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Database: UniProt
Entry: A0A084VXJ1_ANOSI
LinkDB: A0A084VXJ1_ANOSI
Original site: A0A084VXJ1_ANOSI 
ID   A0A084VXJ1_ANOSI        Unreviewed;       262 AA.
AC   A0A084VXJ1;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 44.
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=ZHAS_00010422 {ECO:0000313|EMBL:KFB42685.1};
OS   Anopheles sinensis (Mosquito).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles.
OX   NCBI_TaxID=74873 {ECO:0000313|EMBL:KFB42685.1};
RN   [1] {ECO:0000313|EMBL:KFB42685.1, ECO:0000313|Proteomes:UP000030765}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=24438588; DOI=10.1186/1471-2164-15-42;
RA   Zhou D., Zhang D., Ding G., Shi L., Hou Q., Ye Y., Xu Y., Zhou H.,
RA   Xiong C., Li S., Yu J., Hong S., Yu X., Zou P., Chen C., Chang X., Wang W.,
RA   Lv Y., Sun Y., Ma L., Shen B., Zhu C.;
RT   "Genome sequence of Anopheles sinensis provides insight into genetics basis
RT   of mosquito competence for malaria parasites.";
RL   BMC Genomics 15:42-42(2014).
RN   [2] {ECO:0000313|EnsemblMetazoa:ASIC010422-PA}
RP   IDENTIFICATION.
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) 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|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; ATLV01018076; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; KE525212; KFB42685.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A084VXJ1; -.
DR   STRING; 74873.A0A084VXJ1; -.
DR   EnsemblMetazoa; ASIC010422-RA; ASIC010422-PA; ASIC010422.
DR   VEuPathDB; VectorBase:ASIC010422; -.
DR   VEuPathDB; VectorBase:ASIS000471; -.
DR   OMA; FDEIMIN; -.
DR   UniPathway; UPA00554; UER00611.
DR   Proteomes; UP000030765; 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   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:RU000496};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030765}.
FT   DOMAIN          14..90
FT                   /note="Lactate/malate dehydrogenase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00056"
FT   DOMAIN          93..259
FT                   /note="Lactate/malate dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02866"
FT   ACT_SITE        123
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-1"
FT   BINDING         43
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         66..68
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
SQ   SEQUENCE   262 AA;  28186 MW;  557D645DE3AFD9D3 CRC64;
     MLKIHLELLI ADFAVSAGSR LIVITAGVRQ KEGESRLDLV QRNTDILKGI IPKLVAQSPD
     CTLLVVSNPV DILTYVAWKL SGLPKNRVIG SGTNLDSSRF RFLMSQKLGV APTSCHGWII
     GEHGDSSVPV WSGVNVAGVR LAEINPDIGT DADVEKWGDL HQQVVNSAYE VIRLKGYTSW
     AIGLSVASLA SAILRNTYNV HAVSTLVSGE HGITDDVYLS LPCVLGRNGV SHVVKQILTP
     EETKKLQASA TLMAQVQAGI KF
//
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