ID A0A261Q642_9BACT Unreviewed; 416 AA. AC A0A261Q642; DT 20-DEC-2017, integrated into UniProtKB/TrEMBL. DT 20-DEC-2017, sequence version 1. DT 13-NOV-2019, entry version 6. DE SubName: Full=8-amino-7-oxononanoate synthase {ECO:0000313|EMBL:OZI08201.1}; GN ORFNames=BWI93_10520 {ECO:0000313|EMBL:OZI08201.1}; OS Siphonobacter sp. BAB-5385. OC Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Cytophagaceae; OC Siphonobacter; unclassified Siphonobacter. OX NCBI_TaxID=1864822 {ECO:0000313|EMBL:OZI08201.1, ECO:0000313|Proteomes:UP000215802}; RN [1] {ECO:0000313|EMBL:OZI08201.1, ECO:0000313|Proteomes:UP000215802} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BAB-5385 {ECO:0000313|EMBL:OZI08201.1, RC ECO:0000313|Proteomes:UP000215802}; RA Dhebar S., Dhebar S., Bhargava P., Bagatharia S.B., Soni S., RA Joshi M.N.; RT "Draft genome of Siphonobacter sp. BAB-5385."; RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000256|RuleBase:RU003693, CC ECO:0000256|SAAS:SAAS00612749}; CC -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent CC aminotransferase family. {ECO:0000256|RuleBase:RU003693}. 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:OZI08201.1}. 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; NMPS01000101; OZI08201.1; -; Genomic_DNA. DR Proteomes; UP000215802; Unassembled WGS sequence. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro. DR GO; GO:0016740; F:transferase activity; IEA:InterPro. DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro. DR Gene3D; 3.40.640.10; -; 1. DR Gene3D; 3.90.1150.10; -; 1. DR InterPro; IPR001917; Aminotrans_II_pyridoxalP_BS. DR InterPro; IPR004839; Aminotransferase_I/II. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_dom1. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major. DR Pfam; PF00155; Aminotran_1_2; 1. DR SUPFAM; SSF53383; SSF53383; 1. DR PROSITE; PS00599; AA_TRANSFER_CLASS_2; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000215802}; KW Pyridoxal phosphate {ECO:0000256|RuleBase:RU003693, KW ECO:0000256|SAAS:SAAS00473492}; KW Reference proteome {ECO:0000313|Proteomes:UP000215802}. FT DOMAIN 37 390 Aminotran_1_2. {ECO:0000259|Pfam: FT PF00155}. SQ SEQUENCE 416 AA; 45946 MW; A2D609F98CA86C89 CRC64; MANLGPLGQY SDKVHGYFAF PYLEGEIGPH MKFQGKEMLN WSLNNYLGLA NHPEVRQTDA EAAAQWGMAA PMGARMMSGQ TPYHEELERQ LAEFVQKEDA FLLNFGYQGV MSTIEAIVDY KDVIVYDAES HACLIDGIRL HKAKMGKYFT FKHNDMESLE KNLQRATKLA DEQGGGVLVI TEGVFGMSGN IGKLDEIVAL KQKYNFRLLV DDAHGFGTMG ATGSGVAEHL GVQDGVDLHF STFAKSMASI GGFIAGPKAV IQYLRYNLRS QTYAKSLPMP LVIGAMKRLE LLRTRPELRQ NLWNIVNAVQ NGLRSRGFDI GTTQSPVTPV FLHGEHANSV VTQLVVDLRE NLGIFCSIVV YPVVPKGVIM LRIIPTAVHT LEDVERTLDA FDIIQERLTS GTYADKGFAQ VVKSAV //