ID   Q0U9C3_PHANO            Unreviewed;       447 AA.
AC   Q0U9C3;
DT   05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2006, sequence version 1.
DT   27-MAR-2024, entry version 88.
DE   RecName: Full=4-aminobutyrate aminotransferase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=SNOG_11641 {ECO:0000313|EMBL:EAT80685.1};
OS   Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS   blotch fungus) (Parastagonospora nodorum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC   Parastagonospora.
OX   NCBI_TaxID=321614 {ECO:0000313|EMBL:EAT80685.1, ECO:0000313|Proteomes:UP000001055};
RN   [1] {ECO:0000313|Proteomes:UP000001055}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173
RC   {ECO:0000313|Proteomes:UP000001055};
RX   PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA   Hane J.K., Lowe R.G., Solomon P.S., Tan K.C., Schoch C.L., Spatafora J.W.,
RA   Crous P.W., Kodira C., Birren B.W., Galagan J.E., Torriani S.F.,
RA   McDonald B.A., Oliver R.P.;
RT   "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT   analysis of the wheat pathogen Stagonospora nodorum.";
RL   Plant Cell 19:3347-3368(2007).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|ARBA:ARBA00008954,
CC       ECO:0000256|RuleBase:RU003560}.
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DR   EMBL; CH445344; EAT80685.1; -; Genomic_DNA.
DR   RefSeq; XP_001801880.1; XM_001801828.1.
DR   AlphaFoldDB; Q0U9C3; -.
DR   STRING; 321614.Q0U9C3; -.
DR   EnsemblFungi; SNOT_11641; SNOT_11641; SNOG_11641.
DR   GeneID; 5978793; -.
DR   KEGG; pno:SNOG_11641; -.
DR   VEuPathDB; FungiDB:JI435_116410; -.
DR   eggNOG; KOG1401; Eukaryota.
DR   HOGENOM; CLU_016922_10_1_1; -.
DR   InParanoid; Q0U9C3; -.
DR   OMA; GAIETMK; -.
DR   OrthoDB; 345661at2759; -.
DR   Proteomes; UP000001055; Unassembled WGS sequence.
DR   GO; GO:0003867; F:4-aminobutyrate transaminase activity; IBA:GO_Central.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR   GO; GO:0009450; P:gamma-aminobutyric acid catabolic process; IBA:GO_Central.
DR   CDD; cd00610; OAT_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; IPR005814; Aminotrans_3.
DR   InterPro; IPR049704; Aminotrans_3_PPA_site.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR11986; AMINOTRANSFERASE CLASS III; 1.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000256|ARBA:ARBA00022576};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001055};
KW   Transferase {ECO:0000256|ARBA:ARBA00022576}.
SQ   SEQUENCE   447 AA;  47565 MW;  C3624A64F0B77B20 CRC64;
     MDAAAFGEQH IAKGIGRLTK HVFEEGNGTW ITTDKGVKLL DLTAGIGVVN LGHCHPKVSA
     AAAKQCGKIT HAQVNIGFSS AQITLLKELI PILPDPSLDT VFLWNSGAEA VEAAVKLARA
     ATKKPNIIVM QGSYHGRTNA TSSMTRSKTI YGEGHGPLMG GVFATAFPYY SQFGGATPGT
     PTEELVNQSL LQLKLTLQQQ TSPADTAAII LEPVLGEGGY VPAPPAFMHG LRKICDEHNI
     LLIADEVQSG MGRTGHMWFV EESGVRPDIL IFAKGIANGF PLSGIASSKE FMDRQKPGSM
     GGTYAGNAVA CAAATATIQA FKEERILDNV AARSKQIFSF LNNLKSSGTK AGNLIEDVRG
     SGLMVGVQFA NPALQRDSSN VASKDAQSQP QLAPKIVQEC VKRNMLLLST SVFDVLRFIP
     PLTISEDEMT QACNIFKESL EAVAKDL
//