ID A0A1I6CPJ2_9FIRM Unreviewed; 254 AA. AC A0A1I6CPJ2; DT 22-NOV-2017, integrated into UniProtKB/TrEMBL. DT 22-NOV-2017, sequence version 1. DT 14-DEC-2022, entry version 18. 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=SAMN05660706_101125 {ECO:0000313|EMBL:SFQ95087.1}; OS Desulfoscipio geothermicus DSM 3669. OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Desulfallaceae; OC Desulfoscipio. OX NCBI_TaxID=1121426 {ECO:0000313|EMBL:SFQ95087.1, ECO:0000313|Proteomes:UP000199584}; RN [1] {ECO:0000313|Proteomes:UP000199584} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 3669 {ECO:0000313|Proteomes:UP000199584}; RA Varghese N., Submissions S.; RL Submitted (OCT-2016) 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 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 --------------------------------------------------------------------------- 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; FOYM01000001; SFQ95087.1; -; Genomic_DNA. DR AlphaFoldDB; A0A1I6CPJ2; -. DR STRING; 39060.SAMN05660706_101125; -. DR EnsemblBacteria; SFQ95087; SFQ95087; SAMN05660706_101125. DR UniPathway; UPA00078; UER00161. DR Proteomes; UP000199584; 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 Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_00336; BioD; 1. DR InterPro; IPR004472; DTB_synth_BioD. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR43210; DETHIOBIOTIN SYNTHETASE; 1. DR PIRSF; PIRSF006755; DTB_synth; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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}; Reference proteome {ECO:0000313|Proteomes:UP000199584}. FT ACT_SITE 44 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00336" FT BINDING 19..24 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00336" FT BINDING 23 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00336" FT BINDING 48 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00336" FT BINDING 61 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00336" FT BINDING 61 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00336" FT BINDING 122..125 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00336" FT BINDING 122 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00336" SQ SEQUENCE 254 AA; 26715 MW; 5F27A7E43CD4F4EB CRC64; MYKPLNLLQG YFVTGTDTGI GKTVVTAGLA ANLRQKGINA GIMKPVQTGS KNLNGSLVSV DALFAMTVAG IKDEMELVSP YRLEPPLAPR VAAELTGITI DLFKINRAYQ ELLNRHDFML VEGAGGIMVP IAGRFLMADL IKMLNLPALI VARPGLGTVN HTLLTVEYAK SKGIHVAGII INGLKESEAG TAEKTNPGLI AELSGVPVMG IIPHDAGVDV DTCKPGRVVE LVGAAVDWEM ISLPGTGGMA GEYQ //