ID D5CNB5_SIDLE Unreviewed; 269 AA.
AC D5CNB5;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 27-MAR-2024, entry version 77.
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 OrderedLocusNames=Slit_2587 {ECO:0000313|EMBL:ADE12812.1};
OS Sideroxydans lithotrophicus (strain ES-1).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Gallionellaceae; Sideroxydans.
OX NCBI_TaxID=580332 {ECO:0000313|EMBL:ADE12812.1, ECO:0000313|Proteomes:UP000001625};
RN [1] {ECO:0000313|EMBL:ADE12812.1, ECO:0000313|Proteomes:UP000001625}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ES-1 {ECO:0000313|EMBL:ADE12812.1,
RC ECO:0000313|Proteomes:UP000001625};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Munk A.C., Detter J.C., Han C., Tapia R., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Ivanova N., Emerson D., Woyke T.;
RT "Complete sequence of Sideroxydans lithotrophicus ES-1.";
RL Submitted (MAR-2010) 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}.
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; CP001965; ADE12812.1; -; Genomic_DNA.
DR AlphaFoldDB; D5CNB5; -.
DR STRING; 580332.Slit_2587; -.
DR KEGG; slt:Slit_2587; -.
DR eggNOG; COG2267; Bacteria.
DR HOGENOM; CLU_020336_12_2_4; -.
DR UniPathway; UPA00078; -.
DR Proteomes; UP000001625; 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 {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:UP000001625};
KW Serine esterase {ECO:0000256|ARBA:ARBA00022487, ECO:0000256|HAMAP-
KW Rule:MF_01260}.
FT DOMAIN 26..254
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000259|Pfam:PF00561"
FT ACT_SITE 93
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01260"
FT ACT_SITE 219
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01260"
FT ACT_SITE 247
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01260"
FT BINDING 33
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01260"
FT BINDING 93..94
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01260"
FT BINDING 155..159
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01260"
FT BINDING 247
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01260"
SQ SEQUENCE 269 AA; 29689 MW; 563B1F2BB27FA6C3 CRC64;
MARQMFHDLS GHCMSLHIDS IGSGEPLLLL HGWGMHGGVW SEVAQKLAES HRVHSIDLPG
YGFSRDENAP TLDAIVSVLA ACFAEPIAVC GWSLGGQVAM HWAAREPDKV RRLVLVASTP
CFAAREDWPC GMGSEALGKF AEELELNHAA TLRRFIALQL RGSENERELL AVLRERLFSR
GESDKDALRA GLAILRDIDQ RSGLKDIRQP ALVICGERDK LTPPEASRYL AHALPAARYI
EVAGAAHAPF LSHPDFFVEQ MKSFLHERI
//
