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Database: UniProt
Entry: E6YXI5_BARSR
LinkDB: E6YXI5_BARSR
Original site: E6YXI5_BARSR 
ID   E6YXI5_BARSR            Unreviewed;       264 AA.
AC   E6YXI5;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   27-MAR-2024, entry version 35.
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=B11C_10047 {ECO:0000313|EMBL:CBI81573.1}, BscR1v2_000480
GN   {ECO:0000313|EMBL:AQX30005.1};
OS   Bartonella schoenbuchensis (strain DSM 13525 / NCTC 13165 / R1).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Bartonellaceae; Bartonella.
OX   NCBI_TaxID=687861 {ECO:0000313|EMBL:CBI81573.1};
RN   [1] {ECO:0000313|EMBL:CBI81573.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=R1 {ECO:0000313|EMBL:CBI81573.1};
RX   PubMed=21347280; DOI=10.1371/journal.pgen.1001296;
RA   Engel P., Salzburger W., Liesch M., Chang C.C., Maruyama S., Lanz C.,
RA   Calteau A., Lajus A., Medigue C., Schuster S.C., Dehio C.;
RT   "Parallel evolution of a type IV secretion system in radiating lineages of
RT   the host-restricted bacterial pathogen Bartonella.";
RL   PLoS Genet. 7:E1001296-E1001296(2011).
RN   [2] {ECO:0000313|Proteomes:UP000190811}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R1 {ECO:0000313|Proteomes:UP000190811};
RX   PubMed=28338931; DOI=10.1093/gbe/evx042;
RA   Harms A., Segers F.H., Quebatte M., Mistl C., Manfredi P., Korner J.,
RA   Chomel B.B., Kosoy M., Maruyama S., Engel P., Dehio C.;
RT   "Evolutionary Dynamics of Pathoadaptation Revealed by Three Independent
RT   Acquisitions of the VirB/D4 Type IV Secretion System in Bartonella.";
RL   Genome Biol. Evol. 9:761-776(2017).
RN   [3] {ECO:0000313|EMBL:AQX30005.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R1 {ECO:0000313|EMBL:AQX30005.1};
RA   Harms A., Segers F.H.I.D., Quebatte M., Mistl C., Manfredi P., Koerner J.,
RA   Chomel B., Kosoy M., Maruyama S., Engel P., Dehio C.;
RT   "Evolutionary dynamics of pathoadaptation revealed by three independent
RT   acquisitions of the VirB/D4 type IV secretion system in Bartonella.";
RL   Submitted (FEB-2017) 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}.
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DR   EMBL; CP019789; AQX30005.1; -; Genomic_DNA.
DR   EMBL; FN645506; CBI81573.1; -; Genomic_DNA.
DR   AlphaFoldDB; E6YXI5; -.
DR   STRING; 687861.BscR1v2_000480; -.
DR   Proteomes; UP000190811; Chromosome.
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}.
FT   DOMAIN          49..241
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000259|Pfam:PF12697"
SQ   SEQUENCE   264 AA;  29582 MW;  B14A0E3CB67256E3 CRC64;
     MIDQNIPCQF FSFEDTVLAV RHRKGSRSPG LVWLSGYRSD MLGSKAMVVD AFAQKNNLSC
     LRFDYSGHGE SEGDFFEGTI SRWVKESLAI FEAYCEGPQI LIGSSMGGWI ALRLAMMLAQ
     QNKPLAGMIL IAPAPDFTQA LIEPTLTTVE WKALEEKGYF ERSSSYDLEP TPFTKALLED
     GRNNCVMKGC IDIGCSVHIL QGMEDEIVPY QHALALLDHL PLHDVTLTLV RDANHRFSRP
     QDLDCFEKVL MSLIDRINEP SRSS
//
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