ID A0A0U3GBN5_9ACTN Unreviewed; 255 AA.
AC A0A0U3GBN5;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Acyl-phosphate glycerol 3-phosphate acyltransferase {ECO:0000313|EMBL:ALV36206.1};
GN ORFNames=AS200_32280 {ECO:0000313|EMBL:ALV36206.1};
OS Streptomyces sp. CdTB01.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1725411 {ECO:0000313|EMBL:ALV36206.1, ECO:0000313|Proteomes:UP000068029};
RN [1] {ECO:0000313|EMBL:ALV36206.1, ECO:0000313|Proteomes:UP000068029}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CdTB01 {ECO:0000313|EMBL:ALV36206.1,
RC ECO:0000313|Proteomes:UP000068029};
RA Tian Y., Zhou G., Yang H., Lu X.;
RT "Complete genome sequence of the Streptomyces sp. strain CdTB01, a
RT bacterium tolerant to cadmium.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP013743; ALV36206.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0U3GBN5; -.
DR STRING; 1725411.AS200_32280; -.
DR KEGG; scx:AS200_32280; -.
DR OrthoDB; 9808424at2; -.
DR Proteomes; UP000068029; Chromosome.
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:ALV36206.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000068029};
KW Transferase {ECO:0000313|EMBL:ALV36206.1}.
FT DOMAIN 34..155
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
FT REGION 225..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 226..255
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 255 AA; 27648 MW; 99CFA30741C0E581 CRC64;
MLYGAMKVAI GGPLKVTFRP WVEGLENIPA EGAAILASNH LSFSDSFFLP AVLDRKVTFI
AKAEYFTTPG VKGRLTAAFF KGVGQLPVDR SGARGAGEAA IRSGLEVLER GELFGIYPEG
TRSPDGRLYR GKPGGLARVA LASGAPVIPV AMIDTEKIQP PGKVMPKLMR PGIRIGKALD
FSRYQGMEHD RFVLRAVTDE VMYEIMKLSG QEYVDMYATA AKRQIAEAAK AEKEQAKEQA
KEQSGEQATE EKPEA
//
