ID A0A1W1Y0U7_9NEIS Unreviewed; 255 AA.
AC A0A1W1Y0U7;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Pimeloyl-[acyl-carrier protein] methyl ester esterase {ECO:0000256|HAMAP-Rule:MF_01260};
DE EC=3.1.1.85 {ECO:0000256|HAMAP-Rule:MF_01260};
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 ORFNames=SAMN02745857_04117 {ECO:0000313|EMBL:SMC29776.1};
OS Andreprevotia lacus DSM 23236.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC Chitinibacteraceae; Andreprevotia.
OX NCBI_TaxID=1121001 {ECO:0000313|EMBL:SMC29776.1, ECO:0000313|Proteomes:UP000192761};
RN [1] {ECO:0000313|EMBL:SMC29776.1, ECO:0000313|Proteomes:UP000192761}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23236 {ECO:0000313|EMBL:SMC29776.1,
RC ECO:0000313|Proteomes:UP000192761};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (APR-2017) 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:0000256|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:0000256|HAMAP-
CC Rule:MF_01260};
CC -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis.
CC {ECO:0000256|HAMAP-Rule:MF_01260}.
CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_01260}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01260}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Carboxylesterase
CC BioH family. {ECO:0000256|HAMAP-Rule:MF_01260}.
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DR EMBL; FWXD01000044; SMC29776.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W1Y0U7; -.
DR STRING; 1121001.SAMN02745857_04117; -.
DR OrthoDB; 9798888at2; -.
DR UniPathway; UPA00078; -.
DR Proteomes; UP000192761; 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; 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 {ECO:0000256|ARBA:ARBA00022756, ECO:0000256|HAMAP-
KW Rule:MF_01260};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01260};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01260};
KW Reference proteome {ECO:0000313|Proteomes:UP000192761};
KW Serine esterase {ECO:0000256|ARBA:ARBA00022487, ECO:0000256|HAMAP-
KW Rule:MF_01260}.
FT DOMAIN 14..240
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000259|Pfam:PF00561"
FT ACT_SITE 80
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01260"
FT ACT_SITE 206
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01260"
FT ACT_SITE 234
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01260"
FT BINDING 20
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01260"
FT BINDING 80..81
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01260"
FT BINDING 142..146
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01260"
FT BINDING 234
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01260"
SQ SEQUENCE 255 AA; 27898 MW; 5B4EF4E7444A4479 CRC64;
MSLYFDTVGR GEDVVWLHGW AMNGTVWRQT AAALADDFCH QLVDLPGHGR SAPLAGLTLE
GMVDALEATF PNPVHVVGWS LGGAVATSWA LRRPDQVRSL TLVASSPCFA QRDDWQPAMP
MRTLQQFAAS LGDDWQGTLR RFINLQTLGS PSAREQSKTL LAELLLHGEP DQAALREGLD
ILRDTDLRTR IAELDVPLLL QFGDKDTLSP LGAGDWLAQQ RPDAQYVVHK GAAHVPFLSH
ADDFIAAQRA FLSAI
//
