ID   A0A8J0SV16_XENTR        Unreviewed;       373 AA.
AC   A0A8J0SV16;
DT   25-MAY-2022, integrated into UniProtKB/TrEMBL.
DT   25-MAY-2022, sequence version 1.
DT   22-FEB-2023, entry version 5.
DE   RecName: Full=1-acyl-sn-glycerol-3-phosphate acyltransferase {ECO:0000256|RuleBase:RU361267};
DE            EC=2.3.1.51 {ECO:0000256|RuleBase:RU361267};
GN   Name=agpat1 {ECO:0000313|RefSeq:XP_012823272.2};
GN   Synonyms=1-agpat1 {ECO:0000313|RefSeq:XP_012823272.2}, g15
GN   {ECO:0000313|RefSeq:XP_012823272.2}, lpaat-alpha
GN   {ECO:0000313|RefSeq:XP_012823272.2}, lpaata
GN   {ECO:0000313|RefSeq:XP_012823272.2};
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364 {ECO:0000313|Proteomes:UP000008143, ECO:0000313|RefSeq:XP_012823272.2};
RN   [1] {ECO:0000313|RefSeq:XP_012823272.2}
RP   IDENTIFICATION.
RC   STRAIN=Nigerian {ECO:0000313|RefSeq:XP_012823272.2};
RC   TISSUE=Liver and blood {ECO:0000313|RefSeq:XP_012823272.2};
RG   RefSeq;
RL   Submitted (APR-2022) to UniProtKB.
CC   -!- FUNCTION: Converts 1-acyl-sn-glycerol-3-phosphate (lysophosphatidic
CC       acid or LPA) into 1,2-diacyl-sn-glycerol-3-phosphate (phosphatidic acid
CC       or PA) by incorporating an acyl moiety at the sn-2 position of the
CC       glycerol backbone. {ECO:0000256|ARBA:ARBA00004086}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(11Z)-octadecenoyl-CoA + 1-(9Z-octadecenoyl)-sn-glycero-3-
CC         phosphate = 1-(9Z)-octadecenoyl-2-(11Z)-octadecenoyl-sn-glycero-3-
CC         phosphate + CoA; Xref=Rhea:RHEA:37603, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:74544, ChEBI:CHEBI:75121, ChEBI:CHEBI:75122;
CC         Evidence={ECO:0000256|ARBA:ARBA00000091};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37604;
CC         Evidence={ECO:0000256|ARBA:ARBA00000091};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(9Z)-octadecenoyl-CoA + 1-(6Z,9Z,12Z-octadecatrienoyl)-sn-
CC         glycero-3-phosphate = (6Z,9Z,12Z)-octadecatrienoyl-2-(9Z)-
CC         octadecenoyl-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:37179,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:74581,
CC         ChEBI:CHEBI:74582; Evidence={ECO:0000256|ARBA:ARBA00000191};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37180;
CC         Evidence={ECO:0000256|ARBA:ARBA00000191};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(9Z)-octadecenoyl-CoA + 1-(9Z,12Z,15Z)-octadecatrienoyl-sn-
CC         glycero-3-phosphate = 1-(9Z,12Z,15Z)-octadecatrienoyl-2-(9Z)-
CC         octadecenoyl-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:37139,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:74549,
CC         ChEBI:CHEBI:74550; Evidence={ECO:0000256|ARBA:ARBA00001322};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37140;
CC         Evidence={ECO:0000256|ARBA:ARBA00001322};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(9Z)-octadecenoyl-CoA + 1-(9Z-octadecenoyl)-sn-glycero-3-
CC         phosphate = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + CoA;
CC         Xref=Rhea:RHEA:37131, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387,
CC         ChEBI:CHEBI:74544, ChEBI:CHEBI:74546;
CC         Evidence={ECO:0000256|ARBA:ARBA00000045};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37132;
CC         Evidence={ECO:0000256|ARBA:ARBA00000045};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(9Z)-octadecenoyl-CoA + 1-eicosanoyl-sn-glycero-3-phosphate =
CC         1-eicosanoyl-2-(9Z)-octadecenoyl-sn-glycero-3-phosphate + CoA;
CC         Xref=Rhea:RHEA:37183, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387,
CC         ChEBI:CHEBI:74583, ChEBI:CHEBI:74584;
CC         Evidence={ECO:0000256|ARBA:ARBA00000892};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37184;
CC         Evidence={ECO:0000256|ARBA:ARBA00000892};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(9Z)-octadecenoyl-CoA + 1-hexadecanoyl-sn-glycero-3-phosphate
CC         = 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + CoA;
CC         Xref=Rhea:RHEA:33187, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387,
CC         ChEBI:CHEBI:57518, ChEBI:CHEBI:64839;
CC         Evidence={ECO:0000256|ARBA:ARBA00001203};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33188;
CC         Evidence={ECO:0000256|ARBA:ARBA00001203};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(9Z)-octadecenoyl-CoA + 1-tetradecanoyl-sn-glycerol 3-
CC         phosphate = 1-tetradecanoyl-2-(9Z)-octadecenoyl-sn-glycero-3-
CC         phosphate + CoA; Xref=Rhea:RHEA:37187, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57387, ChEBI:CHEBI:72683, ChEBI:CHEBI:74586;
CC         Evidence={ECO:0000256|ARBA:ARBA00001392};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37188;
CC         Evidence={ECO:0000256|ARBA:ARBA00001392};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(9Z,12Z)-octadecadienoyl-CoA + 1-(9Z-octadecenoyl)-sn-glycero-
CC         3-phosphate = 1-(9Z)-octadecenoyl-2-(9Z,12Z)-octadecadienoyl-sn-
CC         glycero-3-phosphate + CoA; Xref=Rhea:RHEA:37159, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57383, ChEBI:CHEBI:74544, ChEBI:CHEBI:74563;
CC         Evidence={ECO:0000256|ARBA:ARBA00001109};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37160;
CC         Evidence={ECO:0000256|ARBA:ARBA00001109};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + heptadecanoyl-CoA
CC         = 1-(9Z)-octadecenoyl-2-heptadecanoyl-sn-glycero-3-phosphate + CoA;
CC         Xref=Rhea:RHEA:37155, ChEBI:CHEBI:57287, ChEBI:CHEBI:74307,
CC         ChEBI:CHEBI:74544, ChEBI:CHEBI:74558;
CC         Evidence={ECO:0000256|ARBA:ARBA00001467};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37156;
CC         Evidence={ECO:0000256|ARBA:ARBA00001467};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + hexadecanoyl-CoA
CC         = 1-(9Z)-octadecenoyl-2-hexadecanoyl-sn-glycero-3-phosphate + CoA;
CC         Xref=Rhea:RHEA:37143, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379,
CC         ChEBI:CHEBI:74544, ChEBI:CHEBI:74551;
CC         Evidence={ECO:0000256|ARBA:ARBA00000816};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37144;
CC         Evidence={ECO:0000256|ARBA:ARBA00000816};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + pentadecanoyl-CoA
CC         = 1-(9Z)-octadecenoyl-2-pentadecanoyl-sn-glycero-3-phosphate + CoA;
CC         Xref=Rhea:RHEA:37175, ChEBI:CHEBI:57287, ChEBI:CHEBI:74309,
CC         ChEBI:CHEBI:74544, ChEBI:CHEBI:74578;
CC         Evidence={ECO:0000256|ARBA:ARBA00001880};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37176;
CC         Evidence={ECO:0000256|ARBA:ARBA00001880};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + tetradecanoyl-CoA
CC         = 1-(9Z)-octadecenoyl-2-tetradecanoyl-sn-glycero-3-phosphate + CoA;
CC         Xref=Rhea:RHEA:37171, ChEBI:CHEBI:57287, ChEBI:CHEBI:57385,
CC         ChEBI:CHEBI:74544, ChEBI:CHEBI:74579;
CC         Evidence={ECO:0000256|ARBA:ARBA00001783};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37172;
CC         Evidence={ECO:0000256|ARBA:ARBA00001783};
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:ARBA00000300};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19710;
CC         Evidence={ECO:0000256|ARBA:ARBA00000300};
CC   -!- DOMAIN: The HXXXXD motif is essential for acyltransferase activity and
CC       may constitute the binding site for the phosphate moiety of the
CC       glycerol-3-phosphate. {ECO:0000256|RuleBase:RU361267}.
CC   -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate
CC       acyltransferase family. {ECO:0000256|ARBA:ARBA00008655,
CC       ECO:0000256|RuleBase:RU361267}.
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   RefSeq; XP_012823272.2; XM_012967818.3.
DR   Proteomes; UP000008143; Chromosome 8.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0003841; F:1-acylglycerol-3-phosphate O-acyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd07989; LPLAT_AGPAT-like; 1.
DR   InterPro; IPR004552; AGP_acyltrans.
DR   InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR   PANTHER; PTHR10434; 1-ACYL-SN-GLYCEROL-3-PHOSPHATE ACYLTRANSFERASE; 1.
DR   PANTHER; PTHR10434:SF11; 1-ACYL-SN-GLYCEROL-3-PHOSPHATE ACYLTRANSFERASE ALPHA; 1.
DR   Pfam; PF01553; Acyltransferase; 1.
DR   SMART; SM00563; PlsC; 1.
DR   SUPFAM; SSF69593; Glycerol-3-phosphate (1)-acyltransferase; 1.
DR   TIGRFAMs; TIGR00530; AGP_acyltrn; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU361267,
KW   ECO:0000313|RefSeq:XP_012823272.2};
KW   Lipid biosynthesis {ECO:0000256|RuleBase:RU361267};
KW   Lipid metabolism {ECO:0000256|RuleBase:RU361267};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phospholipid biosynthesis {ECO:0000256|RuleBase:RU361267};
KW   Phospholipid metabolism {ECO:0000256|RuleBase:RU361267};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008143};
KW   Transferase {ECO:0000256|RuleBase:RU361267};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        103..121
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        133..153
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        224..242
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          193..308
FT                   /note="Phospholipid/glycerol acyltransferase"
FT                   /evidence="ECO:0000259|SMART:SM00563"
SQ   SEQUENCE   373 AA;  41803 MW;  BFDD375914DE597E CRC64;
     MLTTPLVSDN RYDAASCVRA GVEYTFRAHR VFFCCSAEIL QKDRRLTDRP LCRFHAGMSS
     NVVKAASPLA SAVTGKLQFP WQCNLQSGRP FCNNFANTGA MELSVAQWLL VVCLVAFPLL
     YEWSVSFKYF CKMAFYNGWI LTLAILAIPI CAVRGRNVEN MKVLQFMLLH IKYLYGIKIE
     VRGWENFNIK EPYVVVSNHQ SSLDLLGMME ILPSRCVPIA KRELMYAGTA GLACWLAGVI
     FINRKKTDDA ISVMTEAAET MLKEDVRVWV FPEGTRNHSG SLLPFKRGAF HLAVKAQVPV
     IPVVMSSYKD FYCKKERKFT TGKCTVRILP GVHTKGLSSD DVPELADRVR GMMLEAFSQM
     SSERPGKGPG GVH
//