GenomeNet

Database: UniProt
Entry: I2JI22_9GAMM
LinkDB: I2JI22_9GAMM
Original site: I2JI22_9GAMM 
ID   I2JI22_9GAMM            Unreviewed;       631 AA.
AC   I2JI22;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2012, sequence version 1.
DT   24-JAN-2024, entry version 50.
DE   RecName: Full=Glycerol-3-phosphate acyltransferase {ECO:0000256|ARBA:ARBA00013432};
DE            EC=2.3.1.15 {ECO:0000256|ARBA:ARBA00013113};
GN   ORFNames=DOK_13047 {ECO:0000313|EMBL:EIF42624.1};
OS   gamma proteobacterium BDW918.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC   Spongiibacteraceae.
OX   NCBI_TaxID=1168065 {ECO:0000313|EMBL:EIF42624.1, ECO:0000313|Proteomes:UP000003473};
RN   [1] {ECO:0000313|EMBL:EIF42624.1, ECO:0000313|Proteomes:UP000003473}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BDW918 {ECO:0000313|EMBL:EIF42624.1,
RC   ECO:0000313|Proteomes:UP000003473};
RX   PubMed=22740675; DOI=10.1128/JB.00678-12;
RA   Kim S.M., Cho S.J., Lee S.B.;
RT   "Genome Sequence of the Unclassified Marine Gammaproteobacterium BDW918.";
RL   J. Bacteriol. 194:3753-3754(2012).
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|ARBA:ARBA00000510};
CC   -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-
CC       diacylglycerol from sn-glycerol 3-phosphate: step 1/3.
CC       {ECO:0000256|ARBA:ARBA00004765}.
CC   -!- SIMILARITY: Belongs to the GPAT/DAPAT family.
CC       {ECO:0000256|ARBA:ARBA00007937}.
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:EIF42624.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AJMK01000066; EIF42624.1; -; Genomic_DNA.
DR   AlphaFoldDB; I2JI22; -.
DR   PATRIC; fig|1168065.3.peg.2680; -.
DR   eggNOG; COG2937; Bacteria.
DR   HOGENOM; CLU_015407_1_0_6; -.
DR   OrthoDB; 335193at2; -.
DR   UniPathway; UPA00557; UER00612.
DR   Proteomes; UP000003473; 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; 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   PIRSF; PIRSF000437; GPAT_DHAPAT; 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:EIF42624.1}; Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003473};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EIF42624.1}.
FT   DOMAIN          120..247
FT                   /note="Phospholipid/glycerol acyltransferase"
FT                   /evidence="ECO:0000259|SMART:SM00563"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..17
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   631 AA;  71064 MW;  D96965A5F7B2CE9A CRC64;
     MKEKDIEQDE RDLSQHAGKQ VSEASDSSIT MGKKAIVSKI LGSSRVQNAL RELAVKEGLS
     QSEAHSRARR SLQSLVAVQK PLFTTLFDRV LAPMHTNAWT VDVDQESLRR LEVLSRDNML
     VFLPTHRSYA DPFILTQLIS SSALPRNYIL GGDNIGFWPM GSVVRRSGAI LIRRSFGDDR
     VYKLMIKEYL AYLARSGGNL EWYMEGGRSR TGKLRPPMYG LLRYLGQALS VESRKSVILV
     PVAITYDQLH EIWGMAAEEA GNAKKAKEGL PWLANYARMQ SKWIGTAYVR FGELMSLTEA
     MHPDSKNPST IEKVAIEVFQ RINKVTPVTG PALATLALLA VRNRALTLPE ITHLVSPLLD
     YARRRALPTE VVDELDNHSG IEDALSSLAK ADVLDCYKGG LEPIYNIRAG SHNIAAYYRN
     SAIHWFINRA ILEVTLLHTS HINNGDENIF DQGWDDAHAL RDVLKFEFFF SEKNKFKEEM
     REEALILDAD FFAKVQRAEE RRNMLYQAPF LMAHRVLMPF LEAYVIVAEL MASKGGGTIS
     DESLFIAECL SVGRQWVLQY KIRSPESLSQ ELFKNALKLA KNRDLLEQRL GLHEDRLALK
     DYLHSVVAAL ANVESLDLER CANSQEGGVN E
//
DBGET integrated database retrieval system