ID A0A0Q4CWK3_9SPHN Unreviewed; 244 AA.
AC A0A0Q4CWK3;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Acyl-phosphate glycerol 3-phosphate acyltransferase {ECO:0000313|EMBL:KQM28954.1};
GN ORFNames=ASE58_03665 {ECO:0000313|EMBL:KQM28954.1};
OS Sphingomonas sp. Leaf9.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1735674 {ECO:0000313|EMBL:KQM28954.1, ECO:0000313|Proteomes:UP000051210};
RN [1] {ECO:0000313|EMBL:KQM28954.1, ECO:0000313|Proteomes:UP000051210}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf9 {ECO:0000313|EMBL:KQM28954.1,
RC ECO:0000313|Proteomes:UP000051210};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQM28954.1, ECO:0000313|Proteomes:UP000051210}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf9 {ECO:0000313|EMBL:KQM28954.1,
RC ECO:0000313|Proteomes:UP000051210};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
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:KQM28954.1}.
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DR EMBL; LMKC01000001; KQM28954.1; -; Genomic_DNA.
DR RefSeq; WP_055817896.1; NZ_LMKC01000001.1.
DR AlphaFoldDB; A0A0Q4CWK3; -.
DR Proteomes; UP000051210; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006629; P:lipid metabolic process; 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:SF65; 1-ACYL-SN-GLYCEROL-3-PHOSPHATE ACYLTRANSFERASE; 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:KQM28954.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Transferase {ECO:0000313|EMBL:KQM28954.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 66..180
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 244 AA; 26206 MW; ED4FF32C0754E2CE CRC64;
MTLPARWRLI ARAGGMLAAL LAYLVLHGSW RLLRLRSPWP PRFLGRIARV VGVRTTVVGS
PVPRDVLYLA NHQSWIDILA IAGASGSAFV AKGELRDAPL VGWLCTLNHT LFVDRGDRLG
VARQIDTLRQ ALLADHPVTV FPEGTTSAPG ELLPFKAALL GAIDPPPPGL RVQPVYCDYG
DAHEVAWLGD EPGTTNAARV LARAGRIGLT IHFLEPFDPA GMGRKAVANR ARDAIAAAMA
QGRT
//
