ID I3ZMV2_TERRK Unreviewed; 261 AA.
AC I3ZMV2;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=1-acyl-sn-glycerol-3-phosphate acyltransferase {ECO:0000313|EMBL:AFL90570.1};
GN OrderedLocusNames=Terro_4373 {ECO:0000313|EMBL:AFL90570.1};
OS Terriglobus roseus (strain DSM 18391 / NRRL B-41598 / KBS 63).
OC Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC Terriglobus.
OX NCBI_TaxID=926566 {ECO:0000313|EMBL:AFL90570.1, ECO:0000313|Proteomes:UP000006056};
RN [1] {ECO:0000313|EMBL:AFL90570.1, ECO:0000313|Proteomes:UP000006056}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18391 / NRRL B-41598 / KBS 63
RC {ECO:0000313|Proteomes:UP000006056};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Peters L., Mikhailova N., Munk A.C.C.,
RA Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA Woyke T., Wu D., Brambilla E., Klenk H.-P., Eisen J.A.;
RT "Complete genome of Terriglobus roseus DSM 18391.";
RL Submitted (JUN-2012) 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};
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DR EMBL; CP003379; AFL90570.1; -; Genomic_DNA.
DR RefSeq; WP_014787830.1; NC_018014.1.
DR AlphaFoldDB; I3ZMV2; -.
DR STRING; 926566.Terro_4373; -.
DR KEGG; trs:Terro_4373; -.
DR eggNOG; COG0204; Bacteria.
DR HOGENOM; CLU_027938_6_3_0; -.
DR Proteomes; UP000006056; 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:AFL90570.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000006056};
KW Transferase {ECO:0000313|EMBL:AFL90570.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..34
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 74..188
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
FT REGION 241..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 261 AA; 29135 MW; 994852FE8E00463F CRC64;
MKKLLPWISY LVLIPLMAFV TIICGLFSLL FSLWDKSGRQ QHAMAQFWAK LMLGISLSPV
TVVNPRNLRF GTAAVFACNH LSYMDTPALF GSLPFQFRIL ANHYLFRYPF IGWHLTRSGQ
VPIDQSSMRS QVAGLMRGVA SLKSGMPILI FPDGSRSSDG HVRQFMAGAA YMAIKAQVPL
VPLALIGTFE LLPMHTYHLT PRPLMLVACE PIPTVGMTTK DADRLTNRLM ETIAAEYYER
SPLNRPEPLP ESQAKIPSAQ L
//
