ID A0A0G4KYK7_9PEZI Unreviewed; 357 AA.
AC A0A0G4KYK7;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Aspartate aminotransferase {ECO:0000256|RuleBase:RU000480};
DE EC=2.6.1.1 {ECO:0000256|RuleBase:RU000480};
DE Flags: Fragment;
GN ORFNames=BN1708_017327 {ECO:0000313|EMBL:CRK14854.1};
OS Verticillium longisporum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX NCBI_TaxID=100787 {ECO:0000313|EMBL:CRK14854.1, ECO:0000313|Proteomes:UP000044602};
RN [1] {ECO:0000313|EMBL:CRK14854.1, ECO:0000313|Proteomes:UP000044602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VL1 {ECO:0000313|EMBL:CRK14854.1};
RA Wang D.B., Wang M.;
RL Submitted (MAY-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|ARBA:ARBA00000984,
CC 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}.
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DR EMBL; CVQH01005947; CRK14854.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G4KYK7; -.
DR STRING; 100787.A0A0G4KYK7; -.
DR OrthoDB; 1123851at2759; -.
DR Proteomes; UP000044602; 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:SF22; ASPARTATE AMINOTRANSFERASE, MITOCHONDRIAL; 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:UP000044602};
KW Transferase {ECO:0000256|RuleBase:RU000480}.
FT DOMAIN 5..352
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:CRK14854.1"
FT NON_TER 357
FT /evidence="ECO:0000313|EMBL:CRK14854.1"
SQ SEQUENCE 357 AA; 38962 MW; E19C06E9E5A02772 CRC64;
GKPYVLPSVR TAEQKVVDAK LNKEYAGITG VPDFTKAAAE LAYGADSSAL SRLAITQSIS
GTGALRIGAE FLKRFFPGEK KIYIPTPSWA NHKAVFSDAG LQVEQYRYYN RDTIGLDFEG
MIADIKAAPK GSVFLFHACA HNPTGVDPTQ EQWKEISAIV KASGHFSFFD MAYQGFASGS
TDKDAFALRH FVAEGHDLCL AQSFAKNMGL YGERVGAFSI VANDAAEAKR VDSQIKIVVR
PMYSNPPIHG ARVAAEILTN PALYKQWLGE VKEMADRIIT MRALLKENLE KLGSKHDWSH
ITSQIGMFAY TGLTPEQMDS LAKEHSVYAT KDGRISVAGI TSDNVGRLAE AIFKVKG
//
