ID BIOD_CLOAB Reviewed; 240 AA. AC Q97JC5; DT 25-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2001, sequence version 1. DT 28-JAN-2026, entry version 120. 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=bioD {ECO:0000255|HAMAP-Rule:MF_00336}; GN OrderedLocusNames=CA_C1361; OS Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / IAM OS 19013 / LMG 5710 / NBRC 13948 / NRRL B-527 / VKM B-1787 / 2291 / W). OC Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=272562; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / IAM 19013 / LMG 5710 / NBRC RC 13948 / NRRL B-527 / VKM B-1787 / 2291 / W; RX PubMed=11466286; DOI=10.1128/jb.183.16.4823-4838.2001; RA Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R., RA Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F., RA Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V., RA Smith D.R.; RT "Genome sequence and comparative analysis of the solvent-producing RT bacterium Clostridium acetobutylicum."; RL J. Bacteriol. 183:4823-4838(2001). 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 + CO2 + ATP = (4R,5S)- CC dethiobiotin + ADP + phosphate + 3 H(+); 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 -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP- CC 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 -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00336}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00336}. CC -!- SIMILARITY: Belongs to the dethiobiotin synthetase family. CC {ECO:0000255|HAMAP-Rule:MF_00336}. 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; AE001437; AAK79329.1; -; Genomic_DNA. DR PIR; F97067; F97067. DR RefSeq; WP_010964670.1; NC_003030.1. DR AlphaFoldDB; Q97JC5; -. DR SMR; Q97JC5; -. DR STRING; 272562.CA_C1361; -. DR GeneID; 44997866; -. DR KEGG; cac:CA_C1361; -. DR PATRIC; fig|272562.8.peg.1566; -. DR eggNOG; COG0132; Bacteria. DR HOGENOM; CLU_072551_3_0_9; -. DR OrthoDB; 9802097at2; -. DR UniPathway; UPA00078; UER00161. DR Proteomes; UP000000814; Chromosome. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0004141; F:dethiobiotin synthase activity; IEA:UniProtKB-UniRule. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0042803; F:protein homodimerization activity; IEA:UniProtKB-ARBA. DR GO; GO:0009102; P:biotin biosynthetic process; IEA:UniProtKB-UniRule. DR CDD; cd03109; DTBS; 1. DR FunFam; 3.40.50.300:FF:000292; ATP-dependent dethiobiotin synthetase BioD; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR HAMAP; MF_00336; BioD; 1. DR InterPro; IPR004472; DTB_synth_BioD. DR InterPro; IPR027417; P-loop_NTPase. DR NCBIfam; TIGR00347; bioD; 1. DR PANTHER; PTHR43210:SF2; ATP-DEPENDENT DETHIOBIOTIN SYNTHETASE BIOD 2; 1. DR PANTHER; PTHR43210; DETHIOBIOTIN SYNTHETASE; 1. DR Pfam; PF13500; AAA_26; 1. DR PIRSF; PIRSF006755; DTB_synth; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. PE 3: Inferred from homology; KW ATP-binding; Biotin biosynthesis; Cytoplasm; Ligase; Magnesium; KW Metal-binding; Nucleotide-binding; Reference proteome. FT CHAIN 1..240 FT /note="ATP-dependent dethiobiotin synthetase BioD" FT /id="PRO_0000187958" FT ACT_SITE 37 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00336" FT BINDING 12..17 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00336" FT BINDING 16 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00336" FT BINDING 41 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00336" FT BINDING 54 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00336" FT BINDING 54 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00336" FT BINDING 115..118 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00336" FT BINDING 115 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00336" FT BINDING 179..180 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00336" FT BINDING 207..209 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00336" SQ SEQUENCE 240 AA; 26677 MW; 2FA903A8C23E4AD1 CRC64; MRGIYLVGTD TEIGKTVISA ALVYILCKAG YKTAYFKAAL SDAEELNGKL IPGDTEFVCS LSGIQEDYEK LTPYIYKTAV SPYLASKIEN KPIDIQVIKD KLTKLENEYG YVLCEGSGGV ICPITDVDNK IYTLGNLIKD MKMDVILVCR AGLGTINHTV LTVSYLKNNG IEVKGIIVNQ YEENRLCKDN INMIKKMTGI PILGVMPYIN ENKKNFIEEL KYNACNIFKA DEIAGLMKEV //