ID D2S327_HALTV Unreviewed; 275 AA.
AC D2S327;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 56.
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=Htur_5143 {ECO:0000313|EMBL:ADB63774.1};
OS Haloterrigena turkmenica (strain ATCC 51198 / DSM 5511 / JCM 9101 / NCIMB
OS 13204 / VKM B-1734 / 4k) (Halococcus turkmenicus).
OG Plasmid pHTUR04 {ECO:0000313|EMBL:ADB63774.1,
OG ECO:0000313|Proteomes:UP000001903}.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Haloterrigena.
OX NCBI_TaxID=543526 {ECO:0000313|EMBL:ADB63774.1, ECO:0000313|Proteomes:UP000001903};
RN [1] {ECO:0000313|EMBL:ADB63774.1, ECO:0000313|Proteomes:UP000001903}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51198 / DSM 5511 / JCM 9101 / NCIMB 13204 / VKM B-1734 /
RC 4k {ECO:0000313|Proteomes:UP000001903};
RC PLASMID=pHTUR04 {ECO:0000313|EMBL:ADB63774.1,
RC ECO:0000313|Proteomes:UP000001903};
RX PubMed=21304683; DOI=10.4056/sigs.681272;
RA Saunders E., Tindall B.J., Fahnrich R., Lapidus A., Copeland A.,
RA Del Rio T.G., Lucas S., Chen F., Tice H., Cheng J.F., Han C., Detter J.C.,
RA Bruce D., Goodwin L., Chain P., Pitluck S., Pati A., Ivanova N.,
RA Mavromatis K., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J.,
RA Jeffries C.D., Brettin T., Rohde M., Goker M., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Klenk H.P., Kyrpides N.C.;
RT "Complete genome sequence of Haloterrigena turkmenica type strain (4k).";
RL Stand. Genomic Sci. 2:107-116(2010).
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; CP001864; ADB63774.1; -; Genomic_DNA.
DR RefSeq; WP_012946014.1; NC_013747.1.
DR AlphaFoldDB; D2S327; -.
DR ESTHER; haltv-d2s327; 6_AlphaBeta_hydrolase.
DR GeneID; 8745691; -.
DR KEGG; htu:Htur_5143; -.
DR eggNOG; arCOG01648; Archaea.
DR HOGENOM; CLU_066961_1_0_2; -.
DR OrthoDB; 7531at2157; -.
DR Proteomes; UP000001903; Plasmid pHTUR04.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
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; PF00561; Abhydrolase_1; 1.
DR PRINTS; PR00111; ABHYDROLASE.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 4: Predicted;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ADB63774.1};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Plasmid {ECO:0000313|EMBL:ADB63774.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 28..254
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000259|Pfam:PF00561"
FT REGION 142..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..173
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 275 AA; 30330 MW; D6CE638FC0EE5346 CRC64;
MTETEHRVTV ADGETVAAVH HEAPGDDWIV FCHGFLSDKT GSYERRCRRA VEHGYNAVRF
DFRGCGASDG RFVDQTLSDK LADLHAVLEY VAPPSIVLFG SSFGGKVAFH AAVDDERVEA
VATRAPVTYN RAFDEYRAIV EREDEPSGTS NRRAGAKRHA SREGPDGASG ETASEERHAN
CAGIYEFETG DRIDARFFDD FETYEFDDVA ASLSVPVAIF HGRDDDSVDI GDSVDAAAAL
ETDVLLEAFA TEGHRFSADA EDRLLERLFH WLETQ
//
