(data stored in SCRATCH zone)

SWISSPROT: A5GQJ3_SYNR3

ID   A5GQJ3_SYNR3            Unreviewed;       405 AA.
AC   A5GQJ3;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   12-JUN-2007, sequence version 1.
DT   08-MAY-2019, entry version 76.
DE   RecName: Full=Phosphate acyltransferase {ECO:0000256|HAMAP-Rule:MF_00019, ECO:0000256|SAAS:SAAS00962511};
DE            EC=2.3.1.274 {ECO:0000256|HAMAP-Rule:MF_00019, ECO:0000256|SAAS:SAAS01132328};
DE   AltName: Full=Acyl-ACP phosphotransacylase {ECO:0000256|HAMAP-Rule:MF_00019};
DE   AltName: Full=Acyl-[acyl-carrier-protein]--phosphate acyltransferase {ECO:0000256|HAMAP-Rule:MF_00019};
DE   AltName: Full=Phosphate-acyl-ACP acyltransferase {ECO:0000256|HAMAP-Rule:MF_00019};
GN   Name=plsX {ECO:0000256|HAMAP-Rule:MF_00019,
GN   ECO:0000313|EMBL:CAK27152.1};
GN   OrderedLocusNames=SynRCC307_0249 {ECO:0000313|EMBL:CAK27152.1};
OS   Synechococcus sp. (strain RCC307).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=316278 {ECO:0000313|EMBL:CAK27152.1, 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 reversible formation of acyl-phosphate
CC       (acyl-PO(4)) from acyl-[acyl-carrier-protein] (acyl-ACP). This
CC       enzyme utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA.
CC       {ECO:0000256|HAMAP-Rule:MF_00019, ECO:0000256|SAAS:SAAS00962504}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a fatty acyl-[ACP] + phosphate = an acyl phosphate +
CC         holo-[ACP]; Xref=Rhea:RHEA:42292, Rhea:RHEA-COMP:9685,
CC         Rhea:RHEA-COMP:14125, ChEBI:CHEBI:43474, ChEBI:CHEBI:59918,
CC         ChEBI:CHEBI:64479, ChEBI:CHEBI:138651; EC=2.3.1.274;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00019,
CC         ECO:0000256|SAAS:SAAS01132329};
CC   -!- PATHWAY: Lipid metabolism; phospholipid metabolism.
CC       {ECO:0000256|HAMAP-Rule:MF_00019, ECO:0000256|SAAS:SAAS00962503}.
CC   -!- SUBUNIT: Homodimer. Probably interacts with PlsY.
CC       {ECO:0000256|HAMAP-Rule:MF_00019, ECO:0000256|SAAS:SAAS00962505}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00019}.
CC       Note=Associated with the membrane possibly through PlsY.
CC       {ECO:0000256|HAMAP-Rule:MF_00019}.
CC   -!- SIMILARITY: Belongs to the PlsX family. {ECO:0000256|HAMAP-
CC       Rule:MF_00019, ECO:0000256|SAAS:SAAS00962509}.
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DR   EMBL; CT978603; CAK27152.1; -; Genomic_DNA.
DR   RefSeq; WP_011934667.1; NC_009482.1.
DR   STRING; 316278.SynRCC307_0249; -.
DR   EnsemblBacteria; CAK27152; CAK27152; SynRCC307_0249.
DR   KEGG; syr:SynRCC307_0249; -.
DR   eggNOG; ENOG4105C6B; Bacteria.
DR   eggNOG; COG0416; LUCA.
DR   HOGENOM; HOG000154731; -.
DR   KO; K03621; -.
DR   OMA; DCKPEYL; -.
DR   OrthoDB; 631784at2; -.
DR   BioCyc; SSP316278:G1GJL-245-MONOMER; -.
DR   UniPathway; UPA00085; -.
DR   Proteomes; UP000001115; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0043811; F:phosphate:acyl-[acyl carrier protein] acyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR   HAMAP; MF_00019; PlsX; 1.
DR   InterPro; IPR003664; FA_synthesis.
DR   InterPro; IPR012281; Phospholipid_synth_PlsX-like.
DR   PANTHER; PTHR30100; PTHR30100; 1.
DR   Pfam; PF02504; FA_synthesis; 1.
DR   PIRSF; PIRSF002465; Phsphlp_syn_PlsX; 1.
DR   TIGRFAMs; TIGR00182; plsX; 1.
PE   3: Inferred from homology;
DR   PRODOM; A5GQJ3.
DR   SWISS-2DPAGE; A5GQJ3.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001115};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00019,
KW   ECO:0000256|SAAS:SAAS00962513};
KW   Lipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00019,
KW   ECO:0000256|SAAS:SAAS00962512};
KW   Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_00019,
KW   ECO:0000256|SAAS:SAAS00962501};
KW   Phospholipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00019,
KW   ECO:0000256|SAAS:SAAS00962507};
KW   Phospholipid metabolism {ECO:0000256|HAMAP-Rule:MF_00019,
KW   ECO:0000256|SAAS:SAAS00962508};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001115};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00019,
KW   ECO:0000256|SAAS:SAAS00962500}.
SQ   SEQUENCE   405 AA;  43234 MW;  5FA0AC6F68ED69DD CRC64;
     MAEPQSLPGR TRRPRPRRAI KRLVIWYRRT GPVIRLVNTA HSALGPLRLG QTRPGGARAV
     KGPRLSIAVD GMGGDYAPGP ILEGCLGAIE ELPLKVMFFA EEKPLQAAIK ALELQEAVDQ
     AVAKGHLELI ASGPSVGMDD EATSVRRKRQ ASINLAMDRV KAGEALAVYS AGNSGAVMAA
     AIFRLGRLKG IERPAIGALF PTKDVGQQVL VLDVGANTDC KPSYLHQFAL LGNIYARDVL
     GVKQPRVGLL NIGEEECKGN ELALKTHPLL VEEKRLNFAG NCEGRDVLSG EFDVVVCDGF
     TGNVLLKFLE SVGSVLLEVL KAELPRGRRG KVGSAFLISN LRRIKKRLDH AEHGGALLLG
     VDGLCVIGHG SSKARSVMGA LRLAHAAASH NTLDNLHRLS DEGVG
//

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