ID A0A1Y6BXU0_9BACT Unreviewed; 660 AA. AC A0A1Y6BXU0; DT 30-AUG-2017, integrated into UniProtKB/TrEMBL. DT 30-AUG-2017, sequence version 1. DT 27-NOV-2024, entry version 28. DE RecName: Full=Multifunctional fusion protein {ECO:0000256|HAMAP-Rule:MF_00336, ECO:0000256|HAMAP-Rule:MF_00834}; DE Includes: DE RecName: Full=Adenosylmethionine-8-amino-7-oxononanoate aminotransferase {ECO:0000256|HAMAP-Rule:MF_00834}; DE EC=2.6.1.62 {ECO:0000256|HAMAP-Rule:MF_00834}; DE AltName: Full=7,8-diamino-pelargonic acid aminotransferase {ECO:0000256|HAMAP-Rule:MF_00834}; DE AltName: Full=7,8-diaminononanoate synthase {ECO:0000256|HAMAP-Rule:MF_00834}; DE AltName: Full=Diaminopelargonic acid synthase {ECO:0000256|HAMAP-Rule:MF_00834}; DE Short=DANS {ECO:0000256|HAMAP-Rule:MF_00834}; DE Short=DAPA AT {ECO:0000256|HAMAP-Rule:MF_00834}; DE Short=DAPA aminotransferase {ECO:0000256|HAMAP-Rule:MF_00834}; DE Includes: 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 AltName: Full=Dethiobiotin synthase {ECO:0000256|HAMAP-Rule:MF_00336}; DE Short=DTBS {ECO:0000256|HAMAP-Rule:MF_00336}; GN Name=bioD {ECO:0000256|HAMAP-Rule:MF_00336}; GN Synonyms=bioA {ECO:0000256|HAMAP-Rule:MF_00834}; GN ORFNames=SAMN06296036_11097 {ECO:0000313|EMBL:SMF33592.1}; OS Pseudobacteriovorax antillogorgiicola. OC Bacteria; Bdellovibrionota; Oligoflexia; Oligoflexales; OC Pseudobacteriovoracaceae; Pseudobacteriovorax. OX NCBI_TaxID=1513793 {ECO:0000313|EMBL:SMF33592.1, ECO:0000313|Proteomes:UP000192907}; RN [1] {ECO:0000313|Proteomes:UP000192907} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RKEM611 {ECO:0000313|Proteomes:UP000192907}; RA Varghese N., Submissions S.; 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 7,8- CC diaminopelargonic acid (DAPA, also called 7,8-diammoniononanoate) to CC form a ureido ring. {ECO:0000256|HAMAP-Rule:MF_00336}. CC -!- FUNCTION: Catalyzes the transfer of the alpha-amino group from S- CC adenosyl-L-methionine (SAM) to 7-keto-8-aminopelargonic acid (KAPA) to CC form 7,8-diaminopelargonic acid (DAPA). It is the only aminotransferase CC known to utilize SAM as an amino donor. {ECO:0000256|HAMAP- CC Rule:MF_00834}. 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:0000256|HAMAP- CC Rule:MF_00336}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(8S)-8-amino-7-oxononanoate + S-adenosyl-L-methionine = S- CC adenosyl-4-methylsulfanyl-2-oxobutanoate + (7R,8S)-7,8- CC diammoniononanoate; Xref=Rhea:RHEA:16861, ChEBI:CHEBI:16490, CC ChEBI:CHEBI:59789, ChEBI:CHEBI:149468, ChEBI:CHEBI:149469; CC EC=2.6.1.62; Evidence={ECO:0000256|HAMAP-Rule:MF_00834}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00336}; CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000256|ARBA:ARBA00001933, CC ECO:0000256|HAMAP-Rule:MF_00834}; CC -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis; 7,8- CC diaminononanoate from 8-amino-7-oxononanoate (SAM route): step 1/1. CC {ECO:0000256|HAMAP-Rule:MF_00834}. 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 class-III pyridoxal-phosphate-dependent CC aminotransferase family. BioA subfamily. {ECO:0000256|HAMAP- CC Rule:MF_00834}. 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; FWZT01000010; SMF33592.1; -; Genomic_DNA. DR AlphaFoldDB; A0A1Y6BXU0; -. DR STRING; 1513793.SAMN06296036_11097; -. DR UniPathway; UPA00078; UER00160. 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:UniProtKB-UniRule. 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:UniProtKB-UniRule. DR GO; GO:0009102; P:biotin biosynthetic process; IEA:UniProtKB-UniRule. DR CDD; cd03109; DTBS; 1. DR CDD; cd00610; OAT_like; 1. DR FunFam; 3.40.640.10:FF:000004; Acetylornithine aminotransferase; 1. DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1. DR HAMAP; MF_00834; BioA; 1. DR HAMAP; MF_00336; BioD; 1. DR InterPro; IPR005814; Aminotrans_3. DR InterPro; IPR049704; Aminotrans_3_PPA_site. 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. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small. DR NCBIfam; TIGR00508; bioA; 1. DR NCBIfam; TIGR00347; bioD; 1. DR PANTHER; PTHR42684; ADENOSYLMETHIONINE-8-AMINO-7-OXONONANOATE AMINOTRANSFERASE; 1. DR PANTHER; PTHR42684:SF21; ADENOSYLMETHIONINE-8-AMINO-7-OXONONANOATE AMINOTRANSFERASE; 1. DR Pfam; PF13500; AAA_26; 1. DR Pfam; PF00202; Aminotran_3; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR SUPFAM; SSF53383; PLP-dependent transferases; 1. DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1. PE 3: Inferred from homology; KW Aminotransferase {ECO:0000256|ARBA:ARBA00022576, ECO:0000256|HAMAP- KW Rule:MF_00834}; ATP-binding {ECO:0000256|HAMAP-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|HAMAP-Rule:MF_00336}; KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP- KW Rule:MF_00834}; Reference proteome {ECO:0000313|Proteomes:UP000192907}; KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP- KW Rule:MF_00834}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_00834}. FT ACT_SITE 38 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00336" FT BINDING 13..18 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00336" FT BINDING 17 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00336" FT BINDING 42 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00336" FT BINDING 48 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00336" FT BINDING 48 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00336" FT BINDING 105..108 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00336" FT BINDING 105 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00336" FT BINDING 269 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00834" FT BINDING 329..330 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00834" FT BINDING 362 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00834" FT BINDING 468 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00834" FT BINDING 497 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00834" FT BINDING 531 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00834" FT BINDING 532..533 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00834" FT BINDING 622 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00834" FT SITE 234 FT /note="Participates in the substrate recognition with KAPA FT and in a stacking interaction with the adenine ring of SAM" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00834" FT MOD_RES 497 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00834" 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 //