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
//