ID G5C204_HETGA Unreviewed; 334 AA.
AC G5C204;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=1-acylglycerol-3-phosphate O-acyltransferase ABHD5 {ECO:0000256|ARBA:ARBA00040731};
DE EC=2.3.1.51 {ECO:0000256|ARBA:ARBA00013211};
DE AltName: Full=Abhydrolase domain-containing protein 5 {ECO:0000256|ARBA:ARBA00042413};
DE Flags: Fragment;
GN ORFNames=GW7_17571 {ECO:0000313|EMBL:EHB15565.1};
OS Heterocephalus glaber (Naked mole rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Heterocephalus.
OX NCBI_TaxID=10181 {ECO:0000313|EMBL:EHB15565.1, ECO:0000313|Proteomes:UP000006813};
RN [1] {ECO:0000313|EMBL:EHB15565.1, ECO:0000313|Proteomes:UP000006813}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21993625; DOI=10.1038/nature10533;
RA Kim E.B., Fang X., Fushan A.A., Huang Z., Lobanov A.V., Han L.,
RA Marino S.M., Sun X., Turanov A.A., Yang P., Yim S.H., Zhao X.,
RA Kasaikina M.V., Stoletzki N., Peng C., Polak P., Xiong Z., Kiezun A.,
RA Zhu Y., Chen Y., Kryukov G.V., Zhang Q., Peshkin L., Yang L., Bronson R.T.,
RA Buffenstein R., Wang B., Han C., Li Q., Chen L., Zhao W., Sunyaev S.R.,
RA Park T.J., Zhang G., Wang J., Gladyshev V.N.;
RT "Genome sequencing reveals insights into physiology and longevity of the
RT naked mole rat.";
RL Nature 479:223-227(2011).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + 1-(9Z-octadecenoyl)-sn-
CC glycero-3-phosphate = 1-(9Z)-octadecenoyl-2-(5Z,8Z,11Z,14Z)-
CC eicosatetraenoyl-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:37443,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57368, ChEBI:CHEBI:74544,
CC ChEBI:CHEBI:74928; Evidence={ECO:0000256|ARBA:ARBA00036590};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37444;
CC Evidence={ECO:0000256|ARBA:ARBA00036590};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-
CC glycero-3-phosphate = 1-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-2-(9Z)-
CC octadecenoyl-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:37455,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:74938,
CC ChEBI:CHEBI:74941; Evidence={ECO:0000256|ARBA:ARBA00035818};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37456;
CC Evidence={ECO:0000256|ARBA:ARBA00035818};
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-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-octadecanoyl-sn-glycero-3-phosphate
CC = 1-octadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + CoA;
CC Xref=Rhea:RHEA:37163, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387,
CC ChEBI:CHEBI:74560, ChEBI:CHEBI:74565;
CC Evidence={ECO:0000256|ARBA:ARBA00036294};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37164;
CC Evidence={ECO:0000256|ARBA:ARBA00036294};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + eicosanoyl-CoA =
CC 1-(9Z)-octadecenoyl-2-eicosanoyl-sn-glycero-3-phosphate + CoA;
CC Xref=Rhea:RHEA:37451, ChEBI:CHEBI:57287, ChEBI:CHEBI:57380,
CC ChEBI:CHEBI:74544, ChEBI:CHEBI:74937;
CC Evidence={ECO:0000256|ARBA:ARBA00036557};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37452;
CC Evidence={ECO:0000256|ARBA:ARBA00036557};
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 + octadecanoyl-CoA
CC = 1-(9Z-octadecenoyl)-2-octadecanoyl-sn-glycero-3-phosphate + CoA;
CC Xref=Rhea:RHEA:37147, ChEBI:CHEBI:57287, ChEBI:CHEBI:57394,
CC ChEBI:CHEBI:74544, ChEBI:CHEBI:74552;
CC Evidence={ECO:0000256|ARBA:ARBA00036296};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37148;
CC Evidence={ECO:0000256|ARBA:ARBA00036296};
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the peptidase S33 family. ABHD4/ABHD5 subfamily.
CC {ECO:0000256|ARBA:ARBA00038097}.
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DR EMBL; JH172944; EHB15565.1; -; Genomic_DNA.
DR AlphaFoldDB; G5C204; -.
DR STRING; 10181.G5C204; -.
DR eggNOG; KOG4409; Eukaryota.
DR InParanoid; G5C204; -.
DR Proteomes; UP000006813; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR PANTHER; PTHR42886:SF34; 1-ACYLGLYCEROL-3-PHOSPHATE O-ACYLTRANSFERASE ABHD5; 1.
DR PANTHER; PTHR42886; RE40534P-RELATED; 1.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR PRINTS; PR00111; ABHYDROLASE.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000313|EMBL:EHB15565.1};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Phospholipid biosynthesis {ECO:0000256|ARBA:ARBA00023209};
KW Phospholipid metabolism {ECO:0000256|ARBA:ARBA00023264};
KW Reference proteome {ECO:0000313|Proteomes:UP000006813};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EHB15565.1}.
FT DOMAIN 62..317
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000259|Pfam:PF00561"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EHB15565.1"
SQ SEQUENCE 334 AA; 37277 MW; A463D89EAE94650B CRC64;
RSGWLSGWLP TWCPTSPLLL KEAEEKMLKC VPCTYQKERV LVSNGNKIWT LKFSQDISNK
TPLILLHGFG GGLGLWALNF GALSADRPVY AFDLLGFGRS SRPRFDSDAE EAENQFVESV
EEWRCALGLE RMILLGHNLG GFLAAAYALK YPLRVSHLIL VEPWGFPERP DLADQDRPIP
VWIRALGAAL TPFNPLAGLR IAGPFGLSLV QRLRPDFKRK YSSMFEDDTV AEYIYHCNVQ
TPSGETAFKN MTIPYGWAKR PMLLRIGKLH PDVPVTVIFG ARSCIDGNSG SSIQSLRPQS
YVKTIAILGA GHYVYADQPE EFNQKVKEIC SSVD
//
