ID   A0A1B7NGF1_9AGAM        Unreviewed;       439 AA.
AC   A0A1B7NGF1;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=PLP-dependent transferase {ECO:0000313|EMBL:OAX43854.1};
GN   ORFNames=K503DRAFT_680099 {ECO:0000313|EMBL:OAX43854.1};
OS   Rhizopogon vinicolor AM-OR11-026.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Boletales; Suillineae; Rhizopogonaceae; Rhizopogon.
OX   NCBI_TaxID=1314800 {ECO:0000313|EMBL:OAX43854.1, ECO:0000313|Proteomes:UP000092154};
RN   [1] {ECO:0000313|EMBL:OAX43854.1, ECO:0000313|Proteomes:UP000092154}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AM-OR11-026 {ECO:0000313|EMBL:OAX43854.1,
RC   ECO:0000313|Proteomes:UP000092154};
RG   DOE Joint Genome Institute;
RA   Mujic A.B., Kuo A., Tritt A., Lipzen A., Chen C., Johnson J., Sharma A.,
RA   Barry K., Grigoriev I.V., Spatafora J.W.;
RT   "Comparative genomics of the ectomycorrhizal sister species Rhizopogon
RT   vinicolor and Rhizopogon vesiculosus (Basidiomycota: Boletales) reveals a
RT   divergence of the mating type B locus.";
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|ARBA:ARBA00007441}.
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DR   EMBL; KV448131; OAX43854.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1B7NGF1; -.
DR   STRING; 1314800.A0A1B7NGF1; -.
DR   InParanoid; A0A1B7NGF1; -.
DR   OrthoDB; 176869at2759; -.
DR   Proteomes; UP000092154; Unassembled WGS sequence.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   CDD; cd00609; AAT_like; 1.
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; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR004838; NHTrfase_class1_PyrdxlP-BS.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR43807; FI04487P; 1.
DR   PANTHER; PTHR43807:SF20; FI04487P; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE   3: Inferred from homology;
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW   Reference proteome {ECO:0000313|Proteomes:UP000092154};
KW   Transferase {ECO:0000313|EMBL:OAX43854.1}.
FT   DOMAIN          51..431
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   439 AA;  49128 MW;  B00F8BD6BC30CC78 CRC64;
     MSSISPTLIQ SKGNLSDDRS NIIPFSSRLH GGRALALDVW SIYNAVNLPA DCINLGQGYM
     NFPPPKWVTD AGDEALKSIL PNHYSHPKGR IRLRNAIKNF YQNSFNRELD VETEIIVTSG
     ANQGQYSVFT AFLEHGDEVI MFEPFFDQYL PSVTFNGGTP VYVPLHPHTD GPKPSSGDWK
     IDFDELRRSI TPKAKMIIIN TPHNPVGKVF TREELENIAL LAEEFNLLVM ADEVYDCLVF
     DGKEHVRFAT LPGMWDRTVT VLSAGKAFAA TGWRVGWLIG PPSIIGPTLA ACTRIVFCSN
     SPLQEAAAAG LEQAAQRGFF ENQVKEYQER RDVLISTFDQ LGLKYSHPEG SYFVLLDISR
     VNFPKDYPFP PTIQGRGRDF KACWFIALEI GVSSIPVSEF YCDDHRGIGE NFARFAFCKD
     VETLRQAGER LKGLAKYLV
//