ID A0A2A6YTY8_HELPX Unreviewed; 218 AA. AC A0A2A6YTY8; DT 20-DEC-2017, integrated into UniProtKB/TrEMBL. DT 20-DEC-2017, sequence version 1. DT 07-APR-2021, entry version 12. 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=10.1186/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 7,8- CC diaminopelargonic acid (DAPA, also called 7,8-diammoniononanoate) to CC form a ureido ring. {ECO:0000256|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:0000256|HAMAP- CC Rule:MF_00336}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|ARBA:ARBA00001946, CC ECO:0000256|HAMAP-Rule:MF_00336}; CC -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis; biotin from 7,8- CC diaminononanoate: step 1/2. {ECO:0000256|HAMAP-Rule:MF_00336}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00336}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00336}. CC -!- SIMILARITY: Belongs to the dethiobiotin synthetase family. CC {ECO:0000256|HAMAP-Rule:MF_00336}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00336}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {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 EnsemblBacteria; PDX46352; PDX46352; BB472_00315. 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|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_00336}; KW Biotin biosynthesis {ECO:0000256|ARBA:ARBA00022756, ECO:0000256|HAMAP- KW Rule:MF_00336}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00336}; KW Ligase {ECO:0000256|HAMAP-Rule:MF_00336}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00336}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00336}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_00336}. FT NP_BIND 10..15 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00336" FT NP_BIND 116..119 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00336" FT NP_BIND 176..177 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00336" FT NP_BIND 189..191 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00336" FT ACT_SITE 35 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00336" FT METAL 14 FT /note="Magnesium" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00336" FT METAL 50 FT /note="Magnesium" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00336" FT METAL 116 FT /note="Magnesium" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00336" FT BINDING 39 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00336" FT BINDING 50 FT /note="ATP" FT /evidence="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 //