ID A0A074JVB2_9RHOB Unreviewed; 248 AA.
AC A0A074JVB2;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 26.
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 ORFNames=DT23_02785 {ECO:0000313|EMBL:KEO60429.1};
OS Thioclava indica.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Thioclava.
OX NCBI_TaxID=1353528 {ECO:0000313|EMBL:KEO60429.1, ECO:0000313|Proteomes:UP000027471};
RN [1] {ECO:0000313|EMBL:KEO60429.1, ECO:0000313|Proteomes:UP000027471}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DT23-4 {ECO:0000313|EMBL:KEO60429.1,
RC ECO:0000313|Proteomes:UP000027471};
RX PubMed=25361528; DOI=10.1007/s10482-014-0320-3;
RA Liu Y., Lai Q., Du J., Xu H., Jiang L., Shao Z.;
RT "Thioclava indica sp. nov., isolated from surface seawater of the Indian
RT Ocean.";
RL Antonie Van Leeuwenhoek 107:297-304(2015).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KEO60429.1}.
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DR EMBL; AUNB01000018; KEO60429.1; -; Genomic_DNA.
DR RefSeq; WP_038129605.1; NZ_AUNB01000018.1.
DR AlphaFoldDB; A0A074JVB2; -.
DR STRING; 1353528.DT23_02785; -.
DR eggNOG; COG1073; Bacteria.
DR OrthoDB; 9813296at2; -.
DR Proteomes; UP000027471; Unassembled WGS sequence.
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 InterPro; IPR022742; Hydrolase_4.
DR PANTHER; PTHR16138; MYCOPHENOLIC ACID ACYL-GLUCURONIDE ESTERASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR16138:SF7; PALMITOYL-PROTEIN THIOESTERASE ABHD10, MITOCHONDRIAL; 1.
DR Pfam; PF12146; Hydrolase_4; 1.
DR PRINTS; PR00111; ABHYDROLASE.
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:UP000027471}.
FT DOMAIN 45..129
FT /note="Serine aminopeptidase S33"
FT /evidence="ECO:0000259|Pfam:PF12146"
SQ SEQUENCE 248 AA; 27029 MW; E6E8C3A824284DD2 CRC64;
MTEYLDTPEA RRIAYNLTPG TGPGVVFLGG FKSDMEGTKA LALENWARAQ GRAFLRFDYS
GHGVSGGAFD EGAIGDWYED ARDVIMALTE GPQILVGSSM GGWISLLMAR EHPEKIAGLV
TIAAAPDFTE DGYWASFDQE TRHKLESQGS VEVPSDYGDP YVITRRLINE GRTRLVLRSP
LALPFPTRFL QGTADSAVST ETALRLLDHA DGTDMRLTLV KGADHRFSTS ECLTLIKTAL
AEVIDAQQ
//
