BIOH_VIBVU
ID BIOH_VIBVU Reviewed; 255 AA.
AC Q8DDU4;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 104.
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=VV1_0862;
OS Vibrio vulnificus (strain CMCP6).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=216895;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CMCP6;
RA Rhee J.H., Kim S.Y., Chung S.S., Kim J.J., Moon Y.H., Jeong H., Choy H.E.;
RT "Complete genome sequence of Vibrio vulnificus CMCP6.";
RL Submitted (DEC-2002) 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; AE016795; AAO09365.1; -; Genomic_DNA.
DR RefSeq; WP_011078929.1; NC_004459.3.
DR AlphaFoldDB; Q8DDU4; -.
DR SMR; Q8DDU4; -.
DR ESTHER; vibvu-VV10862; BioH.
DR EnsemblBacteria; AAO09365; AAO09365; VV1_0862.
DR KEGG; vvu:VV1_0862; -.
DR HOGENOM; CLU_020336_12_2_6; -.
DR OMA; LHGWGMN; -.
DR UniPathway; UPA00078; -.
DR Proteomes; UP000002275; Chromosome 1.
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..255
FT /note="Pimeloyl-[acyl-carrier protein] methyl ester
FT esterase"
FT /id="PRO_0000204498"
FT DOMAIN 16..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 255 AA; 28418 MW; F2C27A816B257435 CRC64;
MSTDLHWQTQ GQGPDLVLLH GWGMNGAVWQ QVVERLELHF RLHVVDLPGY GHSAHLHAAS
LEEIAQQLLE HAPKQAIWVG WSLGGLVATH MALHHADYVS KLVTVASSPK FAAEARWRGI
QPQVLSAFTE QLSEDFHTTV ERFMALQAMG SPSARQDVKN LKQAVFSRPQ PNPQSLLAGL
QMLAEVDLRD HLPHLTMPML RLYGRLDGLV PIKVAQDLEK VLPASEQFIF TQSSHAPFIT
EPESFCHQLL SFAGK