ID BIOD1_HAEIN Reviewed; 242 AA. AC P45209; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 28-JAN-2026, entry version 136. DE RecName: Full=ATP-dependent dethiobiotin synthetase BioD 1 {ECO:0000255|HAMAP-Rule:MF_00336}; DE EC=6.3.3.3 {ECO:0000255|HAMAP-Rule:MF_00336}; DE AltName: Full=DTB synthetase 1 {ECO:0000255|HAMAP-Rule:MF_00336}; DE Short=DTBS 1 {ECO:0000255|HAMAP-Rule:MF_00336}; DE AltName: Full=Dethiobiotin synthase 1 {ECO:0000255|HAMAP-Rule:MF_00336}; GN Name=bioD1 {ECO:0000255|HAMAP-Rule:MF_00336}; Synonyms=bioD-A; GN OrderedLocusNames=HI_1445; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Pasteurellales; Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F., RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R., RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D., RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A., RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). 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; L42023; AAC23095.1; -; Genomic_DNA. DR PIR; I64123; I64123. DR AlphaFoldDB; P45209; -. DR SMR; P45209; -. DR STRING; 71421.HI_1445; -. DR EnsemblBacteria; AAC23095; AAC23095; HI_1445. DR KEGG; hin:HI_1445; -. DR PATRIC; fig|71421.8.peg.1507; -. DR eggNOG; COG0132; Bacteria. DR HOGENOM; CLU_072551_0_0_6; -. DR OrthoDB; 9802097at2; -. DR PhylomeDB; P45209; -. DR BioCyc; HINF71421:G1GJ1-1471-MONOMER; -. DR UniPathway; UPA00078; UER00161. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0004141; F:dethiobiotin synthase activity; IBA:GO_Central. 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; IBA:GO_Central. 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; DETHIOBIOTIN SYNTHETASE; 1. DR PANTHER; PTHR43210:SF5; 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..242 FT /note="ATP-dependent dethiobiotin synthetase BioD 1" FT /id="PRO_0000187969" 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 66 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00336" FT BINDING 66 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00336" FT BINDING 124 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00336" FT BINDING 184..185 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00336" FT BINDING 213..215 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00336" FT BINDING 220 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00336" SQ SEQUENCE 242 AA; 26967 MW; 94FCC0501CFAF262 CRC64; MSSFFVAGTD TNVGKTTAAR AMIQALQGQG VQVVGYKPIA CCGEESIYPV AQSENTSDYD HFVNADVLTL MHSTKENVSY QDINSYTFSH CAPMLTQDKM RIKLDKINCD LTRLNQTYQS VVVEGSFGLM TPMAEGKSFA DWIAQQKMPV VLVVGIKDGC VNHALLTVKV IQQLGVPLLG WIANRINPLL SHYAEIVDLL VEHIDAPLLG KIPYLHKPEE QELGHYLTNI DRLMYMQTEF IK //