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Database: UniProt
Entry: A0A423XD51_9PEZI
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Original site: A0A423XD51_9PEZI 
ID   A0A423XD51_9PEZI        Unreviewed;       455 AA.
AC   A0A423XD51;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   RecName: Full=Aspartate aminotransferase {ECO:0000256|RuleBase:RU000480};
DE            EC=2.6.1.1 {ECO:0000256|RuleBase:RU000480};
GN   ORFNames=VPNG_04119 {ECO:0000313|EMBL:ROW13996.1};
OS   Cytospora leucostoma.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Diaporthales; Valsaceae; Cytospora.
OX   NCBI_TaxID=1230097 {ECO:0000313|EMBL:ROW13996.1, ECO:0000313|Proteomes:UP000285146};
RN   [1] {ECO:0000313|EMBL:ROW13996.1, ECO:0000313|Proteomes:UP000285146}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SXYLt {ECO:0000313|EMBL:ROW13996.1,
RC   ECO:0000313|Proteomes:UP000285146};
RA   Yin Z., Huang L.;
RT   "Host preference determinants of Valsa canker pathogens revealed by
RT   comparative genomics.";
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + L-aspartate = L-glutamate + oxaloacetate;
CC         Xref=Rhea:RHEA:21824, ChEBI:CHEBI:16452, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:29991; EC=2.6.1.1;
CC         Evidence={ECO:0000256|RuleBase:RU000480};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738,
CC       ECO:0000256|RuleBase:RU000480}.
CC   -!- MISCELLANEOUS: In eukaryotes there are cytoplasmic, mitochondrial and
CC       chloroplastic isozymes. {ECO:0000256|RuleBase:RU000480}.
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|ARBA:ARBA00007441}.
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:ROW13996.1}.
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DR   EMBL; LKEB01000016; ROW13996.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A423XD51; -.
DR   STRING; 1230097.A0A423XD51; -.
DR   InParanoid; A0A423XD51; -.
DR   Proteomes; UP000285146; Unassembled WGS sequence.
DR   GO; GO:0004069; F:L-aspartate:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
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; IPR000796; Asp_trans.
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; PTHR11879; ASPARTATE AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR11879:SF55; ASPARTATE TRANSAMINASE; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   PRINTS; PR00799; TRANSAMINASE.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000256|RuleBase:RU000480};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW   Reference proteome {ECO:0000313|Proteomes:UP000285146};
KW   Transferase {ECO:0000256|RuleBase:RU000480}.
FT   DOMAIN          75..446
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   455 AA;  49950 MW;  3F607A3BA2EFBE4F CRC64;
     MPSADDSNNK STKSHRRVYN THSSPTNPTN RIRSIANQMA SPVFTTSFPA EAVPQAPVDA
     LFGLMAAYRA DSSPDKVDLG IGAYRGDDAK PWVLPVVKKA DEIIRNDPDL NHEYLPIAGL
     PSFTSKAADL VFGASSPAVA EKRVASFQTI SGTGAVHLGA LFLAKFYKGN RTVYISDPTW
     ANHTQIFNNV GLPVATYPYF DKETKGLDFE GFKSAIAAAP ERSVVLLHAC AHNPTGVDPT
     EQQWREIAEV IRERKHLPFF DSAYQGFASG DLDRDAGAIR YFAEQGFELL VAQSFAKNFG
     LYGERAGAFH FHTSPAPSAQ DTVARVASQL AILQRSEISN PPAYGARVAS IVLNDEALFA
     EWKENLRTMS GRINDMRTAL RAKLEELGTP GTWNHITDQI GMFSYTGLTE AQVLRLREAF
     HVYLTKNGRI SMAGLNTRNV EYFAKAVDTV VREVK
//
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