BIOCD_BORA1
ID BIOCD_BORA1 Reviewed; 465 AA.
AC Q2KXN6;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Biotin biosynthesis bifunctional protein BioCD {ECO:0000305};
DE Includes:
DE RecName: Full=Malonyl-[acyl-carrier protein] O-methyltransferase {ECO:0000250|UniProtKB:P12999};
DE Short=Malonyl-ACP O-methyltransferase;
DE EC=2.1.1.197 {ECO:0000250|UniProtKB:P12999};
DE AltName: Full=Biotin synthesis protein BioC;
DE Includes:
DE RecName: Full=ATP-dependent dethiobiotin synthetase BioD {ECO:0000255|HAMAP-Rule:MF_00336};
DE EC=6.3.3.3 {ECO:0000255|HAMAP-Rule:MF_00336};
DE AltName: Full=DTB synthetase {ECO:0000255|HAMAP-Rule:MF_00336};
DE Short=DTBS {ECO:0000255|HAMAP-Rule:MF_00336};
DE AltName: Full=Dethiobiotin synthase {ECO:0000255|HAMAP-Rule:MF_00336};
GN Name=bioCD {ECO:0000305}; OrderedLocusNames=BAV2451;
OS Bordetella avium (strain 197N).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=360910;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=197N;
RX PubMed=16885469; DOI=10.1128/jb.01927-05;
RA Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D., King N.D.,
RA Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D., Goble A., Lord A.,
RA Murphy L., Quail M.A., Rutter S., Squares R., Squares S., Woodward J.,
RA Parkhill J., Temple L.M.;
RT "Comparison of the genome sequence of the poultry pathogen Bordetella avium
RT with those of B. bronchiseptica, B. pertussis, and B. parapertussis reveals
RT extensive diversity in surface structures associated with host
RT interaction.";
RL J. Bacteriol. 188:6002-6015(2006).
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 synthesis of pimeloyl-ACP via the fatty
CC acid synthetic pathway (By similarity). {ECO:0000250|UniProtKB:P12999}.
CC -!- FUNCTION: Catalyzes a mechanistically unusual reaction, the ATP-
CC dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8-
CC diaminopelargonic acid (DAPA, also called 7,8-diammoniononanoate) to
CC form a ureido ring. {ECO:0000255|HAMAP-Rule:MF_00336}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(7R,8S)-7,8-diammoniononanoate + ATP + CO2 = (4R,5S)-
CC dethiobiotin + ADP + 3 H(+) + phosphate; Xref=Rhea:RHEA:15805,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:149469, ChEBI:CHEBI:149473,
CC ChEBI:CHEBI:456216; EC=6.3.3.3; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00336};
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 Evidence={ECO:0000250|UniProtKB:P12999};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00336};
CC -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis; biotin from 7,8-
CC diaminononanoate: step 1/2. {ECO:0000255|HAMAP-Rule:MF_00336}.
CC -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis.
CC {ECO:0000250|UniProtKB:P12999}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00336}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the methyltransferase
CC superfamily. {ECO:0000250|UniProtKB:P12999}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the dethiobiotin
CC synthetase family. {ECO:0000255|HAMAP-Rule:MF_00336}.
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DR EMBL; AM167904; CAJ50061.1; -; Genomic_DNA.
DR RefSeq; WP_012418111.1; NC_010645.1.
DR AlphaFoldDB; Q2KXN6; -.
DR SMR; Q2KXN6; -.
DR STRING; 360910.BAV2451; -.
DR EnsemblBacteria; CAJ50061; CAJ50061; BAV2451.
DR GeneID; 41394288; -.
DR KEGG; bav:BAV2451; -.
DR eggNOG; COG0132; Bacteria.
DR eggNOG; COG4106; Bacteria.
DR HOGENOM; CLU_046963_0_0_4; -.
DR OMA; MECASIS; -.
DR OrthoDB; 1739932at2; -.
DR UniPathway; UPA00078; -.
DR UniPathway; UPA00078; UER00161.
DR Proteomes; UP000001977; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004141; F:dethiobiotin synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0102130; F:malonyl-CoA methyltransferase 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; 3.40.50.300; -; 1.
DR HAMAP; MF_00336; BioD; 1.
DR InterPro; IPR004472; DTB_synth_BioD.
DR InterPro; IPR041698; Methyltransf_25.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR43210; PTHR43210; 1.
DR Pfam; PF13649; Methyltransf_25; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR TIGRFAMs; TIGR00347; bioD; 1.
PE 3: Inferred from homology;
KW ATP-binding; Biotin biosynthesis; Cytoplasm; Hydrolase; Ligase; Magnesium;
KW Metal-binding; Methyltransferase; Multifunctional enzyme;
KW Nucleotide-binding; Reference proteome; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..465
FT /note="Biotin biosynthesis bifunctional protein BioCD"
FT /id="PRO_0000412486"
FT REGION 1..254
FT /note="Malonyl-ACP O-methyltransferase"
FT REGION 255..465
FT /note="DTB synthetase"
FT ACT_SITE 283
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00336"
FT BINDING 234
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00336"
FT BINDING 263..268
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00336"
FT BINDING 267
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00336"
FT BINDING 287
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00336"
FT BINDING 295
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00336"
FT BINDING 295
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00336"
FT BINDING 351..354
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00336"
FT BINDING 351
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00336"
FT BINDING 435..437
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00336"
SQ SEQUENCE 465 AA; 50246 MW; E169E9595DA64A9B CRC64;
MTPFLPDRSI AKRFDAAADR YEHHAWAQRH AAEALAERIA ALALPAKPRI LEIGCGTGLL
TRALARRLGP ADWTLSDIAP DMLRQARANL NLPARYLRMD GEHPAGLDGQ YDLICSSLAV
QWFGDLNAGL ARLTRWLRPG GHLAIATLAQ ESFKEWHQAH AVLSLRAATP EYPPVADIRA
GLLPGRVDSE QHVQSHHSGL AFLRGLKGIG ATAPRAGHQP LNTAQLRAVL RQFDRQGACV
TYQFAYGQWR KPRGVFVTGT DTGVGKTLVS ALLTRAWQAD YWKPLQTGLA EESGDSATVA
ALARLPPERL HAPAYALQAP LAPWAAASLE NTCIDATRLT LPETAAPLVV EGAGGLYVPI
DERSLIIDLI DNLGLPVVLA ARSGLGTINH TLLSLEALRA RKLPVLGVIM SGPPSDDNRR
AIEHFGRIPV LAQIPQLDVV DAQAVDLWSK QLPTLDSLLS SNASR
