ID H3AE51_LATCH Unreviewed; 351 AA.
AC H3AE51;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 56.
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};
GN Name=ABHD5 {ECO:0000313|Ensembl:ENSLACP00000007922.1};
OS Latimeria chalumnae (Coelacanth).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Coelacanthiformes; Coelacanthidae; Latimeria.
OX NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000007922.1, ECO:0000313|Proteomes:UP000008672};
RN [1] {ECO:0000313|Proteomes:UP000008672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wild caught {ECO:0000313|Proteomes:UP000008672};
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E., Lindblad-Toh K.;
RT "The draft genome of Latimeria chalumnae.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLACP00000007922.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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; AFYH01200541; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01200542; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01200543; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01200544; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01200545; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_006008899.1; XM_006008837.2.
DR AlphaFoldDB; H3AE51; -.
DR MEROPS; S33.975; -.
DR Ensembl; ENSLACT00000007988.1; ENSLACP00000007922.1; ENSLACG00000007012.1.
DR GeneID; 102354368; -.
DR KEGG; lcm:102354368; -.
DR CTD; 566493; -.
DR GeneTree; ENSGT00390000016277; -.
DR HOGENOM; CLU_017361_0_0_1; -.
DR OrthoDB; 276964at2759; -.
DR Proteomes; UP000008672; Unassembled WGS sequence.
DR Bgee; ENSLACG00000007012; Expressed in pectoral fin and 6 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016740; F:transferase 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 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:UP000008672};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 79..332
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000259|Pfam:PF00561"
SQ SEQUENCE 351 AA; 39535 MW; DB62BCE013062320 CRC64;
MKLEENMAEQ ALVPVESRSG WLSSWLPAWC PTSVLLLQEA EEKMLQCIKS KYTKQYVLIS
NGNRIWTLTF NQHHSSKSPL VLLHGFGGGL GLWVLNFDAL CQQRTVYSID LLGFGRSSRP
QLSTDAEEVE NQFVNSIEEW RAKVGVEKMI LLGHNLGGYL AAAYSLKYPS RVKHLVLVEP
WGFPERPNSP EQDRPIPIWI KAIAAMLSPF NPLAGLRVAG PFGLGLVQRL RPDFKQKYFS
LFEDETVTEY IYHCNVQTPS GETAFKNMTI PYGWAKRPML KRIDQIQADI PITVIYGARS
CIDGNSGIAI KALRANSYVE TIPVRGAGHY VYADQPEDFN QKVIEICNSL D
//
