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-OCT-2020, entry version 11.
DE   RecName: Full=7,8-diamino-pelargonic acid aminotransferase {ECO:0000256|ARBA:ARBA00018788};
DE   AltName: Full=7,8-diaminononanoate synthase {ECO:0000256|ARBA:ARBA00016315};
DE   AltName: Full=Diaminopelargonic acid synthase {ECO:0000256|ARBA:ARBA00021746};
GN   ORFNames=A2007_00915 {ECO:0000313|EMBL:OHE71634.1};
OS   Verrucomicrobia bacterium GWC2_42_7.
OC   Bacteria; Verrucomicrobia.
OX   NCBI_TaxID=1802430 {ECO:0000313|EMBL:OHE71634.1, ECO:0000313|Proteomes:UP000184561};
RN   [1] {ECO:0000313|EMBL:OHE71634.1, ECO:0000313|Proteomes:UP000184561}
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., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004746}.
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 EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {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   UniPathway; UPA00078; -.
DR   Proteomes; UP000184561; Unassembled WGS sequence.
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:UniProtKB-UniPathway.
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|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
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
//