BIOH_AROAE
ID BIOH_AROAE Reviewed; 250 AA.
AC Q5NZF6;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 95.
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=AZOSEA34330;
GN ORFNames=ebA6017;
OS Aromatoleum aromaticum (strain EbN1) (Azoarcus sp. (strain EbN1)).
OC Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales;
OC Rhodocyclaceae; Aromatoleum.
OX NCBI_TaxID=76114;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EbN1;
RX PubMed=15551059; DOI=10.1007/s00203-004-0742-9;
RA Rabus R., Kube M., Heider J., Beck A., Heitmann K., Widdel F.,
RA Reinhardt R.;
RT "The genome sequence of an anaerobic aromatic-degrading denitrifying
RT bacterium, strain EbN1.";
RL Arch. Microbiol. 183:27-36(2005).
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; CR555306; CAI09558.1; -; Genomic_DNA.
DR RefSeq; WP_011239218.1; NC_006513.1.
DR AlphaFoldDB; Q5NZF6; -.
DR SMR; Q5NZF6; -.
DR STRING; 76114.ebA6017; -.
DR ESTHER; aroae-q5nzf6; BioH.
DR EnsemblBacteria; CAI09558; CAI09558; ebA6017.
DR KEGG; eba:ebA6017; -.
DR eggNOG; COG2267; Bacteria.
DR HOGENOM; CLU_020336_12_2_4; -.
DR OMA; LHGWGMN; -.
DR OrthoDB; 1282004at2; -.
DR UniPathway; UPA00078; -.
DR Proteomes; UP000006552; Chromosome.
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; PF12697; Abhydrolase_6; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 3: Inferred from homology;
KW Biotin biosynthesis; Cytoplasm; Hydrolase; Reference proteome;
KW Serine esterase.
FT CHAIN 1..250
FT /note="Pimeloyl-[acyl-carrier protein] methyl ester
FT esterase"
FT /id="PRO_0000204470"
FT ACT_SITE 71
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01260"
FT ACT_SITE 202
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01260"
FT ACT_SITE 230
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01260"
FT BINDING 12
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01260"
FT BINDING 71..72
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01260"
FT BINDING 138..142
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01260"
FT BINDING 230
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01260"
SQ SEQUENCE 250 AA; 26598 MW; B75B82A981F8ED27 CRC64;
MNRPDLVLLH GWGLGPQVWS ALTPYLPAGL RVRTPALPGH GGTPARGPTL EAWSDALLPE
LPDDAVVCGW SLGGLVALDL ARRHPHKVAR LVLIGTSPCF VTRPENAAAP WPYGLAASTV
TGFIDDFAHD PAATLRRFVA LQALGDARRR TVSNALNAAL ANLEQCRPAA LGAGLELLAD
TDWRAALDDV RQPVQLIHGA GDALMPLAAA EWLATRLPDA RLARFDDCGH APFLSHPEDC
AVLIEDVVRG
