BIOH_VIBCH
ID BIOH_VIBCH Reviewed; 255 AA.
AC Q9KNL4;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2005, sequence version 2.
DT 03-AUG-2022, entry version 112.
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=VC_2718;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
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 -!- SEQUENCE CAUTION:
CC Sequence=AAF95858.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE003852; AAF95858.1; ALT_INIT; Genomic_DNA.
DR PIR; G82042; G82042.
DR RefSeq; NP_232345.1; NC_002505.1.
DR AlphaFoldDB; Q9KNL4; -.
DR SMR; Q9KNL4; -.
DR STRING; 243277.VC_2718; -.
DR ESTHER; vibch-VC2718; BioH.
DR DNASU; 2615546; -.
DR EnsemblBacteria; AAF95858; AAF95858; VC_2718.
DR KEGG; vch:VC_2718; -.
DR PATRIC; fig|243277.26.peg.2593; -.
DR eggNOG; COG0596; Bacteria.
DR HOGENOM; CLU_020336_12_2_6; -.
DR OMA; LHGWGMN; -.
DR UniPathway; UPA00078; -.
DR Proteomes; UP000000584; 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; Reference proteome;
KW Serine esterase.
FT CHAIN 1..255
FT /note="Pimeloyl-[acyl-carrier protein] methyl ester
FT esterase"
FT /id="PRO_0000204495"
FT DOMAIN 16..241
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; 28109 MW; 490A66F9BE75340A CRC64;
MTMALYWQVS GQGQDLVLVH GWGMNGAVWQ QTAQALSDHF RVHVVDLPGY GHSAEQHAAS
LEEIAQALLE HAPRNAIWVG WSLGGLVATH MALHHSDYVS KLVTVASSPK FAAQGSWRGI
QPDVLTAFTD QLVADFQLTI ERFMALQAMG SPSARQDVKV LKQAVLSRPM PNPQSLLAGL
TMLAEVDLRD ELQHISVPML RLYGRLDGLV PAKVARDLNH LAPYSEAFMF DQSSHAPFMT
EAEAFCQQLI EFATR
