BIOHC_CELJU
ID BIOHC_CELJU Reviewed; 502 AA.
AC B3PI89;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Biotin biosynthesis bifunctional protein BioHC;
DE Includes:
DE RecName: Full=Carboxylesterase BioH;
DE EC=3.1.1.1;
DE AltName: Full=Biotin synthesis protein BioH;
DE Includes:
DE RecName: Full=Malonyl-[acyl-carrier protein] O-methyltransferase;
DE Short=Malonyl-ACP O-methyltransferase;
DE EC=2.1.1.197;
DE AltName: Full=Biotin synthesis protein BioC;
GN Name=bioC; OrderedLocusNames=CJA_0428;
OS Cellvibrio japonicus (strain Ueda107) (Pseudomonas fluorescens subsp.
OS cellulosa).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Cellvibrionales;
OC Cellvibrionaceae; Cellvibrio.
OX NCBI_TaxID=498211;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ueda107;
RX PubMed=18556790; DOI=10.1128/jb.01701-07;
RA DeBoy R.T., Mongodin E.F., Fouts D.E., Tailford L.E., Khouri H.,
RA Emerson J.B., Mohamoud Y., Watkins K., Henrissat B., Gilbert H.J.,
RA Nelson K.E.;
RT "Insights into plant cell wall degradation from the genome sequence of the
RT soil bacterium Cellvibrio japonicus.";
RL J. Bacteriol. 190:5455-5463(2008).
CC -!- FUNCTION: Converts the free carboxyl group of a malonyl-thioester to
CC its methyl ester by transfer of a methyl group from S-adenosyl-L-
CC methionine (SAM). It allows to synthesize pimeloyl-ACP via the fatty
CC acid synthetic pathway (By similarity). {ECO:0000250}.
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 (By
CC similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a carboxylic ester + H2O = a carboxylate + an alcohol + H(+);
CC Xref=Rhea:RHEA:21164, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29067, ChEBI:CHEBI:30879, ChEBI:CHEBI:33308; EC=3.1.1.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=malonyl-[ACP] + S-adenosyl-L-methionine = malonyl-[ACP] methyl
CC ester + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:17105, Rhea:RHEA-
CC COMP:9623, Rhea:RHEA-COMP:9954, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:78449, ChEBI:CHEBI:78845; EC=2.1.1.197;
CC -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis.
CC -!- SIMILARITY: In the N-terminal section; belongs to the AB hydrolase
CC superfamily. Carboxylesterase BioH family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the methyltransferase
CC superfamily. {ECO:0000305}.
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DR EMBL; CP000934; ACE82969.1; -; Genomic_DNA.
DR RefSeq; WP_012486110.1; NC_010995.1.
DR AlphaFoldDB; B3PI89; -.
DR SMR; B3PI89; -.
DR STRING; 498211.CJA_0428; -.
DR ESTHER; celju-b3pi89; BioH.
DR PRIDE; B3PI89; -.
DR EnsemblBacteria; ACE82969; ACE82969; CJA_0428.
DR KEGG; cja:CJA_0428; -.
DR eggNOG; COG1073; Bacteria.
DR eggNOG; COG2226; Bacteria.
DR HOGENOM; CLU_550729_0_0_6; -.
DR OMA; AHTINEG; -.
DR OrthoDB; 1664438at2; -.
DR UniPathway; UPA00078; -.
DR Proteomes; UP000001036; Chromosome.
DR GO; GO:0010340; F:carboxyl-O-methyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; ISS:UniProtKB.
DR GO; GO:0004141; F:dethiobiotin synthase activity; ISS:UniProtKB.
DR GO; GO:0102130; F:malonyl-CoA methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0080030; F:methyl indole-3-acetate esterase activity; IEA:UniProtKB-EC.
DR GO; GO:0009102; P:biotin biosynthetic process; ISS:UniProtKB.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.150; -; 1.
DR Gene3D; 3.40.50.1820; -; 1.
DR HAMAP; MF_00835; BioC; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR011814; BioC.
DR InterPro; IPR013216; Methyltransf_11.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF12697; Abhydrolase_6; 1.
DR Pfam; PF08241; Methyltransf_11; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR TIGRFAMs; TIGR02072; BioC; 1.
PE 3: Inferred from homology;
KW Biotin biosynthesis; Hydrolase; Methyltransferase; Multifunctional enzyme;
KW Reference proteome; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..502
FT /note="Biotin biosynthesis bifunctional protein BioHC"
FT /id="PRO_0000412489"
FT REGION 1..224
FT /note="Carboxylesterase"
FT REGION 225..502
FT /note="Malonyl-ACP O-methyltransferase"
FT ACT_SITE 72
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 195
FT /evidence="ECO:0000250"
FT ACT_SITE 223
FT /evidence="ECO:0000250"
FT BINDING 12
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 134..138
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 223
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 502 AA; 55021 MW; 4F5D07B07B16B36B CRC64;
MTRPVLVLVH GWGCDSRTWQ PVLDGLRELV PVQLVDLPGF GNTPALETFS LPAVLAAIES
QLPERCVLLG WSLGAMLAVQ LAARLPQQVL GVISLAANAR FVASDDYPHA MAPDVNRQFN
SRFAEQPQAA LKMFTGLLAQ GDVQERALLK QLRTQVPDAI NHNWAQALQL LAELDNRAAL
VQLSQPLLHL LAEQDALVPI AAAESLRGLN SQHQIHVIAG SAHAVHWSQP QQLISAVQDF
YETLATAVDK KRVAQSFGKA AATYDSVAGL QRAVGAQLLD YLPAQLDRTR LLDIGSGTGF
FTAQLATRGA EVIALDIAQG MLDFARQQHP QAADWVCGDA ENLPFAQSSV DFIFSSLVIQ
WCARVPQLMQ ELARVLKPGG RAYISTLGPG TLVELKRAWQ QVDNYVHVNR FVGRTSLEQA
VQQAGMQCLA FVESTRRLYF SRLRDLTHEL KALGAHNINP GQAQGLTGRQ RLQAFSLAYE
RERSPQGLPA SYEVYYLVLC KP
