(data stored in SCRATCH zone)

SWISSPROT: A5GR66_SYNR3

ID   A5GR66_SYNR3            Unreviewed;       200 AA.
AC   A5GR66;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   12-JUN-2007, sequence version 1.
DT   08-MAY-2019, entry version 74.
DE   RecName: Full=Glycerol-3-phosphate acyltransferase {ECO:0000256|HAMAP-Rule:MF_01043};
DE   AltName: Full=Acyl-PO4 G3P acyltransferase {ECO:0000256|HAMAP-Rule:MF_01043};
DE   AltName: Full=Acyl-phosphate--glycerol-3-phosphate acyltransferase {ECO:0000256|HAMAP-Rule:MF_01043};
DE   AltName: Full=G3P acyltransferase {ECO:0000256|HAMAP-Rule:MF_01043};
DE            Short=GPAT {ECO:0000256|HAMAP-Rule:MF_01043};
DE            EC=2.3.1.275 {ECO:0000256|HAMAP-Rule:MF_01043};
DE   AltName: Full=Lysophosphatidic acid synthase {ECO:0000256|HAMAP-Rule:MF_01043};
DE            Short=LPA synthase {ECO:0000256|HAMAP-Rule:MF_01043};
GN   Name=plsY {ECO:0000256|HAMAP-Rule:MF_01043};
GN   OrderedLocusNames=SynRCC307_0472 {ECO:0000313|EMBL:CAK27375.1};
OS   Synechococcus sp. (strain RCC307).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=316278 {ECO:0000313|EMBL:CAK27375.1, ECO:0000313|Proteomes:UP000001115};
RN   [1] {ECO:0000313|Proteomes:UP000001115}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCC307 {ECO:0000313|Proteomes:UP000001115};
RG   Genoscope;
RL   Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the transfer of an acyl group from acyl-
CC       phosphate (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form
CC       lysophosphatidic acid (LPA). This enzyme utilizes acyl-phosphate
CC       as fatty acyl donor, but not acyl-CoA or acyl-ACP.
CC       {ECO:0000256|HAMAP-Rule:MF_01043}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an acyl phosphate + sn-glycerol 3-phosphate = a 1-acyl-
CC         sn-glycero-3-phosphate + phosphate; Xref=Rhea:RHEA:34075,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57597, ChEBI:CHEBI:57970,
CC         ChEBI:CHEBI:59918; EC=2.3.1.275; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01043};
CC   -!- PATHWAY: Lipid metabolism; phospholipid metabolism.
CC       {ECO:0000256|HAMAP-Rule:MF_01043, ECO:0000256|SAAS:SAAS00702448}.
CC   -!- SUBUNIT: Probably interacts with PlsX. {ECO:0000256|HAMAP-
CC       Rule:MF_01043, ECO:0000256|SAAS:SAAS00702495}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC       Rule:MF_01043}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_01043}.
CC   -!- SIMILARITY: Belongs to the PlsY family. {ECO:0000256|HAMAP-
CC       Rule:MF_01043, ECO:0000256|SAAS:SAAS00702497}.
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DR   EMBL; CT978603; CAK27375.1; -; Genomic_DNA.
DR   RefSeq; WP_011934890.1; NC_009482.1.
DR   STRING; 316278.SynRCC307_0472; -.
DR   EnsemblBacteria; CAK27375; CAK27375; SynRCC307_0472.
DR   KEGG; syr:SynRCC307_0472; -.
DR   eggNOG; ENOG4105K7Z; Bacteria.
DR   eggNOG; COG0344; LUCA.
DR   HOGENOM; HOG000283807; -.
DR   KO; K08591; -.
DR   OMA; WRHRGNL; -.
DR   OrthoDB; 1691856at2; -.
DR   BioCyc; SSP316278:G1GJL-472-MONOMER; -.
DR   UniPathway; UPA00085; -.
DR   Proteomes; UP000001115; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0043772; F:acyl-phosphate glycerol-3-phosphate acyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_01043; PlsY; 1.
DR   InterPro; IPR003811; G3P_acylTferase_PlsY.
DR   PANTHER; PTHR30309; PTHR30309; 1.
DR   Pfam; PF02660; G3P_acyltransf; 1.
DR   SMART; SM01207; G3P_acyltransf; 1.
DR   TIGRFAMs; TIGR00023; TIGR00023; 1.
PE   3: Inferred from homology;
DR   PRODOM; A5GR66.
DR   SWISS-2DPAGE; A5GR66.
KW   Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_01043};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_01043,
KW   ECO:0000256|SAAS:SAAS00702469};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001115};
KW   Lipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01043,
KW   ECO:0000256|SAAS:SAAS00702478};
KW   Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_01043,
KW   ECO:0000256|SAAS:SAAS00702441};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_01043,
KW   ECO:0000256|SAAS:SAAS00702479};
KW   Phospholipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01043,
KW   ECO:0000256|SAAS:SAAS00702501};
KW   Phospholipid metabolism {ECO:0000256|HAMAP-Rule:MF_01043,
KW   ECO:0000256|SAAS:SAAS00702488};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001115};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01043,
KW   ECO:0000256|SAAS:SAAS00702475};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_01043,
KW   ECO:0000256|SAAS:SAAS00702474};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01043,
KW   ECO:0000256|SAAS:SAAS00702429}.
FT   TRANSMEM     55     77       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01043}.
FT   TRANSMEM     84    102       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01043}.
FT   TRANSMEM    114    134       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01043}.
FT   TRANSMEM    164    180       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01043}.
SQ   SEQUENCE   200 AA;  20166 MW;  7ADF424720156D48 CRC64;
     MNPLAILVVP LGYLLGSFPS GYLAGRWCAG VDIRQLGSGS TGATNVLRQV GKGPALVVFL
     VDVFKGSAAV ILARALLGAG AYGWLVAAGL AALAGHIWPI WLGGKGGKAV ATGFGMLLGL
     VPAVGMACLG VFLTSLALSR IVSISSVLAA AALPLLMAGA GAPGAYLGLG VVAAVMVIWR
     HRSNLSRLLK GEEPRLGQKD
//

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