ID   B8N2F9_ASPFN            Unreviewed;       498 AA.
AC   B8N2F9;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 69.
DE   RecName: Full=alanine transaminase {ECO:0000256|ARBA:ARBA00026106};
DE            EC=2.6.1.2 {ECO:0000256|ARBA:ARBA00026106};
GN   ORFNames=AFLA_036440 {ECO:0000313|EMBL:EED56372.1};
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:EED56372.1, ECO:0000313|Proteomes:UP000001875};
RN   [1] {ECO:0000313|EMBL:EED56372.1, 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   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- PATHWAY: Amino-acid degradation; L-alanine degradation via transaminase
CC       pathway; pyruvate from L-alanine: step 1/1.
CC       {ECO:0000256|ARBA:ARBA00025708}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family. Alanine aminotransferase subfamily.
CC       {ECO:0000256|ARBA:ARBA00025785}.
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DR   EMBL; EQ963473; EED56372.1; -; Genomic_DNA.
DR   RefSeq; XP_002375154.1; XM_002375113.1.
DR   AlphaFoldDB; B8N2F9; -.
DR   STRING; 332952.B8N2F9; -.
DR   EnsemblFungi; EED56372; EED56372; AFLA_036440.
DR   VEuPathDB; FungiDB:AFLA_001523; -.
DR   eggNOG; KOG0258; Eukaryota.
DR   HOGENOM; CLU_014254_3_0_1; -.
DR   OMA; FGFECPP; -.
DR   UniPathway; UPA00528; UER00586.
DR   Proteomes; UP000001875; Unassembled WGS sequence.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   GO; GO:0042853; P:L-alanine catabolic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd00609; AAT_like; 1.
DR   Gene3D; 1.10.287.1970; -; 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; IPR045088; ALAT1/2-like.
DR   InterPro; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR11751; ALANINE AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR11751:SF29; ALANINE TRANSAMINASE; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000313|EMBL:EED56372.1};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EED56372.1}.
FT   DOMAIN          112..480
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   498 AA;  54829 MW;  CE7E1E1AD36643FF CRC64;
     MATQTTVSYT TTRTLSTPAR CLNPDNINPH VTEAKYAVRG ELAVKAEEYR VKLANGDKSL
     PFDSVIFANI GNPQQLDQKP ITFFRQVLSL LENPQLLNNT EALRTSFGYE QDVVDRAKKL
     LADVQSVGAY SHSQGAPVIR QSIAKFIEER DGFPANPQDL FCCAGASSGV STILNIICNG
     PQAGVLVPIP QYPLYTATLS LLNAQCVPYL LEEQKAWGTD VTAIRNSLAQ ARSTGTDVRS
     IVVINPGNPT GASLSAEDIK NVLDLAAEEK LVVIADEVYQ TNVFEGEFIS FKKRLRQLQQ
     ETPGKYDYVE LVSLHSVSKG MVGECGHRGG YFELVGFDPE VQAQIYKLVS IGLCPPVIGQ
     CLLELMVNPP KEGEGSYELY QKEYNGISEG LHKRAFALYE AFQQMEGVEC QKPQGAMYLF
     PTITLPPKAI EAAKAENRAA DEFYCLRLLD ATGVCVVPGS GFGQKENTLH FRTTFLAPGT
     DWVERIVKFH SEFMAKYK
//