ID E2AWN1_CAMFO Unreviewed; 407 AA.
AC E2AWN1;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 24-JAN-2024, entry version 57.
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 ORFNames=EAG_12308 {ECO:0000313|EMBL:EFN62195.1};
OS Camponotus floridanus (Florida carpenter ant).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Formicinae; Camponotus.
OX NCBI_TaxID=104421 {ECO:0000313|Proteomes:UP000000311};
RN [1] {ECO:0000313|EMBL:EFN62195.1, ECO:0000313|Proteomes:UP000000311}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C129 {ECO:0000313|Proteomes:UP000000311};
RX PubMed=20798317; DOI=10.1126/science.1192428;
RA Bonasio R., Zhang G., Ye C., Mutti N.S., Fang X., Qin N., Donahue G.,
RA Yang P., Li Q., Li C., Zhang P., Huang Z., Berger S.L., Reinberg D.,
RA Wang J., Liebig J.;
RT "Genomic comparison of the ants Camponotus floridanus and Harpegnathos
RT saltator.";
RL Science 329:1068-1071(2010).
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 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; GL443346; EFN62195.1; -; Genomic_DNA.
DR RefSeq; XP_011265345.2; XM_011267043.2.
DR AlphaFoldDB; E2AWN1; -.
DR STRING; 104421.E2AWN1; -.
DR EnsemblMetazoa; XM_011267043.2; XP_011265345.2; LOC105256807.
DR GeneID; 105256807; -.
DR InParanoid; E2AWN1; -.
DR OMA; DCCHKVT; -.
DR OrthoDB; 5344346at2759; -.
DR UniPathway; UPA00554; UER00611.
DR Proteomes; UP000000311; Unassembled WGS sequence.
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 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 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|RuleBase:RU000496};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU000496};
KW Reference proteome {ECO:0000313|Proteomes:UP000000311}.
FT DOMAIN 95..233
FT /note="Lactate/malate dehydrogenase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00056"
FT DOMAIN 236..396
FT /note="Lactate/malate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02866"
SQ SEQUENCE 407 AA; 44566 MW; 217649411A58FBFE CRC64;
MVLSSILSKS TLSICLKNLI RVTSIAAIDS IRSQYTRALP PTVLTKIFGS NRGKPFGKDA
TAGSDLQRAV NFVSPCLREE LLCKTSEPVR DCCHKVTIVG AGMVGVAIAN SLLFQRITSH
IAMVDAFPKK LEGEGMDFVH SSIFIGDPKI EYDTDFCVTS NSKVVALCAG VRPIKGESRL
DLVQRNTEIL KNIIPSLVNY SPNAVFVIIS NPVDILAWVT WKLSGLPVHQ VIGSGTHLDS
ARFRYLIADR LGIAPSSVQG LIIGEHGDSM VPLWSGVNVA GVQFRDIIPN IGLETDDERW
HEIVKEVVKL GPMVRCLKGY SNTAIGLSAV DIIIAILRNT QAIIPVSTLV QGHHDVRHEM
FLSLPCTIGE NGITNIIRMH MTEYEKKLFQ VSANAVYDIQ KKINIKT
//