BIOH_ECOLI
ID BIOH_ECOLI Reviewed; 256 AA.
AC P13001; Q2M777;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 172.
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; Synonyms=bioB; OrderedLocusNames=b3412, JW3375;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=2678009; DOI=10.1093/nar/17.19.8004;
RA O'Regan M., Gloeckler R., Bernard S., Ledoux C., Ohsawa I., Lemoine Y.;
RT "Nucleotide sequence of the bioH gene of Escherichia coli.";
RL Nucleic Acids Res. 17:8004-8004(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP FUNCTION IN THE BIOTIN BIOSYNTHESIS, CATALYTIC ACTIVITY, BINDING TO COA,
RP SUBUNIT, MASS SPECTROMETRY, AND MUTAGENESIS OF SER-82.
RC STRAIN=K12 / JM101 / ATCC 33876 / DSM 3948 / NCIMB 11926;
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).
RN [5]
RP FUNCTION AS A CARBOXYLESTERASE AND IN THE SIMVASTATIN BIOCONVERSION,
RP DISRUPTION PHENOTYPE, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=17625941; DOI=10.1016/j.ymben.2007.05.006;
RA Xie X., Wong W.W., Tang Y.;
RT "Improving simvastatin bioconversion in Escherichia coli by deletion of
RT bioH.";
RL Metab. Eng. 9:379-386(2007).
RN [6]
RP SUBSTRATE SPECIFICITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=19307763; DOI=10.4014/jmb.0804.287;
RA Kwon M.A., Kim H.S., Oh J.Y., Song B.K., Song J.K.;
RT "Gene cloning, expression, and characterization of a new carboxylesterase
RT from Serratia sp. SES-01: comparison with Escherichia coli BioHe enzyme.";
RL J. Microbiol. Biotechnol. 19:147-154(2009).
RN [7]
RP FUNCTION AS A CARBOXYLESTERASE, MUTAGENESIS OF SER-82, AND SUBSTRATE
RP SPECIFICITY.
RX PubMed=20693992; DOI=10.1038/nchembio.420;
RA Lin S., Hanson R.E., Cronan J.E.;
RT "Biotin synthesis begins by hijacking the fatty acid synthetic pathway.";
RL Nat. Chem. Biol. 6:682-688(2010).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS), FUNCTION AS A CARBOXYLESTERASE,
RP SUBSTRATE SPECIFICITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=K12 / DH5-alpha;
RX PubMed=12732651; DOI=10.1074/jbc.m303867200;
RA Sanishvili R., Yakunin A.F., Laskowski R.A., Skarina T., Evdokimova E.,
RA Doherty-Kirby A., Lajoie G.A., Thornton J.M., Arrowsmith C.H.,
RA Savchenko A., Joachimiak A., Edwards A.M.;
RT "Integrating structure, bioinformatics, and enzymology to discover
RT function: BioH, a new carboxylesterase from Escherichia coli.";
RL J. Biol. Chem. 278:26039-26045(2003).
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. E.coli
CC employs a methylation and demethylation strategy to allow elongation of
CC a temporarily disguised malonate moiety to a pimelate moiety by the
CC fatty acid synthetic enzymes. BioH shows a preference for short chain
CC fatty acid esters (acyl chain length of up to 6 carbons) and short
CC chain p-nitrophenyl esters. Also displays a weak thioesterase activity.
CC Can form a complex with CoA, and may be involved in the condensation of
CC CoA and pimelic acid into pimeloyl-CoA, a precursor in biotin
CC biosynthesis.
CC -!- FUNCTION: Catalyzes the hydrolysis of the methyl ester bond of
CC dimethylbutyryl-S-methyl mercaptopropionate (DMB-S-MMP) to yield
CC dimethylbutyryl mercaptopropionic acid (DMBS-MPA) during the
CC biocatalytic conversion of simvastin acid from monacolin J acid. Can
CC also use acyl carriers such as dimethylbutyryl-S-ethyl
CC mercaptopropionate (DMB-S-EMP) and dimethylbutyryl-S-methyl
CC thioglycolate (DMB-S-MTG) as the thioester substrates.
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 Evidence={ECO:0000269|PubMed:11904168};
CC -!- ACTIVITY REGULATION: Strongly inhibited by phenylmethylsulfonyl
CC fluoride (PMSF).
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=229 uM for DMB-S-MMP (at Ph 7.9 and at room temperature)
CC {ECO:0000269|PubMed:12732651, ECO:0000269|PubMed:17625941,
CC ECO:0000269|PubMed:19307763};
CC KM=0.29 mM for pNP-acetate {ECO:0000269|PubMed:12732651,
CC ECO:0000269|PubMed:17625941, ECO:0000269|PubMed:19307763};
CC KM=0.35 mM for pNP-propionate {ECO:0000269|PubMed:12732651,
CC ECO:0000269|PubMed:17625941, ECO:0000269|PubMed:19307763};
CC KM=0.33 mM for pNP-butyrate {ECO:0000269|PubMed:12732651,
CC ECO:0000269|PubMed:17625941, ECO:0000269|PubMed:19307763};
CC KM=0.25 mM for pNP-caproate {ECO:0000269|PubMed:12732651,
CC ECO:0000269|PubMed:17625941, ECO:0000269|PubMed:19307763};
CC KM=0.60 mM for pNP-laurate {ECO:0000269|PubMed:12732651,
CC ECO:0000269|PubMed:17625941, ECO:0000269|PubMed:19307763};
CC Note=The highest catalytic efficiency was observed with pNP-acetate,
CC then with pNP-propionate, pNP-butyrate and pNP-caproate.;
CC pH dependence:
CC Optimum pH is 8.0-8.5. The activity is more than 90% in the pH range
CC from 7 to 9. {ECO:0000269|PubMed:12732651,
CC ECO:0000269|PubMed:17625941, ECO:0000269|PubMed:19307763};
CC Temperature dependence:
CC Optimum temperature is between 20 and 30 degrees Celsius.
CC {ECO:0000269|PubMed:12732651, ECO:0000269|PubMed:17625941,
CC ECO:0000269|PubMed:19307763};
CC -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:11904168}.
CC -!- INTERACTION:
CC P13001; P0A6A8: acpP; NbExp=3; IntAct=EBI-1132260, EBI-542566;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- MASS SPECTROMETRY: Mass=28502.0; Mass_error=5.5; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:11904168};
CC -!- DISRUPTION PHENOTYPE: Cells display no detectable hydrolysis of the
CC thioester and no trace of DMB-S-MPA. {ECO:0000269|PubMed:17625941}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Carboxylesterase
CC BioH family. {ECO:0000305}.
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DR EMBL; X15587; CAA33612.1; -; Genomic_DNA.
DR EMBL; U18997; AAA58210.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76437.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77879.1; -; Genomic_DNA.
DR PIR; JQ0081; BVECBH.
DR RefSeq; NP_417871.1; NC_000913.3.
DR RefSeq; WP_001060070.1; NZ_SSZK01000008.1.
DR PDB; 1M33; X-ray; 1.70 A; A=1-256.
DR PDBsum; 1M33; -.
DR AlphaFoldDB; P13001; -.
DR SMR; P13001; -.
DR BioGRID; 4263494; 14.
DR DIP; DIP-9223N; -.
DR IntAct; P13001; 5.
DR STRING; 511145.b3412; -.
DR DrugBank; DB03688; Hydracrylic acid.
DR ESTHER; ecoli-bioh; BioH.
DR MEROPS; S33.994; -.
DR jPOST; P13001; -.
DR PaxDb; P13001; -.
DR PRIDE; P13001; -.
DR EnsemblBacteria; AAC76437; AAC76437; b3412.
DR EnsemblBacteria; BAE77879; BAE77879; BAE77879.
DR GeneID; 947916; -.
DR KEGG; ecj:JW3375; -.
DR KEGG; eco:b3412; -.
DR PATRIC; fig|1411691.4.peg.3317; -.
DR EchoBASE; EB0120; -.
DR eggNOG; COG0596; Bacteria.
DR HOGENOM; CLU_020336_12_2_6; -.
DR InParanoid; P13001; -.
DR OMA; LHGWGMN; -.
DR PhylomeDB; P13001; -.
DR BioCyc; EcoCyc:EG10122-MON; -.
DR BioCyc; MetaCyc:EG10122-MON; -.
DR BRENDA; 3.1.1.1; 2026.
DR BRENDA; 3.1.1.85; 2026.
DR SABIO-RK; P13001; -.
DR UniPathway; UPA00078; -.
DR EvolutionaryTrace; P13001; -.
DR PRO; PR:P13001; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IDA:UniProtKB.
DR GO; GO:0090499; F:pimelyl-[acyl-carrier protein] methyl ester esterase activity; IDA:EcoCyc.
DR GO; GO:0009102; P:biotin biosynthetic process; IDA:UniProtKB.
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 3D-structure; Biotin biosynthesis; Cytoplasm; Hydrolase;
KW Reference proteome; Serine esterase.
FT CHAIN 1..256
FT /note="Pimeloyl-[acyl-carrier protein] methyl ester
FT esterase"
FT /id="PRO_0000204473"
FT DOMAIN 15..242
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255"
FT ACT_SITE 82
FT /note="Nucleophile"
FT ACT_SITE 207
FT /evidence="ECO:0000250"
FT ACT_SITE 235
FT BINDING 22
FT /ligand="substrate"
FT BINDING 82..83
FT /ligand="substrate"
FT BINDING 143..147
FT /ligand="substrate"
FT BINDING 235
FT /ligand="substrate"
FT MUTAGEN 82
FT /note="S->A: No effect on CoA-binding. Loss of
FT Carboxylesterase activity."
FT /evidence="ECO:0000269|PubMed:11904168,
FT ECO:0000269|PubMed:20693992"
FT STRAND 6..9
FT /evidence="ECO:0007829|PDB:1M33"
FT STRAND 13..19
FT /evidence="ECO:0007829|PDB:1M33"
FT HELIX 26..31
FT /evidence="ECO:0007829|PDB:1M33"
FT HELIX 33..37
FT /evidence="ECO:0007829|PDB:1M33"
FT STRAND 40..45
FT /evidence="ECO:0007829|PDB:1M33"
FT HELIX 61..69
FT /evidence="ECO:0007829|PDB:1M33"
FT STRAND 74..81
FT /evidence="ECO:0007829|PDB:1M33"
FT HELIX 83..94
FT /evidence="ECO:0007829|PDB:1M33"
FT HELIX 96..98
FT /evidence="ECO:0007829|PDB:1M33"
FT STRAND 99..106
FT /evidence="ECO:0007829|PDB:1M33"
FT HELIX 122..145
FT /evidence="ECO:0007829|PDB:1M33"
FT HELIX 154..166
FT /evidence="ECO:0007829|PDB:1M33"
FT HELIX 173..185
FT /evidence="ECO:0007829|PDB:1M33"
FT HELIX 191..194
FT /evidence="ECO:0007829|PDB:1M33"
FT STRAND 199..204
FT /evidence="ECO:0007829|PDB:1M33"
FT STRAND 208..210
FT /evidence="ECO:0007829|PDB:1M33"
FT HELIX 214..221
FT /evidence="ECO:0007829|PDB:1M33"
FT STRAND 226..230
FT /evidence="ECO:0007829|PDB:1M33"
FT HELIX 237..240
FT /evidence="ECO:0007829|PDB:1M33"
FT HELIX 242..253
FT /evidence="ECO:0007829|PDB:1M33"
SQ SEQUENCE 256 AA; 28505 MW; 931226F241BBCBF3 CRC64;
MNNIWWQTKG QGNVHLVLLH GWGLNAEVWR CIDEELSSHF TLHLVDLPGF GRSRGFGALS
LADMAEAVLQ QAPDKAIWLG WSLGGLVASQ IALTHPERVQ ALVTVASSPC FSARDEWPGI
KPDVLAGFQQ QLSDDFQRTV ERFLALQTMG TETARQDARA LKKTVLALPM PEVDVLNGGL
EILKTVDLRQ PLQNVSMPFL RLYGYLDGLV PRKVVPMLDK LWPHSESYIF AKAAHAPFIS
HPAEFCHLLV ALKQRV
