ID A0A2A6YTY8_HELPX Unreviewed; 218 AA. AC A0A2A6YTY8; DT 20-DEC-2017, integrated into UniProtKB/TrEMBL. DT 20-DEC-2017, sequence version 1. DT 16-JAN-2019, entry version 5. DE RecName: Full=ATP-dependent dethiobiotin synthetase BioD {ECO:0000256|HAMAP-Rule:MF_00336}; DE EC=6.3.3.3 {ECO:0000256|HAMAP-Rule:MF_00336}; DE AltName: Full=DTB synthetase {ECO:0000256|HAMAP-Rule:MF_00336}; DE Short=DTBS {ECO:0000256|HAMAP-Rule:MF_00336}; DE AltName: Full=Dethiobiotin synthase {ECO:0000256|HAMAP-Rule:MF_00336}; GN Name=bioD {ECO:0000256|HAMAP-Rule:MF_00336}; GN ORFNames=BB472_00315 {ECO:0000313|EMBL:PDX46352.1}; OS Helicobacter pylori (Campylobacter pylori). OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Helicobacter. OX NCBI_TaxID=210 {ECO:0000313|EMBL:PDX46352.1, ECO:0000313|Proteomes:UP000220159}; RN [1] {ECO:0000313|EMBL:PDX46352.1, ECO:0000313|Proteomes:UP000220159} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=2007 {ECO:0000313|EMBL:PDX46352.1, RC ECO:0000313|Proteomes:UP000220159}; RX PubMed=28912838; DOI=.1186/s13099-017-0201-1; RA Gutierrez-Escobar A.J., Trujillo E., Acevedo O., Bravo M.M.; RT "Phylogenomics of Colombian Helicobacter pylori isolates."; RL Gut Pathog 9:52-52(2017). CC -!- FUNCTION: Catalyzes a mechanistically unusual reaction, the ATP- CC dependent insertion of CO2 between the N7 and N8 nitrogen atoms of CC 7,8-diaminopelargonic acid (DAPA) to form an ureido ring. CC {ECO:0000256|HAMAP-Rule:MF_00336, ECO:0000256|SAAS:SAAS00385301}. CC -!- CATALYTIC ACTIVITY: CC Reaction=7,8-diaminononanoate + ATP + CO2 = ADP + dethiobiotin + 3 CC H(+) + phosphate; Xref=Rhea:RHEA:15805, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:16526, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:57861, ChEBI:CHEBI:58500, ChEBI:CHEBI:456216; CC EC=6.3.3.3; Evidence={ECO:0000256|HAMAP-Rule:MF_00336, CC ECO:0000256|SAAS:SAAS01124672}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00336, ECO:0000256|SAAS:SAAS00385353}; CC -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis; biotin from CC 7,8-diaminononanoate: step 1/2. {ECO:0000256|HAMAP-Rule:MF_00336, CC ECO:0000256|SAAS:SAAS00385290}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00336, CC ECO:0000256|SAAS:SAAS00701772}. CC -!- SIMILARITY: Belongs to the dethiobiotin synthetase family. CC {ECO:0000256|HAMAP-Rule:MF_00336, ECO:0000256|SAAS:SAAS00701766}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00336}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:PDX46352.1}. 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; MBJM01000001; PDX46352.1; -; Genomic_DNA. DR UniPathway; UPA00078; UER00161. DR Proteomes; UP000220159; Unassembled WGS sequence. 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:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0009102; P:biotin biosynthetic process; IEA:UniProtKB-UniRule. DR HAMAP; MF_00336; BioD; 1. DR InterPro; IPR004472; DTB_synth_BioD. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR43210; PTHR43210; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00347; bioD; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00336, KW ECO:0000256|SAAS:SAAS00089817}; KW Biotin biosynthesis {ECO:0000256|HAMAP-Rule:MF_00336, KW ECO:0000256|SAAS:SAAS00089830}; KW Complete proteome {ECO:0000313|Proteomes:UP000220159}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00336, KW ECO:0000256|SAAS:SAAS00701761}; KW Ligase {ECO:0000256|HAMAP-Rule:MF_00336, KW ECO:0000256|SAAS:SAAS00089835}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00336, KW ECO:0000256|SAAS:SAAS00089822}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00336, KW ECO:0000256|SAAS:SAAS00462117}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00336, KW ECO:0000256|SAAS:SAAS00089833}. FT NP_BIND 10 15 ATP. {ECO:0000256|HAMAP-Rule:MF_00336}. FT NP_BIND 116 119 ATP. {ECO:0000256|HAMAP-Rule:MF_00336}. FT NP_BIND 189 191 ATP. {ECO:0000256|HAMAP-Rule:MF_00336}. FT METAL 10 10 Magnesium 1. {ECO:0000256|HAMAP-Rule: FT MF_00336}. FT METAL 14 14 Magnesium 2. {ECO:0000256|HAMAP-Rule: FT MF_00336}. FT METAL 50 50 Magnesium 2. {ECO:0000256|HAMAP-Rule: FT MF_00336}. FT METAL 116 116 Magnesium 2. {ECO:0000256|HAMAP-Rule: FT MF_00336}. FT BINDING 39 39 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_00336}. FT BINDING 50 50 ATP. {ECO:0000256|HAMAP-Rule:MF_00336}. SQ SEQUENCE 218 AA; 24522 MW; 437FCCE3F82D1D9A CRC64; MLFISATNTN AGKTTCARLL AQYCNACGVK TILLKPIETG VNDAINHSSD AHLFLQDNRL LDRSLTLKDV SFYRYHKASA PLIAQQEEDP NAPIDTDNLT QRLHNFTKTY DLVIVEGAGG LCVPITLEEN MLDFALKLKA KMLLISHDNL GLINDCLLND FLLKSHQLDY QIAINLRENN TAFHSISLPY IELFNKRSNN PIVIFQQSLK ELMSFALK //