PLSY2_DEHM1
ID PLSY2_DEHM1 Reviewed; 210 AA.
AC Q3Z7W1;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 25-MAY-2022, entry version 85.
DE RecName: Full=Glycerol-3-phosphate acyltransferase 2 {ECO:0000255|HAMAP-Rule:MF_01043};
DE AltName: Full=Acyl-PO4 G3P acyltransferase 2 {ECO:0000255|HAMAP-Rule:MF_01043};
DE AltName: Full=Acyl-phosphate--glycerol-3-phosphate acyltransferase 2 {ECO:0000255|HAMAP-Rule:MF_01043};
DE AltName: Full=G3P acyltransferase 2 {ECO:0000255|HAMAP-Rule:MF_01043};
DE Short=GPAT 2 {ECO:0000255|HAMAP-Rule:MF_01043};
DE EC=2.3.1.275 {ECO:0000255|HAMAP-Rule:MF_01043};
DE AltName: Full=Lysophosphatidic acid synthase 2 {ECO:0000255|HAMAP-Rule:MF_01043};
DE Short=LPA synthase 2 {ECO:0000255|HAMAP-Rule:MF_01043};
GN Name=plsY2 {ECO:0000255|HAMAP-Rule:MF_01043}; OrderedLocusNames=DET0965;
OS Dehalococcoides mccartyi (strain ATCC BAA-2266 / KCTC 15142 / 195)
OS (Dehalococcoides ethenogenes (strain 195)).
OC Bacteria; Chloroflexi; Dehalococcoidia; Dehalococcoidales;
OC Dehalococcoidaceae; Dehalococcoides.
OX NCBI_TaxID=243164;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-2266 / KCTC 15142 / 195;
RX PubMed=15637277; DOI=10.1126/science.1102226;
RA Seshadri R., Adrian L., Fouts D.E., Eisen J.A., Phillippy A.M., Methe B.A.,
RA Ward N.L., Nelson W.C., DeBoy R.T., Khouri H.M., Kolonay J.F., Dodson R.J.,
RA Daugherty S.C., Brinkac L.M., Sullivan S.A., Madupu R., Nelson K.E.,
RA Kang K.H., Impraim M., Tran K., Robinson J.M., Forberger H.A., Fraser C.M.,
RA Zinder S.H., Heidelberg J.F.;
RT "Genome sequence of the PCE-dechlorinating bacterium Dehalococcoides
RT ethenogenes.";
RL Science 307:105-108(2005).
CC -!- FUNCTION: Catalyzes the transfer of an acyl group from acyl-phosphate
CC (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form lysophosphatidic
CC acid (LPA). This enzyme utilizes acyl-phosphate as fatty acyl donor,
CC but not acyl-CoA or acyl-ACP. {ECO:0000255|HAMAP-Rule:MF_01043}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an acyl phosphate + sn-glycerol 3-phosphate = a 1-acyl-sn-
CC glycero-3-phosphate + phosphate; Xref=Rhea:RHEA:34075,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57597, ChEBI:CHEBI:57970,
CC ChEBI:CHEBI:59918; EC=2.3.1.275; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01043};
CC -!- PATHWAY: Lipid metabolism; phospholipid metabolism. {ECO:0000255|HAMAP-
CC Rule:MF_01043}.
CC -!- SUBUNIT: Probably interacts with PlsX. {ECO:0000255|HAMAP-
CC Rule:MF_01043}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01043};
CC Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01043}.
CC -!- SIMILARITY: Belongs to the PlsY family. {ECO:0000255|HAMAP-
CC Rule:MF_01043}.
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DR EMBL; CP000027; AAW39729.1; -; Genomic_DNA.
DR RefSeq; WP_010936667.1; NC_002936.3.
DR AlphaFoldDB; Q3Z7W1; -.
DR SMR; Q3Z7W1; -.
DR STRING; 243164.DET0965; -.
DR EnsemblBacteria; AAW39729; AAW39729; DET0965.
DR KEGG; det:DET0965; -.
DR eggNOG; COG0344; Bacteria.
DR HOGENOM; CLU_081254_7_1_0; -.
DR OMA; PRMKEIK; -.
DR OrthoDB; 1691856at2; -.
DR UniPathway; UPA00085; -.
DR Proteomes; UP000008289; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043772; F:acyl-phosphate glycerol-3-phosphate acyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-UniRule.
DR HAMAP; MF_01043; PlsY; 1.
DR InterPro; IPR003811; G3P_acylTferase_PlsY.
DR PANTHER; PTHR30309; PTHR30309; 1.
DR Pfam; PF02660; G3P_acyltransf; 1.
DR SMART; SM01207; G3P_acyltransf; 1.
PE 3: Inferred from homology;
KW Cell membrane; Lipid biosynthesis; Lipid metabolism; Membrane;
KW Phospholipid biosynthesis; Phospholipid metabolism; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..210
FT /note="Glycerol-3-phosphate acyltransferase 2"
FT /id="PRO_0000188354"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01043"
FT TRANSMEM 54..74
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01043"
FT TRANSMEM 82..102
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01043"
FT TRANSMEM 114..134
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01043"
FT TRANSMEM 141..161
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01043"
FT TRANSMEM 163..183
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01043"
SQ SEQUENCE 210 AA; 22803 MW; 5A1B5659CDF1FA4E CRC64;
MNSLIMVIIA LIAAYFIGST PAPYLAGRIF KGIDIRTVGS KNMGSMNVFY NVGFWPGILV
LAVDIGKGAL AMAVANWLGE GLGIQMLCAL MAIAGHNYPV WLKFKGGKGG ATAIGILAYL
MPEGIPIYIA CFLVLMAITR FPTLSYGISF LSFILVAWLG QHDLGKVLFS LLVVMIPIIM
YIPRMKEIKN KAGSGNAKRA IFRKNLKERL
