BIOH_SALTY
ID BIOH_SALTY Reviewed; 256 AA.
AC Q8ZLI9;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 113.
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}; OrderedLocusNames=STM3509;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
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; AE006468; AAL22371.1; -; Genomic_DNA.
DR RefSeq; NP_462412.1; NC_003197.2.
DR RefSeq; WP_000998146.1; NC_003197.2.
DR PDB; 4NMW; X-ray; 1.50 A; A=1-256.
DR PDBsum; 4NMW; -.
DR AlphaFoldDB; Q8ZLI9; -.
DR SMR; Q8ZLI9; -.
DR STRING; 99287.STM3509; -.
DR ESTHER; salty-BIOH; BioH.
DR PaxDb; Q8ZLI9; -.
DR EnsemblBacteria; AAL22371; AAL22371; STM3509.
DR GeneID; 1255032; -.
DR KEGG; stm:STM3509; -.
DR PATRIC; fig|99287.12.peg.3709; -.
DR HOGENOM; CLU_020336_12_2_6; -.
DR OMA; LHGWGMN; -.
DR PhylomeDB; Q8ZLI9; -.
DR BioCyc; SENT99287:STM3509-MON; -.
DR UniPathway; UPA00078; -.
DR Proteomes; UP000001014; 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..256
FT /note="Pimeloyl-[acyl-carrier protein] methyl ester
FT esterase"
FT /id="PRO_0000204491"
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:4NMW"
FT STRAND 13..19
FT /evidence="ECO:0007829|PDB:4NMW"
FT HELIX 26..32
FT /evidence="ECO:0007829|PDB:4NMW"
FT HELIX 33..37
FT /evidence="ECO:0007829|PDB:4NMW"
FT STRAND 41..45
FT /evidence="ECO:0007829|PDB:4NMW"
FT HELIX 61..69
FT /evidence="ECO:0007829|PDB:4NMW"
FT STRAND 74..81
FT /evidence="ECO:0007829|PDB:4NMW"
FT HELIX 83..94
FT /evidence="ECO:0007829|PDB:4NMW"
FT HELIX 96..98
FT /evidence="ECO:0007829|PDB:4NMW"
FT STRAND 99..106
FT /evidence="ECO:0007829|PDB:4NMW"
FT HELIX 122..132
FT /evidence="ECO:0007829|PDB:4NMW"
FT HELIX 136..145
FT /evidence="ECO:0007829|PDB:4NMW"
FT HELIX 154..166
FT /evidence="ECO:0007829|PDB:4NMW"
FT HELIX 173..185
FT /evidence="ECO:0007829|PDB:4NMW"
FT HELIX 191..194
FT /evidence="ECO:0007829|PDB:4NMW"
FT STRAND 199..204
FT /evidence="ECO:0007829|PDB:4NMW"
FT STRAND 208..210
FT /evidence="ECO:0007829|PDB:4NMW"
FT HELIX 214..221
FT /evidence="ECO:0007829|PDB:4NMW"
FT STRAND 226..230
FT /evidence="ECO:0007829|PDB:4NMW"
FT HELIX 237..240
FT /evidence="ECO:0007829|PDB:4NMW"
FT HELIX 242..254
FT /evidence="ECO:0007829|PDB:4NMW"
SQ SEQUENCE 256 AA; 28269 MW; 085D02EE17DBA339 CRC64;
MNDIWWQTYG EGNCHLVLLH GWGLNAEVWH CIREELGSHF TLHLVDLPGY GRSSGFGAMT
LEEMTAQVAK NAPDQAIWLG WSLGGLVASQ MALTHPERVQ ALVTVASSPC FSAREGWPGI
KPEILGGFQQ QLSDDFQRTV ERFLALQTLG TETARQDART LKSVVLAQPM PDVEVLNGGL
EILKTVDLRE ALKNVNMPFL RLYGYLDGLV PRKIVPLLDT LWPHSTSQIM AKAAHAPFIS
HPAAFCQALM TLKSSL
