LPAT_CHLRE
ID LPAT_CHLRE Reviewed; 332 AA.
AC A8J0J0;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2016, sequence version 2.
DT 25-MAY-2022, entry version 59.
DE RecName: Full=1-acyl-sn-glycerol-3-phosphate acyltransferase CHLREDRAFT_174358;
DE EC=2.3.1.51 {ECO:0000250|UniProtKB:Q8K3K7};
GN ORFNames=CHLREDRAFT_174358 {ECO:0000312|EMBL:EDP02300.1};
OS Chlamydomonas reinhardtii (Chlamydomonas smithii).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX NCBI_TaxID=3055;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC-503, and cw92;
RX PubMed=17932292; DOI=10.1126/science.1143609;
RA Merchant S.S., Prochnik S.E., Vallon O., Harris E.H., Karpowicz S.J.,
RA Witman G.B., Terry A., Salamov A., Fritz-Laylin L.K., Marechal-Drouard L.,
RA Marshall W.F., Qu L.H., Nelson D.R., Sanderfoot A.A., Spalding M.H.,
RA Kapitonov V.V., Ren Q., Ferris P., Lindquist E., Shapiro H., Lucas S.M.,
RA Grimwood J., Schmutz J., Cardol P., Cerutti H., Chanfreau G., Chen C.L.,
RA Cognat V., Croft M.T., Dent R., Dutcher S., Fernandez E., Fukuzawa H.,
RA Gonzalez-Ballester D., Gonzalez-Halphen D., Hallmann A., Hanikenne M.,
RA Hippler M., Inwood W., Jabbari K., Kalanon M., Kuras R., Lefebvre P.A.,
RA Lemaire S.D., Lobanov A.V., Lohr M., Manuell A., Meier I., Mets L.,
RA Mittag M., Mittelmeier T., Moroney J.V., Moseley J., Napoli C.,
RA Nedelcu A.M., Niyogi K., Novoselov S.V., Paulsen I.T., Pazour G.J.,
RA Purton S., Ral J.P., Riano-Pachon D.M., Riekhof W., Rymarquis L.,
RA Schroda M., Stern D., Umen J., Willows R., Wilson N., Zimmer S.L.,
RA Allmer J., Balk J., Bisova K., Chen C.J., Elias M., Gendler K., Hauser C.,
RA Lamb M.R., Ledford H., Long J.C., Minagawa J., Page M.D., Pan J.,
RA Pootakham W., Roje S., Rose A., Stahlberg E., Terauchi A.M., Yang P.,
RA Ball S., Bowler C., Dieckmann C.L., Gladyshev V.N., Green P., Jorgensen R.,
RA Mayfield S., Mueller-Roeber B., Rajamani S., Sayre R.T., Brokstein P.,
RA Dubchak I., Goodstein D., Hornick L., Huang Y.W., Jhaveri J., Luo Y.,
RA Martinez D., Ngau W.C., Otillar B., Poliakov A., Porter A., Szajkowski L.,
RA Werner G., Zhou K., Grigoriev I.V., Rokhsar D.S., Grossman A.R.;
RT "The Chlamydomonas genome reveals the evolution of key animal and plant
RT functions.";
RL Science 318:245-250(2007).
CC -!- FUNCTION: Converts lysophosphatidic acid (LPA) into phosphatidic acid
CC by incorporating an acyl moiety at the sn-2 position of the glycerol
CC backbone. {ECO:0000250|UniProtKB:Q8K3K7}.
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:0000250|UniProtKB:Q8K3K7};
CC -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-
CC diacylglycerol from sn-glycerol 3-phosphate: step 2/3.
CC {ECO:0000250|UniProtKB:Q8K3K7}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
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:0000305}.
CC -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate
CC acyltransferase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EDP02300.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; DS496130; EDP02300.1; ALT_SEQ; Genomic_DNA.
DR AlphaFoldDB; A8J0J0; -.
DR SMR; A8J0J0; -.
DR PaxDb; A8J0J0; -.
DR EnsemblPlants; PNW79030; PNW79030; CHLRE_09g398289v5.
DR Gramene; PNW79030; PNW79030; CHLRE_09g398289v5.
DR HOGENOM; CLU_1385958_0_0_1; -.
DR InParanoid; A8J0J0; -.
DR OrthoDB; 1623097at2759; -.
DR BRENDA; 2.3.1.51; 1318.
DR UniPathway; UPA00557; UER00613.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0003841; F:1-acylglycerol-3-phosphate O-acyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR004552; AGP_acyltrans.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR Pfam; PF01553; Acyltransferase; 1.
DR SMART; SM00563; PlsC; 1.
DR TIGRFAMs; TIGR00530; AGP_acyltrn; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Lipid biosynthesis; Lipid metabolism; Membrane;
KW Phospholipid biosynthesis; Phospholipid metabolism; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..332
FT /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
FT CHLREDRAFT_174358"
FT /id="PRO_0000438131"
FT TRANSMEM 96..116
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 185..205
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOTIF 163..168
FT /note="HXXXXD motif"
FT /evidence="ECO:0000305"
FT MOTIF 235..238
FT /note="EGTR motif"
FT /evidence="ECO:0000305"
SQ SEQUENCE 332 AA; 36241 MW; E61706E3D750725E CRC64;
MARKSSLAQA AIERKPVLLR PQLNVPRMSG ITALPMERRP LPVAPSPSAK PELPARSALV
CHAAAASVPL PNSDSAPQPN VLLAKIRAIM FFAWSFLLSL PLFVTMMVMA PLVLAFDKYR
RLAQHFVNNL WACASTAPFY KVTIIGRENL PPPDKPVVYV ANHQSFLDIY SLFHLQRPFK
FISKTSNFLI PIIGWSMFLT GHVMINRVDR RSQLKCLQQC RDLLAEGAPV LFFPEGTRSL
DCKMAGFKKG AFSVAAKAGV EVVPITLLGT GSLMPSGKES QLRPGQVTIV VHKALPPNKN
ADQLCDAARQ AVASSLPPEL VGSATEMAPD EQ
