ID   BIOH_STRM5              Reviewed;         259 AA.
AC   B4SM83;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 77.
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}; OrderedLocusNames=Smal_3829;
OS   Stenotrophomonas maltophilia (strain R551-3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas; Stenotrophomonas maltophilia group.
OX   NCBI_TaxID=391008;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R551-3;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Taghavi S.,
RA   Monchy S., Newman L., Vangronsveld J., van der Lelie D., Richardson P.;
RT   "Complete sequence of Stenotrophomonas maltophilia R551-3.";
RL   Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; CP001111; ACF53528.1; -; Genomic_DNA.
DR   RefSeq; WP_012512400.1; NC_011071.1.
DR   AlphaFoldDB; B4SM83; -.
DR   SMR; B4SM83; -.
DR   STRING; 391008.Smal_3829; -.
DR   ESTHER; strm5-bioh; BioH.
DR   EnsemblBacteria; ACF53528; ACF53528; Smal_3829.
DR   KEGG; smt:Smal_3829; -.
DR   eggNOG; COG2267; Bacteria.
DR   HOGENOM; CLU_020336_12_2_6; -.
DR   OMA; LHGWGMN; -.
DR   OrthoDB; 1282004at2; -.
DR   BioCyc; SMAL391008:SMAL_RS19445-MON; -.
DR   UniPathway; UPA00078; -.
DR   Proteomes; UP000001867; Chromosome.
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..259
FT                   /note="Pimeloyl-[acyl-carrier protein] methyl ester
FT                   esterase"
FT                   /id="PRO_1000140006"
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        231
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         231
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01260"
SQ   SEQUENCE   259 AA;  27415 MW;  9DA185290C9BF372 CRC64;
     MHIEVTGRGP DLVLIHGWAL QGGVFAPLVQ RLADQFTLHL VDLPGHGHSR DDTTPLRLPF
     VVNAIAAATP PAVWCGWSLG GLFALHAAAT LPKVRGLAMI AATPRFVRGE DWPHAVEPAV
     FEQFGRELAS DFGGTLERFL ALDVMGSAHA REELRTLRQR LVERGAPTER ALLEGLRLLE
     STDLRGALPT LGKPSLWIAG QRDRLVSPAA MQAAAALALG GQALTIAHGG HAPFLGHADE
     VAAALQHFVA GLSPADGGQ