BIOH_NEIMH
ID BIOH_NEIMH Reviewed; 258 AA.
AC E6MWF8;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 41.
DE RecName: Full=Pimeloyl-[acyl-carrier protein] methyl ester esterase;
DE EC=3.1.1.85;
DE AltName: Full=Biotin synthesis protein BioH;
DE AltName: Full=Carboxylesterase BioH;
GN Name=bioH; OrderedLocusNames=NMBH4476_0264; ORFNames=NMH_0998;
OS Neisseria meningitidis serogroup B / serotype 15 (strain H44/76).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=909420;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H44/76;
RX PubMed=21378179; DOI=10.1128/jb.01331-10;
RA Piet J.R., Huis In 't Veld R.A., van Schaik B.D., van Kampen A.H., Baas F.,
RA van de Beek D., Pannekoek Y., van der Ende A.;
RT "Genome sequence of Neisseria meningitidis serogroup B strain H44/76.";
RL J. Bacteriol. 193:2371-2372(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H44/76;
RX PubMed=21368196; DOI=10.1073/pnas.1019751108;
RA Budroni S., Siena E., Hotopp J.C., Seib K.L., Serruto D., Nofroni C.,
RA Comanducci M., Riley D.R., Daugherty S.C., Angiuoli S.V., Covacci A.,
RA Pizza M., Rappuoli R., Moxon E.R., Tettelin H., Medini D.;
RT "Neisseria meningitidis is structured in clades associated with restriction
RT modification systems that modulate homologous recombination.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:4494-4499(2011).
RN [3]
RP ROLE IN BIOTIN BIOSYNTHESIS, BINDING TO COA, AND SUBUNIT.
RC STRAIN=H44/76;
RX PubMed=11904168; DOI=10.1016/s0014-5793(02)02342-6;
RA Tomczyk N.H., Nettleship J.E., Baxter R.L., Crichton H.J., Webster S.P.,
RA Campopiano D.J.;
RT "Purification and characterisation of the BIOH protein from the biotin
RT biosynthetic pathway.";
RL FEBS Lett. 513:299-304(2002).
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 (By
CC similarity). Can form a complex with CoA, and may be involved in the
CC condensation of CoA and pimelic acid into pimeloyl-CoA, a precursor in
CC biotin biosynthesis. {ECO:0000250, ECO:0000269|PubMed:11904168}.
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;
CC -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:11904168}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Carboxylesterase
CC BioH family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ADY94928.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=EFV64152.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AEQZ01000016; EFV64152.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002420; ADY94928.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; E6MWF8; -.
DR SMR; E6MWF8; -.
DR EnsemblBacteria; EFV64152; EFV64152; NMH_0998.
DR KEGG; nmh:NMBH4476_0264; -.
DR PATRIC; fig|909420.3.peg.336; -.
DR HOGENOM; CLU_020336_12_2_4; -.
DR UniPathway; UPA00078; -.
DR Proteomes; UP000032707; Unassembled WGS sequence.
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 1: Evidence at protein level;
KW Biotin biosynthesis; Cytoplasm; Hydrolase; Serine esterase.
FT CHAIN 1..258
FT /note="Pimeloyl-[acyl-carrier protein] methyl ester
FT esterase"
FT /id="PRO_0000411117"
FT DOMAIN 17..241
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255"
FT ACT_SITE 83
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 207
FT /evidence="ECO:0000250"
FT ACT_SITE 235
FT /evidence="ECO:0000250"
FT BINDING 23
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 83..84
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 145..149
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 235
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 258 AA; 28208 MW; E276CAF32714D04E CRC64;
MRRQRERKSM PDAVKKVYLI HGWGANRHMF DDLMPRLPAT WPVSAVDLPG HGDAPFVRPF
DIAAAADGIA AQIDAPADIL GWSLGGLVAL YLAARHPDKV RSLCLTASFA RLTADEDYPE
GLAAPALGKM VGAFRSDYAK HIKQFLQLQL LHTPDADGII GRILPDLARC GTPQALQEAL
DAAERADARH LLDKIDVPVL LVFGGKDAIT PPRMGEYLHR RLKGSRLVVM EKAAHAPFLS
HAEAFAALYR DFVEGGLR
