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Database: UniProt
Entry: Q4Q396_LEIMA
LinkDB: Q4Q396_LEIMA
Original site: Q4Q396_LEIMA 
ID   Q4Q396_LEIMA            Unreviewed;      1436 AA.
AC   Q4Q396;
DT   19-JUL-2005, integrated into UniProtKB/TrEMBL.
DT   19-JUL-2005, sequence version 1.
DT   27-MAR-2024, entry version 84.
DE   SubName: Full=Dihydroxyacetonephosphate acyltransferase {ECO:0000313|EMBL:CAJ07816.1};
DE            EC=2.3.1.42 {ECO:0000313|EMBL:CAJ07816.1};
GN   Name=DAT {ECO:0000313|EMBL:CAJ07816.1};
GN   ORFNames=LMJF_34_1090 {ECO:0000313|EMBL:CAJ07816.1};
OS   Leishmania major.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX   NCBI_TaxID=5664 {ECO:0000313|EMBL:CAJ07816.1, ECO:0000313|Proteomes:UP000000542};
RN   [1] {ECO:0000313|EMBL:CAJ07816.1, ECO:0000313|Proteomes:UP000000542}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MHOM/IL/81/Friedlin {ECO:0000313|Proteomes:UP000000542};
RX   PubMed=16020728; DOI=10.1126/science.1112680;
RA   Ivens A.C., Peacock C.S., Worthey E.A., Murphy L., Aggarwal G.,
RA   Berriman M., Sisk E., Rajandream M.A., Adlem E., Aert R., Anupama A.,
RA   Apostolou Z., Attipoe P., Bason N., Bauser C., Beck A., Beverley S.M.,
RA   Bianchettin G., Borzym K., Bothe G., Bruschi C.V., Collins M., Cadag E.,
RA   Ciarloni L., Clayton C., Coulson R.M., Cronin A., Cruz A.K., Davies R.M.,
RA   De Gaudenzi J., Dobson D.E., Duesterhoeft A., Fazelina G., Fosker N.,
RA   Frasch A.C., Fraser A., Fuchs M., Gabel C., Goble A., Goffeau A.,
RA   Harris D., Hertz-Fowler C., Hilbert H., Horn D., Huang Y., Klages S.,
RA   Knights A., Kube M., Larke N., Litvin L., Lord A., Louie T., Marra M.,
RA   Masuy D., Matthews K., Michaeli S., Mottram J.C., Muller-Auer S.,
RA   Munden H., Nelson S., Norbertczak H., Oliver K., O'neil S., Pentony M.,
RA   Pohl T.M., Price C., Purnelle B., Quail M.A., Rabbinowitsch E.,
RA   Reinhardt R., Rieger M., Rinta J., Robben J., Robertson L., Ruiz J.C.,
RA   Rutter S., Saunders D., Schafer M., Schein J., Schwartz D.C., Seeger K.,
RA   Seyler A., Sharp S., Shin H., Sivam D., Squares R., Squares S., Tosato V.,
RA   Vogt C., Volckaert G., Wambutt R., Warren T., Wedler H., Woodward J.,
RA   Zhou S., Zimmermann W., Smith D.F., Blackwell J.M., Stuart K.D.,
RA   Barrell B., Myler P.J.;
RT   "The genome of the kinetoplastid parasite, Leishmania major.";
RL   Science 309:436-442(2005).
RN   [2] {ECO:0000313|EMBL:CAJ07816.1, ECO:0000313|Proteomes:UP000000542}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MHOM/IL/81/Friedlin {ECO:0000313|Proteomes:UP000000542};
RX   PubMed=22038252; DOI=10.1101/gr.122945.111;
RA   Rogers M.B., Hilley J.D., Dickens N.J., Wilkes J., Bates P.A.,
RA   Depledge D.P., Harris D., Her Y., Herzyk P., Imamura H., Otto T.D.,
RA   Sanders M., Seeger K., Dujardin J.C., Berriman M., Smith D.F.,
RA   Hertz-Fowler C., Mottram J.C.;
RT   "Chromosome and gene copy number variation allow major structural change
RT   between species and strains of Leishmania.";
RL   Genome Res. 21:2129-2142(2011).
CC   -!- SIMILARITY: Belongs to the GPAT/DAPAT family.
CC       {ECO:0000256|ARBA:ARBA00007937}.
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DR   EMBL; FR796430; CAJ07816.1; -; Genomic_DNA.
DR   RefSeq; XP_001686202.1; XM_001686150.1.
DR   STRING; 5664.Q4Q396; -.
DR   EnsemblProtists; CAJ07816; CAJ07816; LMJF_34_1090.
DR   GeneID; 5654871; -.
DR   KEGG; lma:LMJF_34_1090; -.
DR   VEuPathDB; TriTrypDB:LmjF.34.1090; -.
DR   VEuPathDB; TriTrypDB:LMJFC_340019400; -.
DR   VEuPathDB; TriTrypDB:LMJLV39_340018500; -.
DR   VEuPathDB; TriTrypDB:LMJSD75_340018600; -.
DR   eggNOG; KOG3730; Eukaryota.
DR   HOGENOM; CLU_266644_0_0_1; -.
DR   InParanoid; Q4Q396; -.
DR   OMA; NQLIHVC; -.
DR   Proteomes; UP000000542; Chromosome 34.
DR   GO; GO:0020022; C:acidocalcisome; ISO:GeneDB.
DR   GO; GO:0005737; C:cytoplasm; ISO:GeneDB.
DR   GO; GO:0020015; C:glycosome; IDA:GeneDB.
DR   GO; GO:0031966; C:mitochondrial membrane; IBA:GO_Central.
DR   GO; GO:0004366; F:glycerol-3-phosphate O-acyltransferase activity; IBA:GO_Central.
DR   GO; GO:0016287; F:glycerone-phosphate O-acyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008611; P:ether lipid biosynthetic process; IDA:GeneDB.
DR   GO; GO:0006631; P:fatty acid metabolic process; IBA:GO_Central.
DR   GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IBA:GO_Central.
DR   GO; GO:0008654; P:phospholipid biosynthetic process; IBA:GO_Central.
DR   GO; GO:0019432; P:triglyceride biosynthetic process; IBA:GO_Central.
DR   CDD; cd07993; LPLAT_DHAPAT-like; 1.
DR   InterPro; IPR022284; GPAT/DHAPAT.
DR   InterPro; IPR045520; GPAT/DHAPAT_C.
DR   InterPro; IPR041728; GPAT/DHAPAT_LPLAT.
DR   InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR   PANTHER; PTHR12563:SF17; DIHYDROXYACETONE PHOSPHATE ACYLTRANSFERASE; 1.
DR   PANTHER; PTHR12563; GLYCEROL-3-PHOSPHATE ACYLTRANSFERASE; 1.
DR   Pfam; PF01553; Acyltransferase; 1.
DR   Pfam; PF19277; GPAT_C; 1.
DR   SMART; SM00563; PlsC; 1.
DR   SUPFAM; SSF69593; Glycerol-3-phosphate (1)-acyltransferase; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW   ECO:0000313|EMBL:CAJ07816.1}; Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000542};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CAJ07816.1}.
FT   DOMAIN          791..922
FT                   /note="Phospholipid/glycerol acyltransferase"
FT                   /evidence="ECO:0000259|SMART:SM00563"
SQ   SEQUENCE   1436 AA;  155328 MW;  94F79C05CB2A6DB0 CRC64;
     MSFPPPRLAL PEECKQVVLV APIDGFTAAC ACAIATSPLV PLNCRVLVDG IAVKSSSPSS
     GNDSPHMACS SAESAATARD FMNTVQRVEA KLRASRATRR DVSVTHITQF YYGGVSPKAE
     EIGPMLHRIH LLGSGALGET NFTASSTDVT AGSGGSSGVP RVADSVFVLV LSAQSLSPDT
     ESGLKAYDIL LRRLWSAAGP SQAAETASQQ TRVRGSLVIL ADDVYRTAAC AMLSSIAKEV
     ATAVDWVVLL AYAYAMDPPA LEFGATEVAV QAASGISLGG TLPVLCAANA LGVLRHFPVS
     RGEPATITPV DVALNAALLG YVWLCHGELP ECVECAAEMQ YCGLSPAPSH AAAAAETATA
     MPTQPAQCVT RHRMGSFAVA ESRKPGEVSL VWGMVGEYLM SYYGRFADQI SAAFPVAGVL
     TQAPILQFPF SVADWVNFGP EPRAAAYALE GWRAYQQRQR LMEEKVGNAE AAQALKAYVA
     QMDSVVRYIE RTARAAAARD KISAAFAASR RRTASSSFSV PPYRLDDFNV ALYHSLLRRL
     TSHHTLMPYH QCVALVEVDW EAYVSVIARA VLEHLARCVL RSSSGLQHVR SRFHALPVAD
     SANIGSVVRS PPVVSAPDEL APASAAVPSS TKPEAAASAA EAPFAFPEPR RYFTNDFVYR
     GAERIPPFPS LLHKYFDCFV FLHRVGMTAN GWRGDMTPGM TPQVLTSIIA QPNIQRLMTA
     LAAKDGASKK DVEARAKRLL LECGDALNHV HCRTLGLMIR TIFHSIYGRV DVNNGSYERL
     HRYFAMPRVA VVFAPLHRSY IDFLILSEVL ALMRLPLPHI VAGENFLSMG VLATLMRGSG
     ALFMRRSFRD DPLYAALLKE YVRHLVRARR PLEFFIEGAR SRTGKTMAPK LGLLKFVCDT
     FYEPGQQELD DVLIVPVSLS YDEVLEATTH AKELLGVPKP KENPTNMLKA RSLLERMHGN
     IHIHVGEPVS LRSLKQHPRQ CPLPLQPKDE QLRDPAAPAA ATTSVCKTLD TTPSIAKGSS
     ITPIPLLGTV AWHLVYKLQR NTVITPASMV AAVVECLGPY YCTATTMLKE GIDTTAAAPT
     AAAAMPLEKV HQGVEWLRGR LRERGAQLSA EASKLNPAGV VTLALTNLYR YIHITDEMSG
     VTYHPDNVVT RLAVNISTNQ LIHVCMNEAL VAVVAQAFGF VTTPHRPPSG ADGAMLCGVR
     SVKADVLSNQ TQLLQRLLSA EFPNYAEAAP VSFASWLECT VSQLQQCVEE HTVSSQLSGA
     DTHGGTIVHL PVTQYYYFLL QLICPHVEAL YTVLAAASAL LAAYPGKPFG AAEVVTATQR
     ACYILYAERK LRYIVAANKE TLQHYYESLI ALSLLQIKRV PITTTPGQSK VNGGVVAYTV
     GLLGQEAALA RLEVLSTQIK ALWWHPSAAE GVTIDKAAIQ ERVLAVYREL TQPSKM
//
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