BIOHC_SACD2
ID BIOHC_SACD2 Reviewed; 558 AA.
AC Q21FY5;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 84.
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=Sde_3137;
OS Saccharophagus degradans (strain 2-40 / ATCC 43961 / DSM 17024).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Cellvibrionales;
OC Cellvibrionaceae; Saccharophagus.
OX NCBI_TaxID=203122;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2-40 / ATCC 43961 / DSM 17024;
RX PubMed=18516288; DOI=10.1371/journal.pgen.1000087;
RA Weiner R.M., Taylor L.E. II, Henrissat B., Hauser L., Land M.,
RA Coutinho P.M., Rancurel C., Saunders E.H., Longmire A.G., Zhang H.,
RA Bayer E.A., Gilbert H.J., Larimer F., Zhulin I.B., Ekborg N.A., Lamed R.,
RA Richardson P.M., Borovok I., Hutcheson S.;
RT "Complete genome sequence of the complex carbohydrate-degrading marine
RT bacterium, Saccharophagus degradans strain 2-40 T.";
RL PLoS Genet. 4:E1000087-E1000087(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; CP000282; ABD82394.1; -; Genomic_DNA.
DR RefSeq; WP_011469610.1; NC_007912.1.
DR AlphaFoldDB; Q21FY5; -.
DR SMR; Q21FY5; -.
DR STRING; 203122.Sde_3137; -.
DR ESTHER; sacd2-q21fy5; BioH.
DR EnsemblBacteria; ABD82394; ABD82394; Sde_3137.
DR KEGG; sde:Sde_3137; -.
DR eggNOG; COG2226; Bacteria.
DR eggNOG; COG2267; Bacteria.
DR HOGENOM; CLU_550729_0_0_6; -.
DR OMA; AHTINEG; -.
DR OrthoDB; 1664438at2; -.
DR UniPathway; UPA00078; -.
DR Proteomes; UP000001947; Chromosome.
DR GO; GO:0010340; F:carboxyl-O-methyltransferase activity; IEA:UniProtKB-UniRule.
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; IEA:UniProtKB-UniRule.
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..558
FT /note="Biotin biosynthesis bifunctional protein BioHC"
FT /id="PRO_0000412521"
FT REGION 1..287
FT /note="Carboxylesterase"
FT REGION 288..558
FT /note="Malonyl-ACP O-methyltransferase"
FT ACT_SITE 115
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 246
FT /evidence="ECO:0000250"
FT ACT_SITE 274
FT /evidence="ECO:0000250"
FT BINDING 56
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 115..116
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 182..186
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 274
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 558 AA; 60825 MW; 66A23D5483FA9013 CRC64;
MSNIEPSNVK PSNIELGTIP LAEAPATKLE AAYIAKKIAP NNSNPNAPVW VFVHGWGASA
NTWAPLVDEL KSQCEIWLLD LPSFGGNTQA VNSPSAVAAD IAKILPANTV LVGWSLGGML
LPLIAQQIEQ HWPTKTISHC IGLAANAKFA QGDNYTAAMP AETFQTFCAN FNVDPTTTWS
RFGLLQAQGD SNRKLVSRQI KALHNAPMPE QFTAWQQALT WLGAIDNRVL LCEITTPFLH
LFGEGDALVP ADAAVAMAGI NPLHQTLVVA SAGHVLHFSQ PAKIAQIMLA RVHAKRNKAR
VAKSFSNAAT EYDSVAYLQQ KLANTLCEWV PEQAEKIADL GCGTGYCGLQ LQRPERDIYS
LDLAQGMLHT ARSKALAKQQ LFSGVCADIE CLPFISNGFD ALVSGMSMQW CEDLPAVFSE
AHRVLKPNGE MIFSTLGPQT LFELREAWAE ADIKLGRQGC VHVNTFIELD RVEIAAKQAG
FVIEQTSREI HVLTYDSVMP LMRELKTIGA HNVNPGQEQG LTGKARLKAM AQAYEQFRTA
QGVLPLTYEV GFYQLLKV
