BIOH_SHESR
ID BIOH_SHESR Reviewed; 264 AA.
AC Q0HPU6;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 82.
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=Shewmr7_3882;
OS Shewanella sp. (strain MR-7).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=60481;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MR-7;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Nealson K.,
RA Konstantinidis K., Klappenbach J., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome 1 of Shewanella sp. MR-7.";
RL Submitted (AUG-2006) 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; CP000444; ABI44859.1; -; Genomic_DNA.
DR RefSeq; WP_011627598.1; NC_008322.1.
DR AlphaFoldDB; Q0HPU6; -.
DR SMR; Q0HPU6; -.
DR ESTHER; sheon-BIOH; BioH.
DR EnsemblBacteria; ABI44859; ABI44859; Shewmr7_3882.
DR KEGG; shm:Shewmr7_3882; -.
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; 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..264
FT /note="Pimeloyl-[acyl-carrier protein] methyl ester
FT esterase"
FT /id="PRO_1000067275"
FT DOMAIN 23..244
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255"
FT ACT_SITE 87
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01260"
FT ACT_SITE 214
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01260"
FT ACT_SITE 241
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01260"
FT BINDING 29
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01260"
FT BINDING 87..88
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01260"
FT BINDING 150..154
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01260"
FT BINDING 241
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01260"
SQ SEQUENCE 264 AA; 29128 MW; 324E31F6DEE82106 CRC64;
MNATTPAHRP QLHIDTRGQG PDLVMLHGWG VNSAVFTPLH EQLSEYRVHY VDLPGFGLSQ
PIAGDLSTWV DALIHALPAN AIWAGWSLGG LVATQAAIRY PSHIQGLITI ASSPCFMARE
EEAWPGIPPQ VLSMFGEQLG QNLPKTIERF LAIQAMGSET AKDDIKQLRD LVLARPLPDA
AALTQGLDML NQIDLRPQLS AIQQPWLRIW GRLDGLVPKR VQPQMPTANH ITDVMLAKAS
HAPFVSHMEE FLQAITPWLA QFKD
