ID A0A0Q9XJ59_DROMO Unreviewed; 1457 AA.
AC A0A0Q9XJ59;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 38.
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 Name=Dmoj\GI26993 {ECO:0000313|EMBL:KRG05106.1};
GN ORFNames=Dmoj_GI26993 {ECO:0000313|EMBL:KRG05106.1};
OS Drosophila mojavensis (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=7230 {ECO:0000313|EMBL:KRG05106.1, ECO:0000313|Proteomes:UP000009192};
RN [1] {ECO:0000313|EMBL:KRG05106.1, ECO:0000313|Proteomes:UP000009192}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 15081-1352.22 {ECO:0000313|Proteomes:UP000009192};
RX PubMed=17994087; DOI=10.1038/nature06341;
RG Drosophila 12 genomes consortium;
RA Clark A.G., Eisen M.B., Smith D.R., Bergman C.M., Oliver B., Markow T.A.,
RA Kaufman T.C., Kellis M., Gelbart W., Iyer V.N., Pollard D.A., Sackton T.B.,
RA Larracuente A.M., Singh N.D., Abad J.P., Abt D.N., Adryan B., Aguade M.,
RA Akashi H., Anderson W.W., Aquadro C.F., Ardell D.H., Arguello R.,
RA Artieri C.G., Barbash D.A., Barker D., Barsanti P., Batterham P.,
RA Batzoglou S., Begun D., Bhutkar A., Blanco E., Bosak S.A., Bradley R.K.,
RA Brand A.D., Brent M.R., Brooks A.N., Brown R.H., Butlin R.K., Caggese C.,
RA Calvi B.R., Bernardo de Carvalho A., Caspi A., Castrezana S.,
RA Celniker S.E., Chang J.L., Chapple C., Chatterji S., Chinwalla A.,
RA Civetta A., Clifton S.W., Comeron J.M., Costello J.C., Coyne J.A., Daub J.,
RA David R.G., Delcher A.L., Delehaunty K., Do C.B., Ebling H., Edwards K.,
RA Eickbush T., Evans J.D., Filipski A., Findeiss S., Freyhult E., Fulton L.,
RA Fulton R., Garcia A.C., Gardiner A., Garfield D.A., Garvin B.E., Gibson G.,
RA Gilbert D., Gnerre S., Godfrey J., Good R., Gotea V., Gravely B.,
RA Greenberg A.J., Griffiths-Jones S., Gross S., Guigo R., Gustafson E.A.,
RA Haerty W., Hahn M.W., Halligan D.L., Halpern A.L., Halter G.M., Han M.V.,
RA Heger A., Hillier L., Hinrichs A.S., Holmes I., Hoskins R.A., Hubisz M.J.,
RA Hultmark D., Huntley M.A., Jaffe D.B., Jagadeeshan S., Jeck W.R.,
RA Johnson J., Jones C.D., Jordan W.C., Karpen G.H., Kataoka E.,
RA Keightley P.D., Kheradpour P., Kirkness E.F., Koerich L.B., Kristiansen K.,
RA Kudrna D., Kulathinal R.J., Kumar S., Kwok R., Lander E., Langley C.H.,
RA Lapoint R., Lazzaro B.P., Lee S.J., Levesque L., Li R., Lin C.F., Lin M.F.,
RA Lindblad-Toh K., Llopart A., Long M., Low L., Lozovsky E., Lu J., Luo M.,
RA Machado C.A., Makalowski W., Marzo M., Matsuda M., Matzkin L.,
RA McAllister B., McBride C.S., McKernan B., McKernan K., Mendez-Lago M.,
RA Minx P., Mollenhauer M.U., Montooth K., Mount S.M., Mu X., Myers E.,
RA Negre B., Newfeld S., Nielsen R., Noor M.A., O'Grady P., Pachter L.,
RA Papaceit M., Parisi M.J., Parisi M., Parts L., Pedersen J.S., Pesole G.,
RA Phillippy A.M., Ponting C.P., Pop M., Porcelli D., Powell J.R.,
RA Prohaska S., Pruitt K., Puig M., Quesneville H., Ram K.R., Rand D.,
RA Rasmussen M.D., Reed L.K., Reenan R., Reily A., Remington K.A.,
RA Rieger T.T., Ritchie M.G., Robin C., Rogers Y.H., Rohde C., Rozas J.,
RA Rubenfield M.J., Ruiz A., Russo S., Salzberg S.L., Sanchez-Gracia A.,
RA Saranga D.J., Sato H., Schaeffer S.W., Schatz M.C., Schlenke T.,
RA Schwartz R., Segarra C., Singh R.S., Sirot L., Sirota M., Sisneros N.B.,
RA Smith C.D., Smith T.F., Spieth J., Stage D.E., Stark A., Stephan W.,
RA Strausberg R.L., Strempel S., Sturgill D., Sutton G., Sutton G.G., Tao W.,
RA Teichmann S., Tobari Y.N., Tomimura Y., Tsolas J.M., Valente V.L.,
RA Venter E., Venter J.C., Vicario S., Vieira F.G., Vilella A.J.,
RA Villasante A., Walenz B., Wang J., Wasserman M., Watts T., Wilson D.,
RA Wilson R.K., Wing R.A., Wolfner M.F., Wong A., Wong G.K., Wu C.I., Wu G.,
RA Yamamoto D., Yang H.P., Yang S.P., Yorke J.A., Yoshida K., Zdobnov E.,
RA Zhang P., Zhang Y., Zimin A.V., Baldwin J., Abdouelleil A., Abdulkadir J.,
RA Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A., An P.,
RA Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P., Barry A.,
RA Bayul T., Berlin A., Bessette D., Bloom T., Blye J., Boguslavskiy L.,
RA Bonnet C., Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S.,
RA Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P., Costello M.,
RA D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C., Dhargay N., Dooley K.,
RA Dooley E., Doricent M., Dorje P., Dorjee K., Dupes A., Elong R., Falk J.,
RA Farina A., Faro S., Ferguson D., Fisher S., Foley C.D., Franke A.,
RA Friedrich D., Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T.,
RA Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B.,
RA Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L.,
RA Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D.,
RA Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F., LeVine R.,
RA Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y.,
RA Lubonja R., Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C.,
RA McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O.,
RA Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A., Mulrain L.,
RA Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N., Nicol R., Norbu C.,
RA Norbu N., Novod N., O'Neill B., Osman S., Markiewicz E., Oyono O.L.,
RA Patti C., Phunkhang P., Pierre F., Priest M., Raghuraman S., Rege F.,
RA Reyes R., Rise C., Rogov P., Ross K., Ryan E., Settipalli S., Shea T.,
RA Sherpa N., Shi L., Shih D., Sparrow T., Spaulding J., Stalker J.,
RA Stange-Thomann N., Stavropoulos S., Stone C., Strader C., Tesfaye S.,
RA Thomson T., Thoulutsang Y., Thoulutsang D., Topham K., Topping I.,
RA Tsamla T., Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M.,
RA Wilkinson J., Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D.,
RA Zimmer A., Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J.,
RA Chin C., Gnerre S., Grabherr M., Kleber M., Mauceli E., MacCallum I.;
RT "Evolution of genes and genomes on the Drosophila phylogeny.";
RL Nature 450:203-218(2007).
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; CH933808; KRG05106.1; -; Genomic_DNA.
DR RefSeq; XP_015019710.1; XM_015164224.1.
DR EnsemblMetazoa; FBtr0430920; FBpp0388249; FBgn0281730.
DR KEGG; dmo:Dmoj_GI26993; -.
DR InParanoid; A0A0Q9XJ59; -.
DR UniPathway; UPA00554; UER00611.
DR Proteomes; UP000009192; Unassembled WGS sequence.
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; 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 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 Coiled coil {ECO:0000256|SAM:Coils}; NAD {ECO:0000256|RuleBase:RU000496};
KW Oxidoreductase {ECO:0000256|RuleBase:RU000496};
KW Reference proteome {ECO:0000313|Proteomes:UP000009192}.
FT DOMAIN 1147..1284
FT /note="Lactate/malate dehydrogenase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00056"
FT DOMAIN 1289..1453
FT /note="Lactate/malate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02866"
FT REGION 176..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 419..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 505..544
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 629..652
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 682..738
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 760..791
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 803..837
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 916..962
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 982..1057
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 70..106
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 382..410
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 176..193
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..261
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1457 AA; 168809 MW; 7FC632451F59CA7A CRC64;
MSFNRFTSVC MRKSILRSIF ILTGCLDCMH STKLPIKYTP CVSYSKKSDS ASGSSDDCQK
NPCDLYSKIL DKKEKEIERN EAACRKLKEE QQLKQYEENC LIAQRRRLAE EMQCMDQKDK
IALEGMMSCL TRGMRKACKK LAHRKLRNDK ELEQKCAVLI KAAKIKKILK QCDKRRMNTK
SAGDKNKEDS EKKLKKKCKK KKGKTGEPKA EQRCKDSNEQ KDKKKKCPTE KKSKSNSVKE
EKKEKAECNK VDKQKPRNED SDPIETICTS LCRNGKIADA STNPQNKYLI KLEKCIRKEW
SDICKCRETL SKREKIQLAR SHKYLSAHIK EQCRKKVLAE MCAAIKTTCS KDKAAKSKTC
KESATAKKKE PNTDICEEIC ENKELQKEIM EAKREEDEFI KSEIEKLKKK CLEKACKKVD
EKGEEKKTPN KKTKECAPKK KCEKEKQEQQ RKQCEEQKKR QEEVAEKKKC EELAIKEKCE
SLKKKLQEDA IRKKCAMMRM RAVIEKKKEK EEAQKRECEK LKKQKESEGK KKESLKNKCE
QNKKNQEIAE KKEREAEILH QKCEALIKKI EQQIQSVTEK SKAGKASTKV CEAEVDKKQA
DDKKLKEKCE EEALKEKCKA LKKKLQDGIK RKCPGEKHSH EDKAQSKEEK KCKEIDLEGK
CKALKQKLEE DALRIKCAMK KMRDHAEKEK QNKEAEKKKC ENAQKKDQEE AQRKKCEEAK
KQKEEQKKKD EAARCEDLKK KQEEDALRLK CAMKKMREKL EKKKKEEALR KKCEEEKKQK
EKCEDLKKKE EEDAIRAKCA MKKMQDALEK KQKEEAQRKK CEEERKQKEK KRKEEEECEA
LKKKQEEDAI RAKCVMKKIK EELEKKAKEE ALRKKCEEEK KEKEKKRKEE EKCEALKKKQ
EEDAIRAKCA MKKMQEAIEK KEKEEAQRKK CEEEKKRKEA EERKKKEEEK CEALKKKQEE
DAIKAKCAMK KIQEAIAKKE KEEAARKCEE EKKRKEAEEK KRKEEERCQA LKKKQEEDAI
KAKCAMQEAL AKKKKEEAQS KKCEEEKKQR GAQEKEKKEE TSKAKCDFLK KLEEQDVIKK
KCAIRKIRDA IGKKQEDVIR QKCAMKKLRE QEEKERKENE ARRAKAILFR STLYRTNCKQ
DFQAGNKVSI VGAGPVGMGC AFALLTKRVT NNIAIYDVKN DLSSAQRNDL RHASLFLQNC
NIDNSSTIEC TKNSRVVVIA ARPSSKPNES CQDQLLRSAD MIKQIVPELL KLSPKAVFIV
VSSPVDVMAW VARKITNLPY ERCFSTGCHL DTARFRMFIA QLVGVSTSSV QGMVLGEHGD
TSVPIWSSVS VGGTLLKDLL PPIGTDKDPM VWSNVHKSVV NAAYKVIAGK NYTNWAIGLT
VSDVVSAIFE NSNRILSLST NAKGMCGVKD EIFLSLPCIV NQWGIYGVLH PQLSDWEKDK
FKMSAAKLLN TQNSIKL
//
