ID A0A1G3Z420_9BACT Unreviewed; 445 AA. AC A0A1G3Z420; DT 18-JAN-2017, integrated into UniProtKB/TrEMBL. DT 18-JAN-2017, sequence version 1. DT 07-NOV-2018, entry version 8. DE SubName: Full=Adenosylmethionine--8-amino-7-oxononanoate transaminase {ECO:0000313|EMBL:OHE71634.1}; GN ORFNames=A2007_00915 {ECO:0000313|EMBL:OHE71634.1}; OS Verrucomicrobia bacterium GWC2_42_7. OC Bacteria; Verrucomicrobia; unclassified Verrucomicrobia. OX NCBI_TaxID=1802430 {ECO:0000313|EMBL:OHE71634.1}; RN [1] {ECO:0000313|EMBL:OHE71634.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=27774985; DOI=10.1038/ncomms13219; RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J., RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., RA Brodie E.L., Williams K.H., Hubbard S.S., Banfield J.F.; RT "Thousands of microbial genomes shed light on interconnected RT biogeochemical processes in an aquifer system."; RL Nat. Commun. 7:13219-13219(2016). CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent CC aminotransferase family. {ECO:0000256|RuleBase:RU003560}. 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:OHE71634.1}. 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; MIDO01000097; OHE71634.1; -; Genomic_DNA. DR GO; GO:0004015; F:adenosylmethionine-8-amino-7-oxononanoate transaminase activity; IEA:InterPro. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro. DR GO; GO:0009102; P:biotin biosynthetic process; IEA:InterPro. DR CDD; cd00610; OAT_like; 1. DR Gene3D; 3.40.640.10; -; 1. DR Gene3D; 3.90.1150.10; -; 1. DR InterPro; IPR005814; Aminotrans_3. DR InterPro; IPR005815; BioA. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_dom1. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major. DR Pfam; PF00202; Aminotran_3; 1. DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1. DR SUPFAM; SSF53383; SSF53383; 1. DR TIGRFAMs; TIGR00508; bioA; 1. DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1. PE 3: Inferred from homology; KW Pyridoxal phosphate {ECO:0000256|RuleBase:RU003560}. SQ SEQUENCE 445 AA; 49139 MW; 2FC1D9126EBB021B CRC64; MKSNFTTIDK DHSWHPFTQM REYLGQPLLH VERGDGCWLI DTEGKRYLDC NASIWANVHG HNNQEPNDAI VSQVQKLSHA TMLGLNHTAA TELTERLVRL VPGLQRVFLT DNGATAIEVA LKMSFQYWQL VGKPEKTGVI AMEDGYHGDT FGTMAVGGRS IFHSRFNHWL FPVKHISRPL FSECDGVIKE DDSLAINGLK SLLEKHADTT ACLIFEPSIQ GAAGMQLLPE SFEKKARELC DKFGVHLILD EIFVGCGRTG SMTVCGQQGV SPDFLCLSKG LSGGYLPIGA TLTSNAIFEP FLGSYTEYKT LFHGHTFGGN PLACAVSSKS LEMIETLISS QKLSSTINFF KKTALETFGK NPFVKEIRQR GMTLAIDLFP GKEGETFPPN DRIAFKICIE ARNHGLIIRP LGDSILVVPP LVISNDEISF LFNSLSKSIL SKIGR //