ID A0A074MNA4_9SPHN Unreviewed; 247 AA.
AC A0A074MNA4;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=EH32_09585 {ECO:0000313|EMBL:KEO96471.1};
OS Erythrobacter litoralis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Erythrobacter.
OX NCBI_TaxID=39960 {ECO:0000313|EMBL:KEO96471.1, ECO:0000313|Proteomes:UP000027866};
RN [1] {ECO:0000313|EMBL:KEO96471.1, ECO:0000313|Proteomes:UP000027866}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 8509 {ECO:0000313|EMBL:KEO96471.1,
RC ECO:0000313|Proteomes:UP000027866};
RA Zheng Q.;
RT "A comprehensive comparison of genomes of Erythrobacter spp. Strains.";
RL Submitted (APR-2014) 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 -!- 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:KEO96471.1}.
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DR EMBL; JMIX01000005; KEO96471.1; -; Genomic_DNA.
DR RefSeq; WP_034902462.1; NZ_JMIX01000005.1.
DR AlphaFoldDB; A0A074MNA4; -.
DR KEGG; elq:Ga0102493_11819; -.
DR PATRIC; fig|39960.10.peg.3071; -.
DR OrthoDB; 9813296at2; -.
DR Proteomes; UP000027866; 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 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, ECO:0000313|EMBL:KEO96471.1};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Reference proteome {ECO:0000313|Proteomes:UP000027866}.
FT DOMAIN 27..228
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000259|Pfam:PF12697"
SQ SEQUENCE 247 AA; 26719 MW; 28B52A6E72090030 CRC64;
MTDIRFHDMP DGRRIALRKA DGAGPCLVFL PGYMSDMAGG KASALFEQAR DEGRAALLLD
YSGCGESSGS FADGTLSRWR DEVLALVESH VNAPIILVGS SMGGWLMLLV GEALGARDNG
RLAGMVGIAA APDFTRWGYS DEQRAQLAHG QIVYEDNPYG PEPTPTHPGF FADAESHMRL
GQEIAIRCPV RLLHGQCDAD VPWEVSLKLA EALRSDDVQV TLIKDGDHRL SRDADIALLK
RTVSTLT
//
