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LDH_DROME
ID   LDH_DROME               Reviewed;         332 AA.
AC   Q95028; Q9VRW6;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 173.
DE   RecName: Full=L-lactate dehydrogenase {ECO:0000312|FlyBase:FBgn0001258};
DE            EC=1.1.1.27;
GN   Name=Ldh {ECO:0000312|FlyBase:FBgn0001258};
GN   Synonyms=Imp-L3 {ECO:0000303|PubMed:9094207},
GN   ImpL3 {ECO:0000312|FlyBase:FBgn0001258};
GN   ORFNames=CG10160 {ECO:0000312|FlyBase:FBgn0001258};
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Oregon-R;
RX   PubMed=9094207;
RX   DOI=10.1002/(sici)1520-6408(1997)20:1<11::aid-dvg2>3.0.co;2-c;
RA   Abu-Shumays R.L., Fristrom J.W.;
RT   "IMP-L3, A 20-hydroxyecdysone-responsive gene encodes Drosophila lactate
RT   dehydrogenase: structural characterization and developmental studies.";
RL   Dev. Genet. 20:11-22(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
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   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily. LDH family.
CC       {ECO:0000305}.
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DR   EMBL; U68038; AAB07594.1; -; mRNA.
DR   EMBL; AE014296; AAF50666.1; -; Genomic_DNA.
DR   RefSeq; NP_001261474.1; NM_001274545.2.
DR   RefSeq; NP_001261475.1; NM_001274546.1.
DR   RefSeq; NP_001261476.1; NM_001274547.1.
DR   RefSeq; NP_476581.1; NM_057233.5.
DR   AlphaFoldDB; Q95028; -.
DR   SMR; Q95028; -.
DR   BioGRID; 69949; 65.
DR   DIP; DIP-17530N; -.
DR   IntAct; Q95028; 3.
DR   STRING; 7227.FBpp0304375; -.
DR   PaxDb; Q95028; -.
DR   PRIDE; Q95028; -.
DR   DNASU; 45880; -.
DR   EnsemblMetazoa; FBtr0077008; FBpp0076716; FBgn0001258.
DR   EnsemblMetazoa; FBtr0332065; FBpp0304375; FBgn0001258.
DR   EnsemblMetazoa; FBtr0332066; FBpp0304376; FBgn0001258.
DR   EnsemblMetazoa; FBtr0332067; FBpp0304377; FBgn0001258.
DR   GeneID; 45880; -.
DR   KEGG; dme:Dmel_CG10160; -.
DR   CTD; 45880; -.
DR   FlyBase; FBgn0001258; Ldh.
DR   VEuPathDB; VectorBase:FBgn0001258; -.
DR   eggNOG; KOG1495; Eukaryota.
DR   GeneTree; ENSGT00940000164122; -.
DR   HOGENOM; CLU_045401_0_2_1; -.
DR   InParanoid; Q95028; -.
DR   OMA; ASCAEYI; -.
DR   OrthoDB; 1204514at2759; -.
DR   PhylomeDB; Q95028; -.
DR   Reactome; R-DME-70268; Pyruvate metabolism.
DR   SignaLink; Q95028; -.
DR   UniPathway; UPA00554; UER00611.
DR   BioGRID-ORCS; 45880; 0 hits in 3 CRISPR screens.
DR   GenomeRNAi; 45880; -.
DR   PRO; PR:Q95028; -.
DR   Proteomes; UP000000803; Chromosome 3L.
DR   Bgee; FBgn0001258; Expressed in seminal fluid secreting gland and 30 other tissues.
DR   ExpressionAtlas; Q95028; baseline and differential.
DR   Genevisible; Q95028; DM.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004459; F:L-lactate dehydrogenase activity; IBA:GO_Central.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR   Gene3D; 3.90.110.10; -; 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   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; SSF51735; SSF51735; 1.
DR   SUPFAM; SSF56327; SSF56327; 1.
DR   TIGRFAMs; TIGR01771; L-LDH-NAD; 1.
DR   PROSITE; PS00064; L_LDH; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; NAD; Oxidoreductase; Reference proteome.
FT   CHAIN           1..332
FT                   /note="L-lactate dehydrogenase"
FT                   /id="PRO_0000168494"
FT   ACT_SITE        193
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         29..57
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         99
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         106
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         138
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         138
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         169
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         248
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   332 AA;  35537 MW;  E49F1EE2399440F1 CRC64;
     MAAIKDSLLA QVAEVLPSSG HKVTIVGIGQ VGMASAFSIL AQNVSKEVCL IDVCADKLQG
     ELMDLQHGSN FLKNPQITAS TDFAASANSR LCIVTAGVRQ KEGESRLSLV QRNTDILKNI
     IPKLVEYSPD TILLMVSNPV DIMTYVAWKL SGLPKNRVIG SGTNLDSSRF RFLMSQRLGV
     APTSCHGWII GEHGDSSVPV WSGVNIAGVR LRELNPILGT GEDPEKWNEL HKQVVDSAYE
     VIKLKGYTSW AIGLSTASLA SAILRNTSSV AAVSTSVLGE HGIDKDVFLS LPCVLNANGV
     TSVVKQILTP TEVEQLQKSA NIMSDVQAGL KF
 
 
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