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   27-MAR-2024, entry version 179.
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; Pseudomonadota; 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=0.6 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; 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; 511145-b3412; -.
DR   EnsemblBacteria; AAC76437; AAC76437; b3412.
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; PFISHPQ; -.
DR   OrthoDB; 9780744at2; -.
DR   PhylomeDB; P13001; -.
DR   BioCyc; EcoCyc:EG10122-MONOMER; -.
DR   BioCyc; MetaCyc:EG10122-MONOMER; -.
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; alpha/beta hydrolase; 1.
DR   HAMAP; MF_01260; Carboxylester; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000073; AB_hydrolase_1.
DR   InterPro; IPR010076; BioH.
DR   NCBIfam; TIGR01738; bioH; 1.
DR   PANTHER; PTHR43194; HYDROLASE ALPHA/BETA FOLD FAMILY; 1.
DR   PANTHER; PTHR43194:SF5; PIMELOYL-[ACYL-CARRIER PROTEIN] METHYL ESTER ESTERASE; 1.
DR   Pfam; PF00561; Abhydrolase_1; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 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
//