MBLC2_BOVIN
ID MBLC2_BOVIN Reviewed; 279 AA.
AC A5PJT0;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Acyl-coenzyme A thioesterase MBLAC2;
DE Short=Acyl-CoA thioesterase MBLAC2;
DE EC=3.1.2.2 {ECO:0000250|UniProtKB:Q68D91};
DE AltName: Full=Beta-lactamase MBLAC2;
DE EC=3.5.2.6 {ECO:0000250|UniProtKB:Q68D91};
DE AltName: Full=Metallo-beta-lactamase domain-containing protein 2;
DE AltName: Full=Palmitoyl-coenzyme A thioesterase MBLAC2;
GN Name=MBLAC2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Acyl-CoA thioesterases are a group of enzymes that catalyze
CC the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A
CC (CoASH), providing the potential to regulate intracellular levels of
CC acyl-CoAs, free fatty acids and CoASH. Has an acyl-CoA thioesterase
CC activity towards the long chain fatty acyl-CoA thioester palmitoyl-CoA
CC (hexadecanoyl-CoA; C16:0-CoA). Displays a substrate preference for
CC fatty acyl-CoAs with chain-lengths C12-C18.
CC {ECO:0000250|UniProtKB:Q68D91}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + hexadecanoyl-CoA = CoA + H(+) + hexadecanoate;
CC Xref=Rhea:RHEA:16645, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379; EC=3.1.2.2;
CC Evidence={ECO:0000250|UniProtKB:Q68D91};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dodecanoyl-CoA + H2O = CoA + dodecanoate + H(+);
CC Xref=Rhea:RHEA:30135, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:18262, ChEBI:CHEBI:57287, ChEBI:CHEBI:57375;
CC Evidence={ECO:0000250|UniProtKB:Q68D91};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30136;
CC Evidence={ECO:0000250|UniProtKB:Q68D91};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + tetradecanoyl-CoA = CoA + H(+) + tetradecanoate;
CC Xref=Rhea:RHEA:40119, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30807, ChEBI:CHEBI:57287, ChEBI:CHEBI:57385;
CC Evidence={ECO:0000250|UniProtKB:Q68D91};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40120;
CC Evidence={ECO:0000250|UniProtKB:Q68D91};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + octadecanoyl-CoA = CoA + H(+) + octadecanoate;
CC Xref=Rhea:RHEA:30139, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:25629, ChEBI:CHEBI:57287, ChEBI:CHEBI:57394;
CC Evidence={ECO:0000250|UniProtKB:Q68D91};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30140;
CC Evidence={ECO:0000250|UniProtKB:Q68D91};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a beta-lactam + H2O = a substituted beta-amino acid;
CC Xref=Rhea:RHEA:20401, ChEBI:CHEBI:15377, ChEBI:CHEBI:35627,
CC ChEBI:CHEBI:140347; EC=3.5.2.6;
CC Evidence={ECO:0000250|UniProtKB:Q68D91};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q68D91};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:Q68D91};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q68D91}; Lipid-anchor
CC {ECO:0000250|UniProtKB:Q68D91}. Cell membrane
CC {ECO:0000250|UniProtKB:Q68D91}; Lipid-anchor
CC {ECO:0000250|UniProtKB:Q68D91}.
CC -!- PTM: Palmitoylated on Cys-254 by ZDHHC20.
CC {ECO:0000250|UniProtKB:Q68D91}.
CC -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily.
CC Glyoxalase II family. {ECO:0000305}.
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DR EMBL; BC142228; AAI42229.1; -; mRNA.
DR RefSeq; NP_001092549.1; NM_001099079.2.
DR AlphaFoldDB; A5PJT0; -.
DR SMR; A5PJT0; -.
DR STRING; 9913.ENSBTAP00000018096; -.
DR PaxDb; A5PJT0; -.
DR PRIDE; A5PJT0; -.
DR Ensembl; ENSBTAT00000018096; ENSBTAP00000018096; ENSBTAG00000013612.
DR GeneID; 537692; -.
DR KEGG; bta:537692; -.
DR CTD; 153364; -.
DR VEuPathDB; HostDB:ENSBTAG00000013612; -.
DR VGNC; VGNC:31282; MBLAC2.
DR eggNOG; KOG0813; Eukaryota.
DR GeneTree; ENSGT00390000017819; -.
DR HOGENOM; CLU_030571_0_2_1; -.
DR InParanoid; A5PJT0; -.
DR OMA; VASHTHF; -.
DR OrthoDB; 1203911at2759; -.
DR TreeFam; TF319889; -.
DR Proteomes; UP000009136; Chromosome 7.
DR Bgee; ENSBTAG00000013612; Expressed in occipital lobe and 103 other tissues.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008800; F:beta-lactamase activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0102991; F:myristoyl-CoA hydrolase activity; IEA:RHEA.
DR GO; GO:0016290; F:palmitoyl-CoA hydrolase activity; IEA:Ensembl.
DR GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.60.15.10; -; 1.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR Pfam; PF00753; Lactamase_B; 1.
DR SMART; SM00849; Lactamase_B; 1.
DR SUPFAM; SSF56281; SSF56281; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cell membrane; Endoplasmic reticulum; Fatty acid metabolism;
KW Hydrolase; Lipid metabolism; Lipoprotein; Membrane; Metal-binding;
KW Palmitate; Reference proteome; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q68D91"
FT CHAIN 2..279
FT /note="Acyl-coenzyme A thioesterase MBLAC2"
FT /id="PRO_0000325934"
FT BINDING 83
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 85
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 87
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q68D91"
FT BINDING 88
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q68D91"
FT BINDING 170
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 189
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 189
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 231
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q68D91"
FT LIPID 254
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:Q68D91"
SQ SEQUENCE 279 AA; 31257 MW; 745340A95CEC51F3 CRC64;
MSALEWYAHK SLGDGIFWIQ ERFYESGNRA NIWLVRGSEQ DVVIDTGLGL RSLPEYLYSS
GLLRDRAARD NAACRPLLAV ATHVHFDHSG GLYQFDRVAV HHAEAEALAR GDNFETVTWL
SDSEVVRAPS PGWRARQFRV QAVQPTLVLQ DGDVINLGDR QLTVMHMPGH SRGSICLHDK
DRKILFSGDV VYDGSLIDWL PYSRISDYVG TCERLIELVD RGLVEKVLPG HFNTFGAERL
FRLASNYISK AGICHKVSTF AMRSLASLAL RVTNSRTSP
