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Database: UniProt
Entry: K6XDL9_9ACTN
LinkDB: K6XDL9_9ACTN
Original site: K6XDL9_9ACTN 
ID   K6XDL9_9ACTN            Unreviewed;       767 AA.
AC   K6XDL9;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   11-DEC-2019, entry version 39.
DE   RecName: Full=Glycerol-3-phosphate 1-O-acyltransferase {ECO:0000256|SAAS:SAAS01159158};
DE            EC=2.3.1.15 {ECO:0000256|SAAS:SAAS01159158};
GN   Name=plsB {ECO:0000313|EMBL:GAC02463.1};
GN   ORFNames=GONAM_54_00910 {ECO:0000313|EMBL:GAC02463.1};
OS   Gordonia namibiensis NBRC 108229.
OC   Bacteria; Actinobacteria; Corynebacteriales; Gordoniaceae; Gordonia.
OX   NCBI_TaxID=1208314 {ECO:0000313|EMBL:GAC02463.1, ECO:0000313|Proteomes:UP000035058};
RN   [1] {ECO:0000313|EMBL:GAC02463.1, ECO:0000313|Proteomes:UP000035058}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 108229 {ECO:0000313|EMBL:GAC02463.1,
RC   ECO:0000313|Proteomes:UP000035058};
RA   Isaki-Nakamura S., Hosoyama A., Tsuchikane K., Katsumata H., Baba S.,
RA   Yamazaki S., Fujita N.;
RT   "Whole genome shotgun sequence of Gordonia namibiensis NBRC 108229.";
RL   Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an acyl-CoA + sn-glycerol 3-phosphate = a 1-acyl-sn-glycero-3-
CC         phosphate + CoA; Xref=Rhea:RHEA:15325, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57597, ChEBI:CHEBI:57970, ChEBI:CHEBI:58342; EC=2.3.1.15;
CC         Evidence={ECO:0000256|SAAS:SAAS01159161};
CC   -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-
CC       diacylglycerol from sn-glycerol 3-phosphate: step 1/3.
CC       {ECO:0000256|SAAS:SAAS01159170}.
CC   -!- SIMILARITY: Belongs to the GPAT/DAPAT family.
CC       {ECO:0000256|SAAS:SAAS01159165}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:GAC02463.1}.
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DR   EMBL; BAHE01000054; GAC02463.1; -; Genomic_DNA.
DR   RefSeq; WP_006868598.1; NZ_BAHE01000054.1.
DR   EnsemblBacteria; GAC02463; GAC02463; GONAM_54_00910.
DR   UniPathway; UPA00557; UER00612.
DR   Proteomes; UP000035058; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004366; F:glycerol-3-phosphate O-acyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0102420; F:sn-1-glycerol-3-phosphate C16:0-DCA-CoA acyl transferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd07993; LPLAT_DHAPAT-like; 1.
DR   InterPro; IPR022284; GPAT/DHAPAT.
DR   InterPro; IPR041728; GPAT/DHAPAT_LPLAT.
DR   InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR   PANTHER; PTHR12563; PTHR12563; 1.
DR   Pfam; PF01553; Acyltransferase; 1.
DR   PIRSF; PIRSF000437; GPAT_DHAPAT; 1.
DR   SMART; SM00563; PlsC; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|SAAS:SAAS01159160,
KW   ECO:0000313|EMBL:GAC02463.1};
KW   Lipid biosynthesis {ECO:0000256|SAAS:SAAS01159164};
KW   Lipid metabolism {ECO:0000256|SAAS:SAAS01159169};
KW   Membrane {ECO:0000256|SAAS:SAAS01159157};
KW   Phospholipid biosynthesis {ECO:0000256|SAAS:SAAS01159171};
KW   Phospholipid metabolism {ECO:0000256|SAAS:SAAS01159162};
KW   Transferase {ECO:0000256|SAAS:SAAS01159175, ECO:0000313|EMBL:GAC02463.1}.
FT   DOMAIN          241..368
FT                   /note="PlsC"
FT                   /evidence="ECO:0000259|SMART:SM00563"
SQ   SEQUENCE   767 AA;  84674 MW;  26FFC1D805725FF2 CRC64;
     MQMSDPVLVL TKARTSCEMH AVKDWAATAY PDAEVRQGAD VDFDELSPNT LLVPVRPVWL
     PAVRQGERRV TLGDVLVLSN PRRPLGLMQP IIRRRRPDAL RVVAGEPATI AELRERHARD
     QAEGEPFDQY VRIAASVSAE RAERQIVGDR YKVPRLVAEQ ISSSARFQSG AAKLAAELGR
     PTDAVVSEAT DKLSGFVATQ SRLMDDIFSA TFNRLHERAW NVTVDVDTLN SLRTLNKSTG
     LVFLPSHRSY VDPLVLATVL RNNDFPPNLV LGGNNLSFWP VGPVARRAGM IFIRRKFGSD
     PVYKFAMRSY LAYIIEKRFN LEWYIEGGRS RTGKLRKPML GLLNYVVDAA SQLDDADVTI
     VPTSIVYDQL QEVGAIAAED AGGVKKPEGV GWLLRYAKAQ RSYLGEARVR FGTPISLKQA
     LDEAGDGPAR LEKVAFRVMD EINSATPITA TSLVGFAALG AQDRAYTLRE IEAVLAPLLD
     YIDRRGLPGP DPALCRGVGL VRTLRVLAGN GVVTCYEGGS EPVWSVVPEN RAVAAYYRNG
     ALHHFVDRAI VEMGLLALAE GEVKAGSTPI RSNHVGSPPA PDEELLTAAQ REALRIRDLL
     KFEFFFPPKT EYLHRLGIEL DLLAPGWRAV TPTQEWTYEV LHGHTGALFA RRTLQTFFDA
     QLVVATKLVE LGNTAQEKDA LIADCLGLGR QLALQAVLRS KDSVSKDLYD GAYRLADNRG
     LIHGEDIVDL RAARQDWLDE VELMRDRLAR IAAIEDLQPV VAGEEEQ
//
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