BIOH_XYLFM
ID BIOH_XYLFM Reviewed; 255 AA.
AC B0U6I9;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Pimeloyl-[acyl-carrier protein] methyl ester esterase {ECO:0000255|HAMAP-Rule:MF_01260};
DE EC=3.1.1.85 {ECO:0000255|HAMAP-Rule:MF_01260};
DE AltName: Full=Biotin synthesis protein BioH {ECO:0000255|HAMAP-Rule:MF_01260};
DE AltName: Full=Carboxylesterase BioH {ECO:0000255|HAMAP-Rule:MF_01260};
GN Name=bioH {ECO:0000255|HAMAP-Rule:MF_01260};
GN OrderedLocusNames=Xfasm12_0709;
OS Xylella fastidiosa (strain M12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xylella.
OX NCBI_TaxID=405440;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M12;
RX PubMed=20601474; DOI=10.1128/jb.00651-10;
RA Chen J., Xie G., Han S., Chertkov O., Sims D., Civerolo E.L.;
RT "Whole genome sequences of two Xylella fastidiosa strains (M12 and M23)
RT causing almond leaf scorch disease in California.";
RL J. Bacteriol. 192:4534-4534(2010).
CC -!- FUNCTION: The physiological role of BioH is to remove the methyl group
CC introduced by BioC when the pimeloyl moiety is complete. It allows to
CC synthesize pimeloyl-ACP via the fatty acid synthetic pathway through
CC the hydrolysis of the ester bonds of pimeloyl-ACP esters.
CC {ECO:0000255|HAMAP-Rule:MF_01260}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=6-carboxyhexanoyl-[ACP] methyl ester + H2O = 6-
CC carboxyhexanoyl-[ACP] + H(+) + methanol; Xref=Rhea:RHEA:42700,
CC Rhea:RHEA-COMP:9955, Rhea:RHEA-COMP:10186, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17790, ChEBI:CHEBI:78846,
CC ChEBI:CHEBI:82735; EC=3.1.1.85; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01260};
CC -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_01260}.
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01260}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01260}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Carboxylesterase
CC BioH family. {ECO:0000255|HAMAP-Rule:MF_01260}.
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; CP000941; ACA11705.1; -; Genomic_DNA.
DR RefSeq; WP_004083854.1; NC_010513.1.
DR AlphaFoldDB; B0U6I9; -.
DR SMR; B0U6I9; -.
DR ESTHER; xylfa-XF1356; BioH.
DR KEGG; xfm:Xfasm12_0709; -.
DR HOGENOM; CLU_020336_12_2_6; -.
DR OMA; LHGWGMN; -.
DR OrthoDB; 1282004at2; -.
DR UniPathway; UPA00078; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009102; P:biotin biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.1820; -; 1.
DR HAMAP; MF_01260; Carboxylester; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR010076; BioH.
DR Pfam; PF12697; Abhydrolase_6; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR TIGRFAMs; TIGR01738; bioH; 1.
PE 3: Inferred from homology;
KW Biotin biosynthesis; Cytoplasm; Hydrolase; Serine esterase.
FT CHAIN 1..255
FT /note="Pimeloyl-[acyl-carrier protein] methyl ester
FT esterase"
FT /id="PRO_1000140011"
FT ACT_SITE 78
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01260"
FT ACT_SITE 203
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01260"
FT ACT_SITE 233
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01260"
FT BINDING 18
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01260"
FT BINDING 78..79
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01260"
FT BINDING 139..143
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01260"
FT BINDING 233
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01260"
SQ SEQUENCE 255 AA; 27592 MW; B438D33CC65C82FF CRC64;
MYIEVTGYGP ALVLIHGWAM HSGVFAPLVE QLRPHHTLYL VDLPGHGYNH TTPTPLALPQ
VVHAIAAATP PAVWLGWSLG GLFALHAAAT LPQVRGLIML AATPCFVRRE DWPHAVEVSI
FTQFAQDLKQ NYTETINRFL ALDTLGSTHA QSELRQLRKI LNARHTPNTA TLQAGLELLA
HTDLRRAVID LTPPSLWIAG QRDRLVPAAS IQAATALAPS GQTELLTITG GGHAPFLSHA
NQMTAALQHF IATLP
