ID BIOD_ANOFW Reviewed; 222 AA. AC B7GHM4; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 10-FEB-2009, sequence version 1. DT 02-SEP-2026, entry version 87. 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=Aflv_1070; OS Anoxybacillus flavithermus (strain DSM 21510 / WK1). OC Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Anoxybacillaceae; OC Anoxybacillus. OX NCBI_TaxID=491915; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 21510 / WK1; RX PubMed=19014707; DOI=10.1186/gb-2008-9-11-r161; RA Saw J.H., Mountain B.W., Feng L., Omelchenko M.V., Hou S., Saito J.A., RA Stott M.B., Li D., Zhao G., Wu J., Galperin M.Y., Koonin E.V., RA Makarova K.S., Wolf Y.I., Rigden D.J., Dunfield P.F., Wang L., Alam M.; RT "Encapsulated in silica: genome, proteome and physiology of the RT thermophilic bacterium Anoxybacillus flavithermus WK1."; RL Genome Biol. 9:R161.1-R161.16(2008). 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; CP000922; ACJ33446.1; -; Genomic_DNA. DR RefSeq; WP_012574709.1; NC_011567.1. DR AlphaFoldDB; B7GHM4; -. DR SMR; B7GHM4; -. DR STRING; 491915.Aflv_1070; -. DR GeneID; 7037327; -. DR KEGG; afl:Aflv_1070; -. DR PATRIC; fig|491915.6.peg.1092; -. DR eggNOG; COG0132; Bacteria. DR HOGENOM; CLU_072551_3_0_9; -. DR UniPathway; UPA00078; UER00161. 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. FT CHAIN 1..222 FT /note="ATP-dependent dethiobiotin synthetase BioD" FT /id="PRO_1000119855" 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 113..116 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00336" FT BINDING 113 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00336" SQ SEQUENCE 222 AA; 24875 MW; 8EDD14D3E0CC87AA CRC64; MKGFFITGTD TDVGKTFVTA CMLRTLVDKR IRATAYKPVQ SGAQWREGKW IAPDVDVYRK VIDVTDEDGC TYLLQTPCSP HLAAKIDGVT IEPDHIVAHV HQLQQTYDFV LVEGAGGIAV PLVDDSFLIA HLAQLLHFPL IIVARASVGT INHTVLTVEY AKAFGLQIAG IIMNGFSTPK NEIEQENIRM IEEMTHVPVI GEIPHMTNFS HQQIVWRKEW WQ //