ID   A0A0F2NWQ2_9FLAO        Unreviewed;       415 AA.
AC   A0A0F2NWQ2;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   SubName: Full=8-amino-7-oxononanoate synthase {ECO:0000313|EMBL:KJS06453.1};
GN   ORFNames=VR77_05510 {ECO:0000313|EMBL:KJS06453.1};
OS   Flavobacteriales bacterium BRH_c54.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales.
OX   NCBI_TaxID=1629721 {ECO:0000313|EMBL:KJS06453.1, ECO:0000313|Proteomes:UP000033681};
RN   [1] {ECO:0000313|EMBL:KJS06453.1, ECO:0000313|Proteomes:UP000033681}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BRH_c54 {ECO:0000313|EMBL:KJS06453.1};
RA   Bagnoud A., Chourey K., Hettich R.L., de Bruijn I., Andersson A.F.,
RA   Leupin O.X., Schwyn B., Bernier-Latmani R.;
RT   "Microbial metabolic network in the subsurface.";
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|RuleBase:RU003693};
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 EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KJS06453.1}.
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DR   EMBL; LADZ01000021; KJS06453.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F2NWQ2; -.
DR   STRING; 1629721.VR77_05510; -.
DR   PATRIC; fig|1629721.3.peg.845; -.
DR   Proteomes; UP000033681; 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; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR001917; Aminotrans_II_pyridoxalP_BS.
DR   InterPro; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR13693; CLASS II AMINOTRANSFERASE/8-AMINO-7-OXONONANOATE SYNTHASE; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00599; AA_TRANSFER_CLASS_2; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003693}.
FT   DOMAIN          45..392
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
FT   COILED          85..112
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   415 AA;  46072 MW;  9377B7E6D664A3AE CRC64;
     MNDIFEKIKN NRGPLGKYSK EAHGYFAFPK LEGELNNKMK FRGKEVLQWS LNNYLGLGNH
     PEIRKADAAA AADWGLAYPM GARMMSGNSN LHEELEAKLA EFEKKQDAIL LNFGYQGMVS
     AIDALVDRND VIVYDAESHA CILDGVRLHQ GKRFVYQHND MDSLRNMLQK ATKLVEKTNG
     AILVITEGVF GMSGNQGSLK EIVALKSEFN FRLFVDDAHG FGTMGPTGAG TGEAQGCQDG
     IDVYFGTFAK SMASIGGFIA ADEQVIEYFR YNMRSQIYAK SMPMPLVVGN LKRLEMLKNS
     PELREKLWTI AHALQNGLKE NGFNIGTTTT QVTPVVLSGD IPEATNLILD LRENFNLFCS
     IVVYPVVPKG VIMLRLIPTA MHTVEDVEYT INTFKLVKEK LLKGDYKSES IASIS
//