ID A0A1Y6BXU0_9PROT Unreviewed; 660 AA. AC A0A1Y6BXU0; DT 30-AUG-2017, integrated into UniProtKB/TrEMBL. DT 30-AUG-2017, sequence version 1. DT 22-NOV-2017, entry version 4. 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=SAMN06296036_11097 {ECO:0000313|EMBL:SMF33592.1}; OS Pseudobacteriovorax antillogorgiicola. OC Bacteria; Proteobacteria; Oligoflexia; Oligoflexales; OC Pseudobacteriovoracaceae; Pseudobacteriovorax. OX NCBI_TaxID=1513793 {ECO:0000313|EMBL:SMF33592.1, ECO:0000313|Proteomes:UP000192907}; RN [1] {ECO:0000313|EMBL:SMF33592.1, ECO:0000313|Proteomes:UP000192907} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RKEM611 {ECO:0000313|EMBL:SMF33592.1, RC ECO:0000313|Proteomes:UP000192907}; RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I., RA Dimitrov K.M., Suarez D.L., Swayne D.E.; RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases. 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: ATP + 7,8-diaminononanoate + CO(2) = ADP + CC phosphate + dethiobiotin. {ECO:0000256|HAMAP-Rule:MF_00336, CC ECO:0000256|SAAS:SAAS00385333}. 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 -!- SIMILARITY: Belongs to the dethiobiotin synthetase family. CC {ECO:0000256|HAMAP-Rule:MF_00336}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|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; FWZT01000010; SMF33592.1; -; Genomic_DNA. DR UniPathway; UPA00078; UER00161. DR Proteomes; UP000192907; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004015; F:adenosylmethionine-8-amino-7-oxononanoate transaminase activity; IEA:InterPro. 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:0030170; F:pyridoxal phosphate binding; IEA:InterPro. DR GO; GO:0009102; P:biotin biosynthetic process; IEA:UniProtKB-UniRule. DR CDD; cd00610; OAT_like; 1. DR Gene3D; 3.40.640.10; -; 1. DR Gene3D; 3.90.1150.10; -; 2. DR HAMAP; MF_00336; BioD; 1. DR InterPro; IPR005814; Aminotrans_3. DR InterPro; IPR005815; BioA. DR InterPro; IPR004472; DTB_synth_BioD. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_sub2. DR Pfam; PF00202; Aminotran_3; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF53383; SSF53383; 1. DR TIGRFAMs; TIGR00508; bioA; 1. DR TIGRFAMs; TIGR00347; bioD; 1. DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 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:UP000192907}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00336}; 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}; KW Reference proteome {ECO:0000313|Proteomes:UP000192907}. FT NP_BIND 105 108 ATP. {ECO:0000256|HAMAP-Rule:MF_00336}. FT METAL 13 13 Magnesium 1. {ECO:0000256|HAMAP-Rule: FT MF_00336}. FT METAL 17 17 Magnesium 2. {ECO:0000256|HAMAP-Rule: FT MF_00336}. FT METAL 48 48 Magnesium 2. {ECO:0000256|HAMAP-Rule: FT MF_00336}. FT METAL 105 105 Magnesium 2. {ECO:0000256|HAMAP-Rule: FT MF_00336}. FT BINDING 42 42 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_00336}. FT BINDING 48 48 ATP. {ECO:0000256|HAMAP-Rule:MF_00336}. SQ SEQUENCE 660 AA; 72577 MW; 28124FC2ED3CD5E2 CRC64; MSYKLFVTGT DTDVGKTFVS QSLLIGALRQ EFDLSYWKPV QTGHPDSDLA SIKKQIPDLK ARPTSFVYKE PASPDQAASL ELRPAPRLEQ LLEELQQIQE NTLIEGAGGL LVPLNEDNET WLSFLKKAGI PCIVVARTGL GTLNHTALTL RTLDLHNVPV AAVILSGKKH EANERSLSRM FPEHRFLHLD SIEDTHSSSY TEACQRLWCD LTASAVSSPS SLLALDQKHC WHPYTQHKGA ATPLEIKRAE GPWLHVSTGE KLIDGTSSWW SNTIGHGRPE IAEAIFKQQQ TIDHIIFAGA THEGAVKLSQ RLSQLTEHQF PRVFFTDNGS CAVEVGLKIA AQMAFNRGDK GRTKFLSLEG AYHGDTFGAM SVGGTEGFHG PFSPFQFESL KIKPVTAHPS AICPEGAAAR ETEIQKLKAL FSSCGHELAA VVLEPMVQGA SGMNMHDLTW LRSLVAIAKD HQVPVIFDEV FTGLGRCGAW FAYQKAGVEP DIICLAKGLT GGNLPLAVTM TTDRIFEQFY SDDKRKALYH GHTYTANAIC CAAANATLDI YEREDLIKRS AEIESRFKSW IKQHEAELGL AQARAMGSIL AWEIPGSGLG DYFNPIAARV PEEARKFGLF LRPLGNTMYF LPALTITDEE LSFCLNALEK TVRAISSYNA //