ID K3XQ16_SETIT Unreviewed; 398 AA.
AC K3XQ16;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=1-acylglycerol-3-phosphate O-acyltransferase {ECO:0000256|ARBA:ARBA00013211};
DE EC=2.3.1.51 {ECO:0000256|ARBA:ARBA00013211};
GN Name=101761251 {ECO:0000313|EnsemblPlants:KQL07249};
GN ORFNames=SETIT_5G340900v2 {ECO:0000313|EMBL:RCV27646.1};
OS Setaria italica (Foxtail millet) (Panicum italicum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Panicodae; Paniceae; Cenchrinae; Setaria.
OX NCBI_TaxID=4555 {ECO:0000313|EMBL:RCV27646.1};
RN [1] {ECO:0000313|EMBL:RCV27646.1, ECO:0000313|Proteomes:UP000004995}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Yugu1 {ECO:0000313|EnsemblPlants:KQL07249,
RC ECO:0000313|Proteomes:UP000004995}, and Yugu1
RC {ECO:0000313|EMBL:RCV27646.1};
RX PubMed=22580951; DOI=10.1038/nbt.2196;
RA Bennetzen J.L., Schmutz J., Wang H., Percifield R., Hawkins J.,
RA Pontaroli A.C., Estep M., Feng L., Vaughn J.N., Grimwood J., Jenkins J.,
RA Barry K., Lindquist E., Hellsten U., Deshpande S., Wang X., Wu X.,
RA Mitros T., Triplett J., Yang X., Ye C.Y., Mauro-Herrera M., Wang L., Li P.,
RA Sharma M., Sharma R., Ronald P.C., Panaud O., Kellogg E.A., Brutnell T.P.,
RA Doust A.N., Tuskan G.A., Rokhsar D., Devos K.M.;
RT "Reference genome sequence of the model plant Setaria.";
RL Nat. Biotechnol. 30:555-561(2012).
RN [2] {ECO:0000313|EMBL:RCV27646.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Yugu1 {ECO:0000313|EMBL:RCV27646.1};
RA Noorani M.;
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblPlants:KQL07249}
RP IDENTIFICATION.
RC STRAIN=Yugu1 {ECO:0000313|EnsemblPlants:KQL07249};
RG EnsemblPlants;
RL Submitted (AUG-2018) to UniProtKB.
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}.
CC -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-
CC diacylglycerol from sn-glycerol 3-phosphate: step 2/3.
CC {ECO:0000256|ARBA:ARBA00004728}.
CC -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate
CC acyltransferase family. {ECO:0000256|ARBA:ARBA00008655}.
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DR EMBL; AGNK02003329; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CM003532; RCV27646.1; -; Genomic_DNA.
DR RefSeq; XP_004970189.1; XM_004970132.2.
DR RefSeq; XP_004970190.1; XM_004970133.2.
DR AlphaFoldDB; K3XQ16; -.
DR STRING; 4555.K3XQ16; -.
DR EnsemblPlants; KQL07249; KQL07249; SETIT_003996mg.
DR GeneID; 101761251; -.
DR Gramene; KQL07249; KQL07249; SETIT_003996mg.
DR KEGG; sita:101761251; -.
DR eggNOG; KOG1505; Eukaryota.
DR HOGENOM; CLU_041844_0_0_1; -.
DR InParanoid; K3XQ16; -.
DR OMA; GTHAKKV; -.
DR OrthoDB; 2906776at2759; -.
DR UniPathway; UPA00557; UER00613.
DR Proteomes; UP000004995; Chromosome V.
DR GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0003841; F:1-acylglycerol-3-phosphate O-acyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0016746; F:acyltransferase activity; IBA:GO_Central.
DR GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd07990; LPLAT_LCLAT1-like; 1.
DR InterPro; IPR032098; Acyltransf_C.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR PANTHER; PTHR10983:SF76; 1-ACYL-SN-GLYCEROL-3-PHOSPHATE ACYLTRANSFERASE EPSILON; 1.
DR PANTHER; PTHR10983; 1-ACYLGLYCEROL-3-PHOSPHATE ACYLTRANSFERASE-RELATED; 1.
DR Pfam; PF16076; Acyltransf_C; 1.
DR Pfam; PF01553; Acyltransferase; 1.
DR SMART; SM00563; PlsC; 1.
DR SUPFAM; SSF69593; Glycerol-3-phosphate (1)-acyltransferase; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000004995};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 43..68
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 335..354
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 360..379
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 117..239
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 398 AA; 45634 MW; 89A3178488E53AAD CRC64;
MNGSNGSQEH HVSGEEEVHH VSRPILNNGP KHRPLTPMRQ CRGVACVAVI LSTAFLLIVY
LAPITTFVVR LFSVHYSRKA TSFLFGMWLS LWPFLFEKIN KTKVVFSGEN VIPKRRVLIF
ANHRTEVDWM YLWDLALRKG HLGYIKYILK SSLMKLPIFS WAFHIFEFIP VERKWEIDEA
IIQNKLSKFK NPRDPIWLAV FPEGTDYTEK KCIKSQEYAS EHGLPKLEHV LLPKTKGFIC
CLQQLRSSLD AVYDVTIAYK HRLPDFLDNV YGVDPSEVHI HIRTIQLSDI PTSEDEITEW
MIERFRQKDQ LLSDFFAKGH FPDEGTEGDL STPKCLANVF VIVGLTGICL YLTLFSSVWF
KIYVVASCAY LSFVTYYSVL PPQLVGSPEG GVKAKKAV
//
