ID A0A0M7GC82_ENTCL Unreviewed; 260 AA. AC A0A0M7GC82; DT 09-DEC-2015, integrated into UniProtKB/TrEMBL. DT 09-DEC-2015, sequence version 1. DT 10-APR-2019, entry version 23. DE RecName: Full=Pimeloyl-[acyl-carrier protein] methyl ester esterase {ECO:0000256|HAMAP-Rule:MF_01260, ECO:0000256|SAAS:SAAS00064125}; DE EC=3.1.1.85 {ECO:0000256|HAMAP-Rule:MF_01260, ECO:0000256|SAAS:SAAS00370949}; DE AltName: Full=Biotin synthesis protein BioH {ECO:0000256|HAMAP-Rule:MF_01260}; DE AltName: Full=Carboxylesterase BioH {ECO:0000256|HAMAP-Rule:MF_01260}; GN Name=bioH_1 {ECO:0000313|EMBL:STQ08699.1}; GN Synonyms=bioH {ECO:0000256|HAMAP-Rule:MF_01260}; GN ORFNames=NCTC10005_01385 {ECO:0000313|EMBL:STQ08699.1}; OS Enterobacter cloacae. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Enterobacter; Enterobacter cloacae complex. OX NCBI_TaxID=550 {ECO:0000313|EMBL:STQ08699.1, ECO:0000313|Proteomes:UP000255106}; RN [1] {ECO:0000313|EMBL:STQ08699.1, ECO:0000313|Proteomes:UP000255106} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NCTC10005 {ECO:0000313|EMBL:STQ08699.1, RC ECO:0000313|Proteomes:UP000255106}; RG Pathogen Informatics; RA Doyle S.; RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: The physiological role of BioH is to remove the methyl CC group introduced by BioC when the pimeloyl moiety is complete. It CC allows to synthesize pimeloyl-ACP via the fatty acid synthetic CC pathway through the hydrolysis of the ester bonds of pimeloyl-ACP CC esters. {ECO:0000256|HAMAP-Rule:MF_01260, CC ECO:0000256|SAAS:SAAS00186858}. CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + pimeloyl-[ACP] methyl ester = H(+) + methanol + CC pimeloyl-[ACP]; Xref=Rhea:RHEA:42700, Rhea:RHEA-COMP:9955, CC Rhea:RHEA-COMP:10186, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:17790, ChEBI:CHEBI:78846, ChEBI:CHEBI:82735; CC EC=3.1.1.85; Evidence={ECO:0000256|HAMAP-Rule:MF_01260, CC ECO:0000256|SAAS:SAAS01122655}; CC -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis. CC {ECO:0000256|HAMAP-Rule:MF_01260, ECO:0000256|SAAS:SAAS00370947}. CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_01260, CC ECO:0000256|SAAS:SAAS00370950}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01260, CC ECO:0000256|SAAS:SAAS00370942}. CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. CC Carboxylesterase BioH family. {ECO:0000256|HAMAP-Rule:MF_01260, CC ECO:0000256|SAAS:SAAS00561353}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; UGJB01000004; STQ08699.1; -; Genomic_DNA. DR RefSeq; WP_013099094.1; NZ_MTFV01000022.1. DR EnsemblBacteria; CUI92421; CUI92421; ERS370009_02983. DR UniPathway; UPA00078; -. DR Proteomes; UP000255106; Unassembled WGS sequence. 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 3: Inferred from homology; KW Biotin biosynthesis {ECO:0000256|HAMAP-Rule:MF_01260, KW ECO:0000256|SAAS:SAAS00064126}; KW Complete proteome {ECO:0000313|Proteomes:UP000255106}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01260, KW ECO:0000256|SAAS:SAAS00064115}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01260, KW ECO:0000256|SAAS:SAAS00064120, ECO:0000313|EMBL:STQ08699.1}; KW Serine esterase {ECO:0000256|HAMAP-Rule:MF_01260, KW ECO:0000256|SAAS:SAAS00064127}. FT REGION 82 83 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_01260}. FT REGION 143 147 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_01260}. FT ACT_SITE 82 82 Nucleophile. {ECO:0000256|HAMAP-Rule: FT MF_01260}. FT ACT_SITE 207 207 {ECO:0000256|HAMAP-Rule:MF_01260}. FT ACT_SITE 235 235 {ECO:0000256|HAMAP-Rule:MF_01260}. FT BINDING 22 22 Substrate; via amide nitrogen and FT carbonyl oxygen. {ECO:0000256|HAMAP-Rule: FT MF_01260}. FT BINDING 235 235 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_01260}. SQ SEQUENCE 260 AA; 28645 MW; E0ECC8D805342B4F CRC64; MKTLWWQTVG TGNRHLVLLH GWGLNAEVWH CVNEELASHF TLHLVDLPGF GRSCGYGAMS LDEMAQQVLA AAPQQAIWLG WSLGGLVASE VALTNPERVQ ALVTVASSPN FSAQEEWPGI KPDVLSNFQR QLSEDYQRTV ERFLALQTMG TESARKDARL LKQTVLSLPM PDVEVLNGGL ELLKTVDLRE PLTALAVPHL RIYGYLDGLV PRKVVPLLDE LWPESQSLTI AKAAHAPFIS HPAEFCSALI AFSHEVPTTP //