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Pimeloyl-[acyl-carrier protein] methyl ester esterase (EC 3.1.1.85) (Biotin synthesis protein BioH) (Carboxylesterase BioH)

 BIOH_ECOLI              Reviewed;         256 AA.
P13001; Q2M777;
01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
01-JAN-1990, sequence version 1.
05-JUL-2017, entry version 146.
RecName: Full=Pimeloyl-[acyl-carrier protein] methyl ester esterase;
EC=3.1.1.85;
AltName: Full=Biotin synthesis protein BioH;
AltName: Full=Carboxylesterase BioH;
Name=bioH; Synonyms=bioB; OrderedLocusNames=b3412, JW3375;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12;
PubMed=2678009; DOI=10.1093/nar/17.19.8004;
O'Regan M., Gloeckler R., Bernard S., Ledoux C., Ohsawa I.,
Lemoine Y.;
"Nucleotide sequence of the bioH gene of Escherichia coli.";
Nucleic Acids Res. 17:8004-8004(1989).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[4]
FUNCTION IN THE BIOTIN BIOSYNTHESIS, CATALYTIC ACTIVITY, BINDING TO
COA, SUBUNIT, MASS SPECTROMETRY, AND MUTAGENESIS OF SER-82.
STRAIN=K12 / JM101 / ATCC 33876 / DSM 3948 / NCIMB 11926;
PubMed=11904168; DOI=10.1016/S0014-5793(02)02342-6;
Tomczyk N.H., Nettleship J.E., Baxter R.L., Crichton H.J.,
Webster S.P., Campopiano D.J.;
"Purification and characterisation of the BIOH protein from the biotin
biosynthetic pathway.";
FEBS Lett. 513:299-304(2002).
[5]
FUNCTION AS A CARBOXYLESTERASE AND IN THE SIMVASTATIN BIOCONVERSION,
DISRUPTION PHENOTYPE, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=17625941; DOI=10.1016/j.ymben.2007.05.006;
Xie X., Wong W.W., Tang Y.;
"Improving simvastatin bioconversion in Escherichia coli by deletion
of bioH.";
Metab. Eng. 9:379-386(2007).
[6]
SUBSTRATE SPECIFICITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=19307763;
Kwon M.A., Kim H.S., Oh J.Y., Song B.K., Song J.K.;
"Gene cloning, expression, and characterization of a new
carboxylesterase from Serratia sp. SES-01: comparison with Escherichia
coli BioHe enzyme.";
J. Microbiol. Biotechnol. 19:147-154(2009).
[7]
FUNCTION AS A CARBOXYLESTERASE, MUTAGENESIS OF SER-82, AND SUBSTRATE
SPECIFICITY.
PubMed=20693992; DOI=10.1038/nchembio.420;
Lin S., Hanson R.E., Cronan J.E.;
"Biotin synthesis begins by hijacking the fatty acid synthetic
pathway.";
Nat. Chem. Biol. 6:682-688(2010).
[8]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS), FUNCTION AS A CARBOXYLESTERASE,
SUBSTRATE SPECIFICITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
STRAIN=K12 / DH5-alpha;
PubMed=12732651; DOI=10.1074/jbc.M303867200;
Sanishvili R., Yakunin A.F., Laskowski R.A., Skarina T.,
Evdokimova E., Doherty-Kirby A., Lajoie G.A., Thornton J.M.,
Arrowsmith C.H., Savchenko A., Joachimiak A., Edwards A.M.;
"Integrating structure, bioinformatics, and enzymology to discover
function: BioH, a new carboxylesterase from Escherichia coli.";
J. Biol. Chem. 278:26039-26045(2003).
-!- FUNCTION: The physiological role of BioH is to remove the methyl
group introduced by BioC when the pimeloyl moiety is complete. It
allows to synthesize pimeloyl-ACP via the fatty acid synthetic
pathway through the hydrolysis of the ester bonds of pimeloyl-ACP
esters. E.coli employs a methylation and demethylation strategy to
allow elongation of a temporarily disguised malonate moiety to a
pimelate moiety by the fatty acid synthetic enzymes. BioH shows a
preference for short chain fatty acid esters (acyl chain length of
up to 6 carbons) and short chain p-nitrophenyl esters. Also
displays a weak thioesterase activity. Can form a complex with
CoA, and may be involved in the condensation of CoA and pimelic
acid into pimeloyl-CoA, a precursor in biotin biosynthesis.
-!- FUNCTION: Catalyzes the hydrolysis of the methyl ester bond of
dimethylbutyryl-S-methyl mercaptopropionate (DMB-S-MMP) to yield
dimethylbutyryl mercaptopropionic acid (DMBS-MPA) during the
biocatalytic conversion of simvastin acid from monacolin J acid.
Can also use acyl carriers such as dimethylbutyryl-S-ethyl
mercaptopropionate (DMB-S-EMP) and dimethylbutyryl-S-methyl
thioglycolate (DMB-S-MTG) as the thioester substrates.
-!- CATALYTIC ACTIVITY: Pimeloyl-[acyl-carrier protein] methyl ester +
H(2)O = pimeloyl-[acyl-carrier protein] + methanol.
{ECO:0000269|PubMed:11904168}.
-!- ENZYME REGULATION: Strongly inhibited by phenylmethylsulfonyl
fluoride (PMSF).
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=229 uM for DMB-S-MMP (at Ph 7.9 and at room temperature)
{ECO:0000269|PubMed:12732651, ECO:0000269|PubMed:17625941,
ECO:0000269|PubMed:19307763};
KM=0.29 mM for pNP-acetate {ECO:0000269|PubMed:12732651,
ECO:0000269|PubMed:17625941, ECO:0000269|PubMed:19307763};
KM=0.35 mM for pNP-propionate {ECO:0000269|PubMed:12732651,
ECO:0000269|PubMed:17625941, ECO:0000269|PubMed:19307763};
KM=0.33 mM for pNP-butyrate {ECO:0000269|PubMed:12732651,
ECO:0000269|PubMed:17625941, ECO:0000269|PubMed:19307763};
KM=0.25 mM for pNP-caproate {ECO:0000269|PubMed:12732651,
ECO:0000269|PubMed:17625941, ECO:0000269|PubMed:19307763};
KM=0.60 mM for pNP-laurate {ECO:0000269|PubMed:12732651,
ECO:0000269|PubMed:17625941, ECO:0000269|PubMed:19307763};
Note=The highest catalytic efficiency was observed with pNP-
acetate, then with pNP-propionate, pNP-butyrate and pNP-
caproate.;
pH dependence:
Optimum pH is 8.0-8.5. The activity is more than 90% in the pH
range from 7 to 9. {ECO:0000269|PubMed:12732651,
ECO:0000269|PubMed:17625941, ECO:0000269|PubMed:19307763};
Temperature dependence:
Optimum temperature is between 20 and 30 degrees Celsius.
{ECO:0000269|PubMed:12732651, ECO:0000269|PubMed:17625941,
ECO:0000269|PubMed:19307763};
-!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis.
-!- SUBUNIT: Monomer. {ECO:0000269|PubMed:11904168}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
-!- MASS SPECTROMETRY: Mass=28502.0; Mass_error=5.5;
Method=Electrospray; Range=1-256;
Evidence={ECO:0000269|PubMed:11904168};
-!- DISRUPTION PHENOTYPE: Cells display no detectable hydrolysis of
the thioester and no trace of DMB-S-MPA.
{ECO:0000269|PubMed:17625941}.
-!- SIMILARITY: Belongs to the AB hydrolase superfamily.
Carboxylesterase BioH family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X15587; CAA33612.1; -; Genomic_DNA.
EMBL; U18997; AAA58210.1; -; Genomic_DNA.
EMBL; U00096; AAC76437.1; -; Genomic_DNA.
EMBL; AP009048; BAE77879.1; -; Genomic_DNA.
PIR; JQ0081; BVECBH.
RefSeq; NP_417871.1; NC_000913.3.
RefSeq; WP_001060070.1; NZ_LN832404.1.
PDB; 1M33; X-ray; 1.70 A; A=1-256.
PDBsum; 1M33; -.
ProteinModelPortal; P13001; -.
SMR; P13001; -.
BioGrid; 4263494; 14.
DIP; DIP-9223N; -.
IntAct; P13001; 4.
MINT; MINT-1253056; -.
STRING; 316385.ECDH10B_3587; -.
DrugBank; DB03688; 3-Hydroxy-Propanoic Acid.
ESTHER; ecoli-bioh; BioH.
MEROPS; S33.994; -.
PaxDb; P13001; -.
PRIDE; P13001; -.
EnsemblBacteria; AAC76437; AAC76437; b3412.
EnsemblBacteria; BAE77879; BAE77879; BAE77879.
GeneID; 947916; -.
KEGG; ecj:JW3375; -.
KEGG; eco:b3412; -.
PATRIC; fig|1411691.4.peg.3317; -.
EchoBASE; EB0120; -.
EcoGene; EG10122; bioH.
eggNOG; ENOG4105D3C; Bacteria.
eggNOG; COG0596; LUCA.
HOGENOM; HOG000028062; -.
InParanoid; P13001; -.
KO; K02170; -.
PhylomeDB; P13001; -.
BioCyc; EcoCyc:EG10122-MONOMER; -.
BioCyc; MetaCyc:EG10122-MONOMER; -.
BRENDA; 3.1.1.1; 2026.
BRENDA; 3.1.1.85; 2026.
SABIO-RK; P13001; -.
UniPathway; UPA00078; -.
EvolutionaryTrace; P13001; -.
PRO; PR:P13001; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0052689; F:carboxylic ester hydrolase activity; IDA:UniProtKB.
GO; GO:0090499; F:pimelyl-[acyl-carrier protein] methyl ester esterase activity; IDA:EcoCyc.
GO; GO:0009102; P:biotin biosynthetic process; IDA:UniProtKB.
Gene3D; 3.40.50.1820; -; 1.
HAMAP; MF_01260; Carboxylester; 1.
InterPro; IPR029058; AB_hydrolase.
InterPro; IPR000073; AB_hydrolase_1.
InterPro; IPR010076; BioH.
Pfam; PF00561; Abhydrolase_1; 1.
SUPFAM; SSF53474; SSF53474; 1.
TIGRFAMs; TIGR01738; bioH; 1.
1: Evidence at protein level;
3D-structure; Biotin biosynthesis; Complete proteome; Cytoplasm;
Hydrolase; Reference proteome; Serine esterase.
CHAIN 1 256 Pimeloyl-[acyl-carrier protein] methyl
ester esterase.
/FTId=PRO_0000204473.
DOMAIN 15 242 AB hydrolase-1. {ECO:0000255}.
REGION 82 83 Substrate binding.
REGION 143 147 Substrate binding.
ACT_SITE 82 82 Nucleophile.
ACT_SITE 207 207 {ECO:0000250}.
ACT_SITE 235 235
BINDING 22 22 Substrate; via amide nitrogen and
carbonyl oxygen.
BINDING 235 235 Substrate.
MUTAGEN 82 82 S->A: No effect on CoA-binding. Loss of
Carboxylesterase activity.
{ECO:0000269|PubMed:11904168,
ECO:0000269|PubMed:20693992}.
STRAND 6 9 {ECO:0000244|PDB:1M33}.
STRAND 13 19 {ECO:0000244|PDB:1M33}.
HELIX 26 31 {ECO:0000244|PDB:1M33}.
HELIX 33 37 {ECO:0000244|PDB:1M33}.
STRAND 40 45 {ECO:0000244|PDB:1M33}.
HELIX 61 69 {ECO:0000244|PDB:1M33}.
STRAND 74 81 {ECO:0000244|PDB:1M33}.
HELIX 83 94 {ECO:0000244|PDB:1M33}.
HELIX 96 98 {ECO:0000244|PDB:1M33}.
STRAND 99 106 {ECO:0000244|PDB:1M33}.
HELIX 122 145 {ECO:0000244|PDB:1M33}.
HELIX 154 166 {ECO:0000244|PDB:1M33}.
HELIX 173 185 {ECO:0000244|PDB:1M33}.
HELIX 191 194 {ECO:0000244|PDB:1M33}.
STRAND 199 204 {ECO:0000244|PDB:1M33}.
STRAND 208 210 {ECO:0000244|PDB:1M33}.
HELIX 214 221 {ECO:0000244|PDB:1M33}.
STRAND 226 230 {ECO:0000244|PDB:1M33}.
HELIX 237 240 {ECO:0000244|PDB:1M33}.
HELIX 242 253 {ECO:0000244|PDB:1M33}.
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


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