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Database: UniProt
Entry: F3NRI9_9ACTN
LinkDB: F3NRI9_9ACTN
Original site: F3NRI9_9ACTN 
ID   F3NRI9_9ACTN            Unreviewed;       275 AA.
AC   F3NRI9;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   SubName: Full=1-acylglycerol-3-phosphate O-acyltransferase {ECO:0000313|EMBL:EGG44173.1};
GN   ORFNames=SGM_5753 {ECO:0000313|EMBL:EGG44173.1};
OS   Streptomyces griseoaurantiacus M045.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces; Streptomyces aurantiacus group.
OX   NCBI_TaxID=996637 {ECO:0000313|EMBL:EGG44173.1, ECO:0000313|Proteomes:UP000003022};
RN   [1] {ECO:0000313|EMBL:EGG44173.1, ECO:0000313|Proteomes:UP000003022}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M045 {ECO:0000313|EMBL:EGG44173.1,
RC   ECO:0000313|Proteomes:UP000003022};
RX   PubMed=21551298; DOI=10.1128/JB.05053-11;
RA   Li F., Jiang P., Zheng H., Wang S., Zhao G., Qin S., Liu Z.;
RT   "Draft genome sequence of the marine bacterium Streptomyces
RT   griseoaurantiacus M045, which produces novel manumycin-type antibiotics
RT   with a pABA core component.";
RL   J. Bacteriol. 193:3417-3418(2011).
CC   -!- FUNCTION: Converts lysophosphatidic acid (LPA) into phosphatidic acid
CC       by incorporating acyl moiety at the 2 position.
CC       {ECO:0000256|ARBA:ARBA00037183}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1-acyl-sn-glycero-3-phosphate + an acyl-CoA = a 1,2-diacyl-
CC         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|ARBA:ARBA00001141};
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:EGG44173.1}.
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DR   EMBL; AEYX01000044; EGG44173.1; -; Genomic_DNA.
DR   AlphaFoldDB; F3NRI9; -.
DR   STRING; 996637.SGM_5753; -.
DR   eggNOG; COG0204; Bacteria.
DR   Proteomes; UP000003022; Unassembled WGS sequence.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR   CDD; cd07989; LPLAT_AGPAT-like; 1.
DR   InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR   PANTHER; PTHR10434; 1-ACYL-SN-GLYCEROL-3-PHOSPHATE ACYLTRANSFERASE; 1.
DR   PANTHER; PTHR10434:SF60; 1-ACYL-SN-GLYCEROL-3-PHOSPHATE ACYLTRANSFERASE LPAT1, CHLOROPLASTIC; 1.
DR   Pfam; PF01553; Acyltransferase; 1.
DR   SMART; SM00563; PlsC; 1.
DR   SUPFAM; SSF69593; Glycerol-3-phosphate (1)-acyltransferase; 1.
PE   4: Predicted;
KW   Acyltransferase {ECO:0000313|EMBL:EGG44173.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003022};
KW   Transferase {ECO:0000313|EMBL:EGG44173.1}.
FT   DOMAIN          51..172
FT                   /note="Phospholipid/glycerol acyltransferase"
FT                   /evidence="ECO:0000259|SMART:SM00563"
FT   REGION          245..275
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        245..268
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   275 AA;  29697 MW;  4265D2E8E5FF69AD CRC64;
     MSGDIVYGLS EDTGGTRLLY GAMKVTVGGT LKLAFRPWVE GLEHVPAEGP AILASNHLSF
     SDSFFLPAVL DRKVTFIAKA EYFTTPGVKG RMTAAFFKGA GQLPVDRSGA RGAGEAAVRS
     GIEVLRRGEL FGIYPEGTRS PDGRLYRGKP GGLARVALAT GAPVLPVAMI DTEKIQPPGK
     VVPKLMRPGI RIGWPLDFSR YQGMEHDRFV LRAVTDEVMY EIMRLSGQEY VDIYATAAKR
     RLADAAKAEK QAQAEKQAEA EKQSRAEKRA PGTGA
//
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