ID E3HL08_ACHXA Unreviewed; 286 AA.
AC E3HL08;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=Acyltransferase family protein 4 {ECO:0000313|EMBL:ADP15681.1};
GN OrderedLocusNames=AXYL_02360 {ECO:0000313|EMBL:ADP15681.1};
OS Achromobacter xylosoxidans (strain A8).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Achromobacter.
OX NCBI_TaxID=762376 {ECO:0000313|EMBL:ADP15681.1, ECO:0000313|Proteomes:UP000006876};
RN [1] {ECO:0000313|EMBL:ADP15681.1, ECO:0000313|Proteomes:UP000006876}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A8 {ECO:0000313|EMBL:ADP15681.1,
RC ECO:0000313|Proteomes:UP000006876};
RX PubMed=21097610; DOI=10.1128/JB.01299-10;
RA Strnad H., Ridl J., Paces J., Kolar M., Vlcek C., Paces V.;
RT "Complete genome sequence of the haloaromatic acids-degrading bacterium
RT Achromobacter xylosoxidans A8.";
RL J. Bacteriol. 193:791-792(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 -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
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DR EMBL; CP002287; ADP15681.1; -; Genomic_DNA.
DR AlphaFoldDB; E3HL08; -.
DR STRING; 762376.AXYL_02360; -.
DR KEGG; axy:AXYL_02360; -.
DR eggNOG; COG0204; Bacteria.
DR HOGENOM; CLU_078753_0_0_4; -.
DR Proteomes; UP000006876; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:ADP15681.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Transferase {ECO:0000313|EMBL:ADP15681.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..44
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 98..206
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 286 AA; 31764 MW; B229D04C6AE2120E CRC64;
MDLDTHCMTS ATPARQDFWL WRLFATGMAF TLFGIGGVLL RVLVFPPQRL LPGDKADRQR
RARGALNRTF RMFIRFMVRT GILTVEFKGA ERLGQPGQMI LANHPSLLDV VFLVGHVKNA
NCIVKHGLAT NPFTRGPVAN AGYITNDESF DMFDRAADAL RAGETLIVFP EGTRTPRDAM
PRFHRGACAI ALRGARVVTP VVISMNPRSL TKGEPWYRIP PCRMRYVIRV GEDIDPATWS
GAHPLPIAGR KMNDYLHAYF EAELAHAAPA GALMNEQPPQ AVEVES
//
