ID K1Z598_9BACT Unreviewed; 576 AA.
AC K1Z598;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Phospholipid/glycerol acyltransferase domain-containing protein {ECO:0000259|SMART:SM00563};
GN ORFNames=ACD_62C00557G0006 {ECO:0000313|EMBL:EKD50385.1};
OS uncultured bacterium.
OC Bacteria; environmental samples.
OX NCBI_TaxID=77133 {ECO:0000313|EMBL:EKD50385.1};
RN [1] {ECO:0000313|EMBL:EKD50385.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23019650; DOI=10.1126/science.1224041;
RA Wrighton K.C., Thomas B.C., Sharon I., Miller C.S., Castelle C.J.,
RA VerBerkmoes N.C., Wilkins M.J., Hettich R.L., Lipton M.S., Williams K.H.,
RA Long P.E., Banfield J.F.;
RT "Fermentation, hydrogen, and sulfur metabolism in multiple uncultivated
RT bacterial phyla.";
RL Science 337:1661-1665(2012).
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:EKD50385.1}.
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DR EMBL; AMFJ01026360; EKD50385.1; -; Genomic_DNA.
DR AlphaFoldDB; K1Z598; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
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 Membrane {ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..24
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 69..92
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 98..117
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 250..414
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 576 AA; 65735 MW; E51D11B0D500DCC0 CRC64;
MQRNFLVLAA VFYVLPLIKF LYFISRHFLG VLISASQKIM SRSNRSQEPV SFFYNALAFI
AEVEYYFQFF RFLCVGVPVI LWWLVSTITL LTGHHGSLGV PSYIGLFFLA MLVFWHAGQK
KMADLRASQL IVMFPDIHPG IFFRKYKFEL TYGGIDFFHS DPSDQAWASH MDYRKGRRAQ
QKKTLFVKAV FDMAYVAHIC LSGLKYLGPS YLRAFADQLI AVLGKRLLQL SESSLSVLGA
EKLQGLQGKF ILIFNHKSAF DFALTPYVLS HITVNNRRVR PRFILAQDHF KDNWFLYHVI
GMGKAAEAID MIFVSRKDQK KSFDNLKQAA QTMIEKDVDI AIYPQGTRAA GNYDRADKRR
DAGYYTTVRK KDLNSKWPHL KRGTAFLALD VLTQLRVSGD DQELHLVFIG ISGTATVLPK
GSLAVQTEAE VVFTIGDVLS LSPHMLDDLF VADQPREEAP LARKKFATEL TGVINEKLLS
VLNLKFQLLQ RFLTELKGQF HYDNERLQVV QNNMVMIDKS SDVVFEILDK IYSLPVSQWN
GYLSQLSQML LGKPDLTRFE ILAHDVTEDL LSLKAK
//
