(data stored in ACNUC8465 zone)

SWISSPROT: B6H266_PENRW

ID   B6H266_PENRW            Unreviewed;       292 AA.
AC   B6H266;
DT   16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT   16-DEC-2008, sequence version 1.
DT   07-JUN-2017, entry version 48.
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=Pc13g04040 {ECO:0000313|EMBL:CAP91473.1}, PCH_Pc13g04040
GN   {ECO:0000313|EMBL:CAP91473.1};
OS   Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 /
OS   Wisconsin 54-1255) (Penicillium chrysogenum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC   Penicillium chrysogenum species complex.
OX   NCBI_TaxID=500485 {ECO:0000313|EMBL:CAP91473.1, ECO:0000313|Proteomes:UP000000724};
RN   [1] {ECO:0000313|EMBL:CAP91473.1, ECO:0000313|Proteomes:UP000000724}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255
RC   {ECO:0000313|Proteomes:UP000000724};
RX   PubMed=18820685; DOI=10.1038/nbt.1498;
RA   van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA   Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA   Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA   Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A.,
RA   van der Klei I.J., van Peij N.N.M.E., Veenhuis M., von Doehren H.,
RA   Wagner C., Wortman J.R., Bovenberg R.A.L.;
RT   "Genome sequencing and analysis of the filamentous fungus Penicillium
RT   chrysogenum.";
RL   Nat. Biotechnol. 26:1161-1168(2008).
CC   -!- CATALYTIC ACTIVITY: Acyl-CoA + 1-acyl-sn-glycerol 3-phosphate =
CC       CoA + 1,2-diacyl-sn-glycerol 3-phosphate.
CC       {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}.
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DR   EMBL; AM920428; CAP91473.1; -; Genomic_DNA.
DR   RefSeq; XP_002558840.1; XM_002558794.1.
DR   STRING; 500485.XP_002558840.1; -.
DR   EnsemblFungi; CAP91473; CAP91473; PCH_Pc13g04040.
DR   GeneID; 8304049; -.
DR   KEGG; pcs:Pc13g04040; -.
DR   eggNOG; KOG2848; Eukaryota.
DR   eggNOG; COG0204; LUCA.
DR   HOGENOM; HOG000026375; -.
DR   KO; K13509; -.
DR   OMA; CHRAMRT; -.
DR   OrthoDB; EOG092C4MB5; -.
DR   BioCyc; PCHR:PC13G04040-MONOMER; -.
DR   Proteomes; UP000000724; Contig Pc00c13.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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;
DR   PRODOM; B6H266.
DR   SWISS-2DPAGE; B6H266.
KW   Acyltransferase {ECO:0000256|RuleBase:RU361267};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000724};
KW   Lipid biosynthesis {ECO:0000256|RuleBase:RU361267};
KW   Lipid metabolism {ECO:0000256|RuleBase:RU361267};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phospholipid biosynthesis {ECO:0000256|RuleBase:RU361267};
KW   Phospholipid metabolism {ECO:0000256|RuleBase:RU361267};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000724};
KW   Transferase {ECO:0000256|RuleBase:RU361267};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM      6     25       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     37     61       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN      101    218       PlsC. {ECO:0000259|SMART:SM00563}.
SQ   SEQUENCE   292 AA;  31768 MW;  8D779E52F039239A CRC64;
     MSFGSYIVSG VSSFVVLTVS LFAIGQKVPR AAFAARCLAS YGSLLVSAAY GVIVSVCLRL
     VGYGRISQWA AGRSFKWMMR LTTGVTFEVV EGAEYLSTRP AVFIGNHQTE LDVLMLGCVF
     PPYCSVTAKK SLRNVPFLGW FMSLSRTVFI DRANRETALK AFDGAAAEMR DHRQSVFIFA
     EGTRSYSDEP TLLPFKKGAF HLAVKAGVPI VPIVTENYSH VLSPRAWRFN AGTIKIRVLP
     PIPTKDLTSG DVDSLTQSTR DSMLKTLAAM SHAHKNEVDG ARANGVSSAI EI
//

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