ID   BIOH_SERMA              Reviewed;         255 AA.
AC   Q8GHL1;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 68.
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};
OS   Serratia marcescens.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Serratia.
OX   NCBI_TaxID=615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION AS AN ESTERASE, ROLE IN BIOTIN
RP   BIOSYNTHESIS, AND SUBCELLULAR LOCATION.
RC   STRAIN=Sr41 / 8000;
RX   PubMed=12527210; DOI=10.1016/s0378111902011502;
RA   Akatsuka H., Kawai E., Imai Y., Sakurai N., Omori K.;
RT   "The Serratia marcescens bioH gene encodes an esterase.";
RL   Gene 302:185-192(2003).
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. Also displays
CC       a weak thioesterase activity. Can form a complex with CoA, and may be
CC       involved in the condensation of CoA and pimelic acid into pimeloyl-CoA,
CC       a precursor in biotin biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01260,
CC       ECO:0000269|PubMed:12527210}.
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       ECO:0000269|PubMed:12527210}.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Carboxylesterase
CC       BioH family. {ECO:0000255|HAMAP-Rule:MF_01260}.
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DR   EMBL; AB089611; BAC53660.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8GHL1; -.
DR   SMR; Q8GHL1; -.
DR   STRING; 273526.SMDB11_3876; -.
DR   ESTHER; serma-bioH; BioH.
DR   UniPathway; UPA00078; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0052689; F:carboxylic ester hydrolase activity; ISS:UniProtKB.
DR   GO; GO:0009102; P:biotin biosynthetic process; IDA:UniProtKB.
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   1: Evidence at protein level;
KW   Biotin biosynthesis; Cytoplasm; Hydrolase; Serine esterase.
FT   CHAIN           1..255
FT                   /note="Pimeloyl-[acyl-carrier protein] methyl ester
FT                   esterase"
FT                   /id="PRO_0000204492"
FT   DOMAIN          16..241
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        81
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01260"
FT   ACT_SITE        206
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01260"
FT   ACT_SITE        234
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01260"
FT   BINDING         22
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01260"
FT   BINDING         81..82
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01260"
FT   BINDING         142..146
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01260"
FT   BINDING         234
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01260"
SQ   SEQUENCE   255 AA;  27859 MW;  572BDEC13EB488F2 CRC64;
     MTALYWQTIG EGERDLVLLH GWGLNAEVWS CIQALTPHFR LHLVDLPGYG RSQGFGALSL
     AQMTEIVLAA APPQAWWLGW SLGGLVASQA ALMQPQRVSG LITVASSPCF AARDEWPGIR
     PDVLSGFQHQ LSLDFQRTVE RFLALQTLGT ESARQDARQL KAVVLNQPTP SVEVLNGGLE
     ILRTADLRAP LAELNLPLLR IYGYLDGLVP RKVAELLDAA WPNSTSQIVA KAAHAPFISH
     PDEFVTMIEA FIAAH