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Database: UniProt
Entry: A0A0D8ZVW9_9CYAN
LinkDB: A0A0D8ZVW9_9CYAN
Original site: A0A0D8ZVW9_9CYAN 
ID   A0A0D8ZVW9_9CYAN        Unreviewed;       212 AA.
AC   A0A0D8ZVW9;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   16-JAN-2019, entry version 13.
DE   RecName: Full=1-acyl-sn-glycerol-3-phosphate acyltransferase {ECO:0000256|RuleBase:RU361267};
DE            EC=2.3.1.51 {ECO:0000256|RuleBase:RU361267};
GN   ORFNames=UH38_04955 {ECO:0000313|EMBL:KJH72890.1};
OS   Aliterella atlantica CENA595.
OC   Bacteria; Cyanobacteria; Chroococcidiopsidales;
OC   Chroococcidiopsidaceae; Aliterella.
OX   NCBI_TaxID=1618023 {ECO:0000313|EMBL:KJH72890.1, ECO:0000313|Proteomes:UP000032452};
RN   [1] {ECO:0000313|EMBL:KJH72890.1, ECO:0000313|Proteomes:UP000032452}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CENA595 {ECO:0000313|EMBL:KJH72890.1,
RC   ECO:0000313|Proteomes:UP000032452};
RA   Rigonato J., Alvarenga D.O., Branco L.H., Varani A.M., Brandini F.P.,
RA   Fiore M.F.;
RT   "Draft genome of a novel marine cyanobacterium (Chroococcales)
RT   isolated from South Atlantic Ocean.";
RL   Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1-acyl-sn-glycero-3-phosphate + an acyl-CoA = a 1,2-
CC         diacyl-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:19709,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57970, ChEBI:CHEBI:58342,
CC         ChEBI:CHEBI:58608; EC=2.3.1.51;
CC         Evidence={ECO:0000256|RuleBase:RU361267};
CC   -!- DOMAIN: The HXXXXD motif is essential for acyltransferase activity
CC       and may constitute the binding site for the phosphate moiety of
CC       the glycerol-3-phosphate. {ECO:0000256|RuleBase:RU361267}.
CC   -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate
CC       acyltransferase family. {ECO:0000256|RuleBase:RU361267}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KJH72890.1}.
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DR   EMBL; JYON01000003; KJH72890.1; -; Genomic_DNA.
DR   RefSeq; WP_045053509.1; NZ_JYON01000003.1.
DR   EnsemblBacteria; KJH72890; KJH72890; UH38_04955.
DR   PATRIC; fig|1618023.3.peg.868; -.
DR   OrthoDB; 1756450at2; -.
DR   Proteomes; UP000032452; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0003841; F:1-acylglycerol-3-phosphate O-acyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR004552; AGP_acyltrans.
DR   InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR   Pfam; PF01553; Acyltransferase; 1.
DR   SMART; SM00563; PlsC; 1.
DR   TIGRFAMs; TIGR00530; AGP_acyltrn; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU361267,
KW   ECO:0000313|EMBL:KJH72890.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000032452};
KW   Lipid biosynthesis {ECO:0000256|RuleBase:RU361267};
KW   Lipid metabolism {ECO:0000256|RuleBase:RU361267};
KW   Phospholipid biosynthesis {ECO:0000256|RuleBase:RU361267};
KW   Phospholipid metabolism {ECO:0000256|RuleBase:RU361267};
KW   Reference proteome {ECO:0000313|Proteomes:UP000032452};
KW   Transferase {ECO:0000256|RuleBase:RU361267,
KW   ECO:0000313|EMBL:KJH72890.1}.
FT   DOMAIN       46    158       PlsC. {ECO:0000259|SMART:SM00563}.
SQ   SEQUENCE   212 AA;  22905 MW;  825FA0051774505C CRC64;
     MGKSREPAIS LFLYHLFKWS VVSPTLHLYL RGRIYGVENV PKRGPLVVVS NHASHFDSPI
     LSCALRRPVA YMAKEELFDI PILGKAIQLY GAYPVSRGAA DRSAIRSALK SLDNGWATGL
     FLEGTRTPDG RITEPKLGAA LIAAKAQASI LPVSLWGTQG ILHRGSPIPH SVPVTVRIGE
     AIAAPSSTDK LELQAVTQKC ALAIKELHDL GR
//
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