ID U1LIX5_9GAMM Unreviewed; 245 AA.
AC U1LIX5;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 49.
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=PRUB_25017 {ECO:0000313|EMBL:ERG42362.1};
OS Pseudoalteromonas rubra DSM 6842.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=1117318 {ECO:0000313|EMBL:ERG42362.1};
RN [1] {ECO:0000313|EMBL:ERG42362.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29570 {ECO:0000313|EMBL:ERG42362.1};
RX PubMed=22374963; DOI=10.1128/JB.06822-11;
RA Xie B.B., Shu Y.L., Qin Q.L., Rong J.C., Zhang X.Y., Chen X.L., Zhou B.C.,
RA Zhang Y.Z.;
RT "Genome sequence of the cycloprodigiosin-producing bacterial strain
RT Pseudoalteromonas rubra ATCC 29570(T).";
RL J. Bacteriol. 194:1637-1638(2012).
RN [2] {ECO:0000313|EMBL:ERG42362.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 29570 {ECO:0000313|EMBL:ERG42362.1};
RA Xie B.-B., Rong J.-C., Qin Q.-L., Shu Y.-L., Zhang Y.-Z.;
RT "Genome sequence of Pseudoalteromonas rubra.";
RL Submitted (APR-2013) 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 -!- 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:ERG42362.1}.
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DR EMBL; AHCD02000190; ERG42362.1; -; Genomic_DNA.
DR AlphaFoldDB; U1LIX5; -.
DR eggNOG; COG0596; Bacteria.
DR OrthoDB; 9780744at2; -.
DR UniPathway; UPA00078; -.
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 Serine esterase {ECO:0000256|ARBA:ARBA00022487, ECO:0000256|HAMAP-
KW Rule:MF_01260}.
FT DOMAIN 5..233
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000259|Pfam:PF00561"
FT ACT_SITE 74
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01260"
FT ACT_SITE 199
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01260"
FT ACT_SITE 227
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01260"
FT BINDING 11
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01260"
FT BINDING 74..75
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01260"
FT BINDING 135..139
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01260"
FT BINDING 227
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01260"
SQ SEQUENCE 245 AA; 27043 MW; 0F6B9ACB66DA6BE0 CRC64;
MQSEIVLLHG WGMNKQVWQL SIEQLQQVQP LPVRAINLAG FGGAEFPEHC KSLDDIADEI
ATELADGSVL IGWSLGGLVA LNLAHRYPAK VAKVVMVASN PCFVEQPDWP GIKPKVLAGF
KQALADDSAK TIERFLAIQA MGSEHARDDI KQLRQLLAQL PEPHPEALSL GLDALNRCDY
RAYFRELTQP VFGLFGRLDA LVPGDVIERM SALNPHFKAF VLPKASHAPF ISHKDEFVTH
LKSIL
//
