T.A., Gu Y.,
RA Heath P., Heger A., Karakoc E., Kolb-Kokocinski A., Laird G.K., Lunter G.,
RA Meader S., Mort M., Mullikin J.C., Munch K., O'Connor T.D., Phillips A.D.,
RA Prado-Martinez J., Rogers A.S., Sajjadian S., Schmidt D., Shaw K.,
RA Simpson J.T., Stenson P.D., Turner D.J., Vigilant L., Vilella A.J.,
RA Whitener W., Zhu B., Cooper D.N., de Jong P., Dermitzakis E.T.,
RA Eichler E.E., Flicek P., Goldman N., Mundy N.I., Ning Z., Odom D.T.,
RA Ponting C.P., Quail M.A., Ryder O.A., Searle S.M., Warren W.C.,
RA Wilson R.K., Schierup M.H., Rogers J., Tyler-Smith C., Durbin R.;
RT "Insights into hominid evolution from the gorilla genome sequence.";
RL Nature 483:169-175(2012).
RN [3] {ECO:0000313|Ensembl:ENSGGOP00000036371.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Possible role in sperm motility.
CC {ECO:0000256|ARBA:ARBA00037359}.
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 -!- SUBUNIT: Homotetramer. Interacts with RABL2/RABL2A; binds
CC preferentially to GTP-bound RABL2. {ECO:0000256|ARBA:ARBA00038717}.
CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. LDH family.
CC {ECO:0000256|ARBA:ARBA00006054}.
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DR EMBL; CABD030077710; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030077711; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_004050839.1; XM_004050791.2.
DR RefSeq; XP_004050840.1; XM_004050792.2.
DR AlphaFoldDB; A0A2I2YN53; -.
DR STRING; 9593.ENSGGOP00000036371; -.
DR Ensembl; ENSGGOT00000055206.1; ENSGGOP00000036371.1; ENSGGOG00000015884.3.
DR GeneID; 101138644; -.
DR KEGG; ggo:101138644; -.
DR CTD; 3948; -.
DR GeneTree; ENSGT00940000161479; -.
DR InParanoid; A0A2I2YN53; -.
DR OMA; HFSTIVG; -.
DR OrthoDB; 5344346at2759; -.
DR UniPathway; UPA00554; UER00611.
DR Proteomes; UP000001519; Chromosome 11.
DR Bgee; ENSGGOG00000015884; Expressed in testis and 6 other cell types or tissues.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0031514; C:motile cilium; IEA:Ensembl.
DR GO; GO:0004459; F:L-lactate dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0006754; P:ATP biosynthetic process; IEA:Ensembl.
DR GO; GO:0030317; P:flagellated sperm motility; IEA:Ensembl.
DR GO; GO:0019244; P:lactate biosynthetic process from pyruvate; IEA:Ensembl.
DR GO; GO:0006089; P:lactate metabolic process; IBA:GO_Central.
DR GO; GO:0019516; P:lactate oxidation; IEA:Ensembl.
DR GO; GO:0042867; P:pyruvate catabolic process; IEA:Ensembl.
DR GO; GO:0006090; P:pyruvate metabolic process; IBA:GO_Central.
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:SF5; L-LACTATE DEHYDROGENASE C CHAIN; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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:UP000001519}.
FT DOMAIN 21..160
FT /note="Lactate/malate dehydrogenase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00056"
FT DOMAIN 164..327
FT /note="Lactate/malate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02866"
FT ACT_SITE 193
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-1"
FT BINDING 27..32
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 52
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 113
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 136..138
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
SQ SEQUENCE 332 AA; 36311 MW; 9E40048DDA7FB7EE CRC64;
MSTVKEQLIE KLIEDDKDSQ CKITIVGTGA VGMACAISIL LKDLADELAL VDVALDKLKG
EMMDLQHGSL FFSTSKITSG KDYSVSANSR IVIVTAGARQ QEGETRLALV QRNVAIMKSI
IPAIVHYSPD CKILVVSNPV DILTYIVWKI SGLPVTRVIG SGCNLDSARF RYLIGEKLGV
HPTSCHGWII GEHGDSSVPL WSGVNVAGVA LKTLDPKLGT DSDKEHWKNI HKQVIQSAYE
IIKLKGYTSW AIGLSVMDLV GSILKNLRRV HPVSTMVKGL YGIKEELFLS IPCVLGRNGV
SDVVKINLNS EEEALFKKSA ETLWNIQKDL IF
//
