ID H3ZF30_9ALTE Unreviewed; 251 AA.
AC H3ZF30;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 24-JAN-2024, entry version 52.
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=AJE_09824 {ECO:0000313|EMBL:EHR40848.1};
OS Alishewanella jeotgali KCTC 22429.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Alishewanella.
OX NCBI_TaxID=1129374 {ECO:0000313|EMBL:EHR40848.1, ECO:0000313|Proteomes:UP000012046};
RN [1] {ECO:0000313|EMBL:EHR40848.1, ECO:0000313|Proteomes:UP000012046}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 22429 {ECO:0000313|EMBL:EHR40848.1,
RC ECO:0000313|Proteomes:UP000012046};
RX PubMed=22461542; DOI=10.1128/JB.00153-12;
RA Jung J., Chun J., Park W.;
RT "Genome Sequence of Extracellular-Protease-Producing Alishewanella jeotgali
RT Isolated from Traditional Korean Fermented Seafood.";
RL J. Bacteriol. 194:2097-2097(2012).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EHR40848.1}.
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; AHTH01000028; EHR40848.1; -; Genomic_DNA.
DR RefSeq; WP_008950736.1; NZ_AHTH01000028.1.
DR AlphaFoldDB; H3ZF30; -.
DR STRING; 1129374.AJE_09824; -.
DR PATRIC; fig|1129374.4.peg.1956; -.
DR eggNOG; COG0596; Bacteria.
DR UniPathway; UPA00078; -.
DR Proteomes; UP000012046; 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 PRINTS; PR00111; ABHYDROLASE.
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 Serine esterase {ECO:0000256|ARBA:ARBA00022487, ECO:0000256|HAMAP-
KW Rule:MF_01260}.
FT DOMAIN 10..239
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000259|Pfam:PF00561"
FT ACT_SITE 79
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01260"
FT ACT_SITE 204
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01260"
FT ACT_SITE 232
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01260"
FT BINDING 18
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01260"
FT BINDING 79..80
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01260"
FT BINDING 140..144
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01260"
FT BINDING 232
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01260"
SQ SEQUENCE 251 AA; 27261 MW; AB65CA37BEF1D8F2 CRC64;
MAEHSTTAKP TLVLLHGWGL NQGVWSEVQL QLAGDFQVLA LDLPGFGLSR QFPPAYRLDE
VLSQLAAQLP EQSYLCGWSL GGLLAIALAA TYPDKVKQLA LVAATPKFLA TDDWPGMRAE
VMQQFASALS QNLPQTIQRF LAIQALGSEH AKQDILKLRD SIAHFPEAQP QAVVQALTLL
ADTDLRQQFA ALTQPVVGCY GRLDSLVPVA VLPLLQQLQP AAKLTVLAKA SHAPFISHPG
EFCQWLRSAL Q
//
