ID   BIOH_ECODH              Reviewed;         256 AA.
AC   B1X758;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   03-AUG-2022, entry version 72.
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=ECDH10B_3587;
OS   Escherichia coli (strain K12 / DH10B).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=316385;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / DH10B;
RX   PubMed=18245285; DOI=10.1128/jb.01695-07;
RA   Durfee T., Nelson R., Baldwin S., Plunkett G. III, Burland V., Mau B.,
RA   Petrosino J.F., Qin X., Muzny D.M., Ayele M., Gibbs R.A., Csorgo B.,
RA   Posfai G., Weinstock G.M., Blattner F.R.;
RT   "The complete genome sequence of Escherichia coli DH10B: insights into the
RT   biology of a laboratory workhorse.";
RL   J. Bacteriol. 190:2597-2606(2008).
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; CP000948; ACB04470.1; -; Genomic_DNA.
DR   RefSeq; WP_001060070.1; NC_010473.1.
DR   AlphaFoldDB; B1X758; -.
DR   SMR; B1X758; -.
DR   ESTHER; ecoli-bioh; BioH.
DR   MEROPS; S33.994; -.
DR   KEGG; ecd:ECDH10B_3587; -.
DR   HOGENOM; CLU_020336_12_2_6; -.
DR   OMA; LHGWGMN; -.
DR   BioCyc; ECOL316385:ECDH10B_RS18235-MON; -.
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; PF00561; Abhydrolase_1; 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..256
FT                   /note="Pimeloyl-[acyl-carrier protein] methyl ester
FT                   esterase"
FT                   /id="PRO_1000139990"
FT   DOMAIN          15..242
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        82
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01260"
FT   ACT_SITE        207
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01260"
FT   ACT_SITE        235
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01260"
FT   BINDING         22
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01260"
FT   BINDING         82..83
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01260"
FT   BINDING         143..147
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01260"
FT   BINDING         235
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01260"
SQ   SEQUENCE   256 AA;  28505 MW;  931226F241BBCBF3 CRC64;
     MNNIWWQTKG QGNVHLVLLH GWGLNAEVWR CIDEELSSHF TLHLVDLPGF GRSRGFGALS
     LADMAEAVLQ QAPDKAIWLG WSLGGLVASQ IALTHPERVQ ALVTVASSPC FSARDEWPGI
     KPDVLAGFQQ QLSDDFQRTV ERFLALQTMG TETARQDARA LKKTVLALPM PEVDVLNGGL
     EILKTVDLRQ PLQNVSMPFL RLYGYLDGLV PRKVVPMLDK LWPHSESYIF AKAAHAPFIS
     HPAEFCHLLV ALKQRV