BIOH_KLEP7
ID BIOH_KLEP7 Reviewed; 257 AA.
AC A6TF35;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 83.
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=KPN78578_37450; ORFNames=KPN_03782;
OS Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=272620;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700721 / MGH 78578;
RG The Klebsiella pneumonia Genome Sequencing Project;
RA McClelland M., Sanderson E.K., Spieth J., Clifton W.S., Latreille P.,
RA Sabo A., Pepin K., Bhonagiri V., Porwollik S., Ali J., Wilson R.K.;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000647; ABR79169.1; -; Genomic_DNA.
DR RefSeq; WP_004174021.1; NC_009648.1.
DR PDB; 6K5E; X-ray; 2.26 A; A/B/C/D/E/F=1-257.
DR PDBsum; 6K5E; -.
DR AlphaFoldDB; A6TF35; -.
DR SMR; A6TF35; -.
DR STRING; 272620.KPN_03782; -.
DR ESTHER; klep3-bioh; BioH.
DR jPOST; A6TF35; -.
DR EnsemblBacteria; ABR79169; ABR79169; KPN_03782.
DR KEGG; kpn:KPN_03782; -.
DR HOGENOM; CLU_020336_12_2_6; -.
DR OMA; LHGWGMN; -.
DR UniPathway; UPA00078; -.
DR Proteomes; UP000000265; 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..257
FT /note="Pimeloyl-[acyl-carrier protein] methyl ester
FT esterase"
FT /id="PRO_1000067270"
FT DOMAIN 15..241
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:6K5E"
FT STRAND 13..19
FT /evidence="ECO:0007829|PDB:6K5E"
FT HELIX 26..29
FT /evidence="ECO:0007829|PDB:6K5E"
FT TURN 30..32
FT /evidence="ECO:0007829|PDB:6K5E"
FT HELIX 33..36
FT /evidence="ECO:0007829|PDB:6K5E"
FT TURN 37..39
FT /evidence="ECO:0007829|PDB:6K5E"
FT STRAND 40..45
FT /evidence="ECO:0007829|PDB:6K5E"
FT HELIX 51..53
FT /evidence="ECO:0007829|PDB:6K5E"
FT HELIX 61..69
FT /evidence="ECO:0007829|PDB:6K5E"
FT STRAND 74..81
FT /evidence="ECO:0007829|PDB:6K5E"
FT HELIX 83..94
FT /evidence="ECO:0007829|PDB:6K5E"
FT HELIX 96..98
FT /evidence="ECO:0007829|PDB:6K5E"
FT STRAND 99..106
FT /evidence="ECO:0007829|PDB:6K5E"
FT HELIX 122..134
FT /evidence="ECO:0007829|PDB:6K5E"
FT HELIX 136..145
FT /evidence="ECO:0007829|PDB:6K5E"
FT HELIX 154..166
FT /evidence="ECO:0007829|PDB:6K5E"
FT HELIX 173..185
FT /evidence="ECO:0007829|PDB:6K5E"
FT TURN 189..194
FT /evidence="ECO:0007829|PDB:6K5E"
FT STRAND 199..204
FT /evidence="ECO:0007829|PDB:6K5E"
FT STRAND 208..210
FT /evidence="ECO:0007829|PDB:6K5E"
FT HELIX 215..218
FT /evidence="ECO:0007829|PDB:6K5E"
FT STRAND 226..230
FT /evidence="ECO:0007829|PDB:6K5E"
FT HELIX 237..240
FT /evidence="ECO:0007829|PDB:6K5E"
FT HELIX 242..256
FT /evidence="ECO:0007829|PDB:6K5E"
SQ SEQUENCE 257 AA; 28264 MW; 6FCB6561A40EC5D5 CRC64;
MNDIWWQTIG EGDCHLVLLH GWGLNAQVWD CITPQLASHF TLHLVDLPGY GRSGGFGAMS
LEAMAQRVLE QAPPQAVWLG WSLGGLVASQ VAIMRPERVQ ALVTVASSPC FAARDDWPGI
KPEVLAGFQQ QLSDDFQRTV ERFLALQTMG TESARQDARA LKQAVLSLPM PSAEALNGGL
EILRTVDLRQ ALVRLPMPFL RLYGRLDGLV PRKIVPLLDD LWPESESILF DKAAHAPFVS
HPAAFCEPLL ALKTRLG
