ID   BIOH_PHOLL              Reviewed;         261 AA.
AC   Q7N9V7;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   27-MAR-2024, entry version 115.
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=plu0204;
OS   Photorhabdus laumondii subsp. laumondii (strain DSM 15139 / CIP 105565 /
OS   TT01) (Photorhabdus luminescens subsp. laumondii).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Photorhabdus.
OX   NCBI_TaxID=243265;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15139 / CIP 105565 / TT01;
RX   PubMed=14528314; DOI=10.1038/nbt886;
RA   Duchaud E., Rusniok C., Frangeul L., Buchrieser C., Givaudan A.,
RA   Taourit S., Bocs S., Boursaux-Eude C., Chandler M., Charles J.-F.,
RA   Dassa E., Derose R., Derzelle S., Freyssinet G., Gaudriault S., Medigue C.,
RA   Lanois A., Powell K., Siguier P., Vincent R., Wingate V., Zouine M.,
RA   Glaser P., Boemare N., Danchin A., Kunst F.;
RT   "The genome sequence of the entomopathogenic bacterium Photorhabdus
RT   luminescens.";
RL   Nat. Biotechnol. 21:1307-1313(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; BX571859; CAE12499.1; -; Genomic_DNA.
DR   RefSeq; WP_011144604.1; NC_005126.1.
DR   AlphaFoldDB; Q7N9V7; -.
DR   SMR; Q7N9V7; -.
DR   STRING; 243265.plu0204; -.
DR   ESTHER; pholu-BIOH; BioH.
DR   GeneID; 24168446; -.
DR   KEGG; plu:plu0204; -.
DR   eggNOG; COG0596; Bacteria.
DR   HOGENOM; CLU_020336_12_2_6; -.
DR   OrthoDB; 9780744at2; -.
DR   UniPathway; UPA00078; -.
DR   Proteomes; UP000002514; 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; alpha/beta hydrolase; 1.
DR   HAMAP; MF_01260; Carboxylester; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000073; AB_hydrolase_1.
DR   InterPro; IPR010076; BioH.
DR   NCBIfam; TIGR01738; bioH; 1.
DR   PANTHER; PTHR43194; HYDROLASE ALPHA/BETA FOLD FAMILY; 1.
DR   PANTHER; PTHR43194:SF5; PIMELOYL-[ACYL-CARRIER PROTEIN] METHYL ESTER ESTERASE; 1.
DR   Pfam; PF00561; Abhydrolase_1; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE   3: Inferred from homology;
KW   Biotin biosynthesis; Cytoplasm; Hydrolase; Reference proteome;
KW   Serine esterase.
FT   CHAIN           1..261
FT                   /note="Pimeloyl-[acyl-carrier protein] methyl ester
FT                   esterase"
FT                   /id="PRO_0000204486"
FT   DOMAIN          16..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"
SQ   SEQUENCE   261 AA;  29519 MW;  A010A29E2A51B77A CRC64;
     MADLFWQTSD EGSRDLVLLH GWGLNAEVWR SIEMRCAPHF RLHLVDLPGY GRSQKYGPMN
     LADMADEVWR YAPENALWLG WSLGGLVASR IALDHQDKVA GLITVASSPH FSAESDWPGI
     KPEVLHDFEH QLSKDFQRTV ERFLALQTLG TDSARQDARL LKSVVLAQPM PSVEVLHVGL
     EILRTEDLRQ PLAELAIPFL RIYGYLDGLV PRKIINILDE KWPRSVSAMM RHAAHAPFIS
     HPDEFVGLLT EFASREVLQG R
//