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Database: UniProt
Entry: B8NDA6_ASPFN
LinkDB: B8NDA6_ASPFN
Original site: B8NDA6_ASPFN 
ID   B8NDA6_ASPFN            Unreviewed;       517 AA.
AC   B8NDA6;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   24-JAN-2024, entry version 71.
DE   RecName: Full=4-aminobutyrate aminotransferase {ECO:0000256|ARBA:ARBA00018543};
DE            EC=2.6.1.19 {ECO:0000256|ARBA:ARBA00012912};
DE   AltName: Full=GABA aminotransferase {ECO:0000256|ARBA:ARBA00031787};
DE   AltName: Full=Gamma-amino-N-butyrate transaminase {ECO:0000256|ARBA:ARBA00030204};
GN   ORFNames=AFLA_056670 {ECO:0000313|EMBL:EED51404.1};
OS   Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS   / JCM 12722 / SRRC 167).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=332952 {ECO:0000313|EMBL:EED51404.1, ECO:0000313|Proteomes:UP000001875};
RN   [1] {ECO:0000313|EMBL:EED51404.1, ECO:0000313|Proteomes:UP000001875}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 /
RC   SRRC 167 {ECO:0000313|Proteomes:UP000001875};
RX   PubMed=25883274; DOI=10.1128/genomeA.00168-15;
RA   Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA   Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT   "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT   aflatoxin contamination of food and feed.";
RL   Genome Announc. 3:E0016815-E0016815(2015).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + 4-aminobutanoate = L-glutamate + succinate
CC         semialdehyde; Xref=Rhea:RHEA:23352, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:57706, ChEBI:CHEBI:59888; EC=2.6.1.19;
CC         Evidence={ECO:0000256|ARBA:ARBA00000442};
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; EQ963477; EED51404.1; -; Genomic_DNA.
DR   RefSeq; XP_002378411.1; XM_002378370.1.
DR   AlphaFoldDB; B8NDA6; -.
DR   STRING; 332952.B8NDA6; -.
DR   EnsemblFungi; EED51404; EED51404; AFLA_056670.
DR   VEuPathDB; FungiDB:AFLA_004707; -.
DR   eggNOG; KOG1405; Eukaryota.
DR   HOGENOM; CLU_016922_12_0_1; -.
DR   OMA; DWPQASF; -.
DR   Proteomes; UP000001875; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
DR   GO; GO:0034386; F:4-aminobutyrate:2-oxoglutarate transaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:EnsemblFungi.
DR   GO; GO:0009450; P:gamma-aminobutyric acid catabolic process; IEA:EnsemblFungi.
DR   GO; GO:0006536; P:glutamate metabolic process; IEA:EnsemblFungi.
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; IPR004631; 4NH2But_aminotransferase_euk.
DR   InterPro; IPR005814; Aminotrans_3.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   NCBIfam; TIGR00699; GABAtrns_euk; 1.
DR   PANTHER; PTHR43206:SF1; 4-AMINOBUTYRATE AMINOTRANSFERASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43206; AMINOTRANSFERASE; 1.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
SQ   SEQUENCE   517 AA;  57222 MW;  9BBA4FCDF46A3F38 CRC64;
     MASIARSSFR LRSVTRVPTA RTISTTPHLR AAAKPFFADE PAGPKLATAI PGPKNKAATA
     ELDKVFDVRS LNMLTDYSKS IGNYIADLDG NVLLDVYAQI ASIPVGYNNP HLTKVAQSPE
     MTTSLINRPA LGNFPSADWA DILNTGILKV APKGLNQVFT AMAGSDANET AYKAAFMYYR
     QLQRGGPEKE FTEEELQTTM NNQSPGSPQL SIMSFKSAFH GRLFGSLSTT RSKPIHKLDI
     PAFDWPQAPF PSLKYPLEEH AQENAQEEQR CLQETERLIK EWHNPVAAVV VEPIQSEGGD
     NHASPAFFRG LREITKRNNV LFIVDEVQTG VGATGKFWAH DHWNLETPPD MVTFSKKAQT
     AGYYYGNPAL RPNKPYRQFN TWMGDPARAL IFRGIIEEIE RLNLVEHTAK TGEYLYSGLQ
     RLAEKYPEHL QNLRGKGQGT FIAWDTPKRD EFLGKAKGVG VNIGGSGVSA VRLRPMLIFQ
     QHHGKSNSTL AQTCRTGANV SAADILLESI EKIIKQL
//
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