BIOH_SHIFL
ID BIOH_SHIFL Reviewed; 262 AA.
AC Q83PW0; Q7UAT4;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 4.
DT 03-AUG-2022, entry version 121.
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};
GN OrderedLocusNames=SF3435, S4329;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(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.
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; AE005674; AAN44896.2; -; Genomic_DNA.
DR EMBL; AE014073; AAP19285.1; -; Genomic_DNA.
DR RefSeq; NP_709189.2; NC_004337.2.
DR RefSeq; WP_001060072.1; NZ_WPGW01000066.1.
DR PDB; 4ETW; X-ray; 2.05 A; A/C=1-257.
DR PDBsum; 4ETW; -.
DR AlphaFoldDB; Q83PW0; -.
DR SMR; Q83PW0; -.
DR STRING; 198214.SF3435; -.
DR ESTHER; shifl-BIOH; BioH.
DR EnsemblBacteria; AAN44896; AAN44896; SF3435.
DR EnsemblBacteria; AAP19285; AAP19285; S4329.
DR GeneID; 1026527; -.
DR KEGG; sfl:SF3435; -.
DR KEGG; sfx:S4329; -.
DR PATRIC; fig|198214.7.peg.4052; -.
DR HOGENOM; CLU_020336_12_2_6; -.
DR OMA; LHGWGMN; -.
DR OrthoDB; 1282004at2; -.
DR BRENDA; 3.1.1.85; 5712.
DR UniPathway; UPA00078; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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; 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..262
FT /note="Pimeloyl-[acyl-carrier protein] methyl ester
FT esterase"
FT /id="PRO_0000204494"
FT DOMAIN 15..242
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255"
FT ACT_SITE 82
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01260"
FT ACT_SITE 207
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01260"
FT ACT_SITE 235
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01260"
FT BINDING 22
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01260"
FT BINDING 82..83
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01260"
FT BINDING 143..147
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01260"
FT BINDING 235
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01260"
FT STRAND 6..9
FT /evidence="ECO:0007829|PDB:4ETW"
FT STRAND 13..19
FT /evidence="ECO:0007829|PDB:4ETW"
FT HELIX 26..31
FT /evidence="ECO:0007829|PDB:4ETW"
FT HELIX 33..37
FT /evidence="ECO:0007829|PDB:4ETW"
FT STRAND 40..45
FT /evidence="ECO:0007829|PDB:4ETW"
FT HELIX 61..69
FT /evidence="ECO:0007829|PDB:4ETW"
FT STRAND 74..81
FT /evidence="ECO:0007829|PDB:4ETW"
FT HELIX 83..94
FT /evidence="ECO:0007829|PDB:4ETW"
FT HELIX 96..98
FT /evidence="ECO:0007829|PDB:4ETW"
FT STRAND 99..106
FT /evidence="ECO:0007829|PDB:4ETW"
FT HELIX 122..133
FT /evidence="ECO:0007829|PDB:4ETW"
FT HELIX 136..148
FT /evidence="ECO:0007829|PDB:4ETW"
FT HELIX 154..167
FT /evidence="ECO:0007829|PDB:4ETW"
FT HELIX 173..185
FT /evidence="ECO:0007829|PDB:4ETW"
FT HELIX 191..194
FT /evidence="ECO:0007829|PDB:4ETW"
FT STRAND 199..204
FT /evidence="ECO:0007829|PDB:4ETW"
FT STRAND 208..210
FT /evidence="ECO:0007829|PDB:4ETW"
FT HELIX 214..221
FT /evidence="ECO:0007829|PDB:4ETW"
FT STRAND 225..230
FT /evidence="ECO:0007829|PDB:4ETW"
FT HELIX 237..240
FT /evidence="ECO:0007829|PDB:4ETW"
FT HELIX 242..256
FT /evidence="ECO:0007829|PDB:4ETW"
SQ SEQUENCE 262 AA; 29148 MW; 468108F08E5C0312 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
HPVEFCHLLV ALKQRVLVVS ES
