ID A1B0M3_PARDP Unreviewed; 249 AA.
AC A1B0M3;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=Palmitoyl-protein thioesterase ABHD10, mitochondrial {ECO:0000256|ARBA:ARBA00039314};
DE EC=3.1.1.93 {ECO:0000256|ARBA:ARBA00039132};
DE AltName: Full=Acyl-protein thioesterase ABHD10 {ECO:0000256|ARBA:ARBA00042645};
DE AltName: Full=Alpha/beta hydrolase domain-containing protein 10 {ECO:0000256|ARBA:ARBA00042704};
DE AltName: Full=Mycophenolic acid acyl-glucuronide esterase, mitochondrial {ECO:0000256|ARBA:ARBA00041520};
GN OrderedLocusNames=Pden_0956 {ECO:0000313|EMBL:ABL69067.1};
OS Paracoccus denitrificans (strain Pd 1222).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Paracoccus.
OX NCBI_TaxID=318586 {ECO:0000313|EMBL:ABL69067.1, ECO:0000313|Proteomes:UP000000361};
RN [1] {ECO:0000313|Proteomes:UP000000361}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pd 1222 {ECO:0000313|Proteomes:UP000000361};
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Spiro S.,
RA Richardson D.J., Moir J.W.B., Ferguson S.J., van Spanning R.J.M.,
RA Richardson P.;
RT "Complete sequence of chromosome 1 of Paracoccus denitrificans PD1222.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + S-hexadecanoyl-L-cysteinyl-[protein] = H(+) +
CC hexadecanoate + L-cysteinyl-[protein]; Xref=Rhea:RHEA:19233,
CC Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:11032, ChEBI:CHEBI:7896,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950,
CC ChEBI:CHEBI:74151; EC=3.1.2.22;
CC Evidence={ECO:0000256|ARBA:ARBA00037021};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19234;
CC Evidence={ECO:0000256|ARBA:ARBA00037021};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + mycophenolic acid O-acyl-beta-D-glucuronide = D-
CC glucuronate + H(+) + mycophenolate; Xref=Rhea:RHEA:34179,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58720,
CC ChEBI:CHEBI:62932, ChEBI:CHEBI:66982; EC=3.1.1.93;
CC Evidence={ECO:0000256|ARBA:ARBA00035894};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:34180;
CC Evidence={ECO:0000256|ARBA:ARBA00035894};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000489; ABL69067.1; -; Genomic_DNA.
DR RefSeq; WP_011747295.1; NC_008686.1.
DR AlphaFoldDB; A1B0M3; -.
DR STRING; 318586.Pden_0956; -.
DR ESTHER; pardp-a1b0m3; AlphaBeta_hydrolase.
DR EnsemblBacteria; ABL69067; ABL69067; Pden_0956.
DR GeneID; 75500493; -.
DR KEGG; pde:Pden_0956; -.
DR eggNOG; COG1073; Bacteria.
DR HOGENOM; CLU_066961_0_0_5; -.
DR OrthoDB; 9813296at2; -.
DR Proteomes; UP000000361; Chromosome 1.
DR GO; GO:0016787; F:hydrolase activity; 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; PTHR16138; MYCOPHENOLIC ACID ACYL-GLUCURONIDE ESTERASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR16138:SF7; PALMITOYL-PROTEIN THIOESTERASE ABHD10, MITOCHONDRIAL; 1.
DR Pfam; PF12697; Abhydrolase_6; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Reference proteome {ECO:0000313|Proteomes:UP000000361}.
FT DOMAIN 25..228
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000259|Pfam:PF12697"
SQ SEQUENCE 249 AA; 27195 MW; C61563CF5742FCD0 CRC64;
MTQFLEGPQG RRIAYNRIEG QGPGVVFLGG FRSDMQGTKA LWLEDWARAR GRAFLRFDYS
GHGESSGMFE EGAIGDWFAD AMAAIRGLTE GRQVLVGSSM GGWIGLLLAR TMPERLAGLV
TVAAAPDFTE RGYWAGFSAA ERAALLERGR VEQPSDYGDA PYVITRRLIE DGRDHLVLDQ
PLPLPFPVRF LQGTEDADVP MSWALDLLAH GKGEDMRLVL VKGADHRFST PDCLALIGDA
LDEVLARAG
//
