ID A0A0M7GC82_9BURK Unreviewed; 260 AA. AC A0A0M7GC82; DT 09-DEC-2015, integrated into UniProtKB/TrEMBL. DT 09-DEC-2015, sequence version 1. DT 10-MAY-2017, entry version 13. DE RecName: Full=Pimeloyl-[acyl-carrier protein] methyl ester esterase {ECO:0000256|HAMAP-Rule:MF_01260, ECO:0000256|SAAS:SAAS00646000}; DE EC=3.1.1.85 {ECO:0000256|HAMAP-Rule:MF_01260, ECO:0000256|SAAS:SAAS00645997}; 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 {ECO:0000256|HAMAP-Rule:MF_01260, GN ECO:0000313|EMBL:CUI92421.1}; GN ORFNames=ERS370009_02983 {ECO:0000313|EMBL:CUI92421.1}; OS Achromobacter sp. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Alcaligenaceae; Achromobacter. OX NCBI_TaxID=134375 {ECO:0000313|EMBL:CUI92421.1, ECO:0000313|Proteomes:UP000053062}; RN [1] {ECO:0000313|EMBL:CUI92421.1, ECO:0000313|Proteomes:UP000053062} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC13047 {ECO:0000313|EMBL:CUI92421.1, RC ECO:0000313|Proteomes:UP000053062}; RA Jackson K.R., Lunt B.L., Fisher J.N.B., Gardner A.V., Bailey M.E., RA Deus L.M., Earl A.S., Gibby P.D., Hartmann K.A., Liu J.E., Manci A.M., RA Nielsen D.A., Solomon M.B., Breakwell D.P., Burnett S.H., Grose J.H.; RL Submitted (SEP-2015) 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:SAAS00645987}. CC -!- CATALYTIC ACTIVITY: Pimeloyl-[acyl-carrier protein] methyl ester + CC H(2)O = pimeloyl-[acyl-carrier protein] + methanol. CC {ECO:0000256|HAMAP-Rule:MF_01260, ECO:0000256|SAAS:SAAS00646002}. CC -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis. CC {ECO:0000256|HAMAP-Rule:MF_01260, ECO:0000256|SAAS:SAAS00645991}. CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_01260, CC ECO:0000256|SAAS:SAAS00645993}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01260, CC ECO:0000256|SAAS:SAAS00646004}. CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. CC Carboxylesterase BioH family. {ECO:0000256|HAMAP-Rule:MF_01260, CC ECO:0000256|SAAS:SAAS00645995}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01260}. 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; CYTA01000018; CUI92421.1; -; Genomic_DNA. DR RefSeq; WP_013099094.1; NZ_CYTA01000018.1. DR RefSeq; WP_013099094.1; NZ_CYTA01000018.1. DR RefSeq; WP_013099094.1; NZ_CYTA01000018.1. DR ProteinModelPortal; A0A0M7GC82; -. DR UniPathway; UPA00078; -. DR Proteomes; UP000053062; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009102; P:biotin biosynthetic process; IEA:UniProtKB-HAMAP. 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:SAAS00645985}; KW Complete proteome {ECO:0000313|Proteomes:UP000053062}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01260, KW ECO:0000256|SAAS:SAAS00645998}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01260, KW ECO:0000256|SAAS:SAAS00645988, ECO:0000313|EMBL:CUI92421.1}; KW Serine esterase {ECO:0000256|HAMAP-Rule:MF_01260, KW ECO:0000256|SAAS:SAAS00645990}. FT DOMAIN 15 242 AB hydrolase-1 (Alpha/Beta hydrolase fold FT 1). {ECO:0000259|Pfam:PF00561}. FT REGION 82 83 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 //