ID   A0A3N2PP40_9PEZI        Unreviewed;       484 AA.
AC   A0A3N2PP40;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 13.
DE   RecName: Full=alanine transaminase {ECO:0000256|ARBA:ARBA00026106};
DE            EC=2.6.1.2 {ECO:0000256|ARBA:ARBA00026106};
GN   ORFNames=SODALDRAFT_402142 {ECO:0000313|EMBL:ROT36263.1};
OS   Sodiomyces alkalinus F11.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Sodiomyces.
OX   NCBI_TaxID=1314773 {ECO:0000313|EMBL:ROT36263.1, ECO:0000313|Proteomes:UP000272025};
RN   [1] {ECO:0000313|EMBL:ROT36263.1, ECO:0000313|Proteomes:UP000272025}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F11 {ECO:0000313|EMBL:ROT36263.1,
RC   ECO:0000313|Proteomes:UP000272025};
RX   PubMed=30368956; DOI=10.1111/mec.14912;
RA   Grum-Grzhimaylo A.A., Falkoski D.L., van den Heuvel J.,
RA   Valero-Jimenez C.A., Min B., Choi I.G., Lipzen A., Daum C.G., Aanen D.K.,
RA   Tsang A., Henrissat B., Bilanenko E.N., de Vries R.P., van Kan J.A.L.,
RA   Grigoriev I.V., Debets A.J.M.;
RT   "The obligate alkalophilic soda-lake fungus Sodiomyces alkalinus has
RT   shifted to a protein diet.";
RL   Mol. Ecol. 27:4808-4819(2018).
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; ML119059; ROT36263.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3N2PP40; -.
DR   STRING; 1314773.A0A3N2PP40; -.
DR   OrthoDB; 5472891at2759; -.
DR   UniPathway; UPA00528; UER00586.
DR   Proteomes; UP000272025; 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:ROT36263.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000272025};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ROT36263.1}.
FT   DOMAIN          97..466
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   484 AA;  53217 MW;  B190133811994C4F CRC64;
     MSTLKPRLHI DNISPHVRSA QYAVRGELAT LSEEYRARLA KGDTDLPFDQ VISANIGNPQ
     QLDQKPLTFI RQVLSLVENP KLLDHEDVLL NQLDYKTDVI ERAKWLLSKV GSVGAYSASA
     GVPAIKESIA KFIERRDGFP ADPSKIYLSG GASSGVNTLL HVICAGPDTG VLVPIPQYPL
     YTASLSILNA RCVPYNLDEE SGWSTDLEII RASHDKAVAE GTDVRALVII NPGNPTGASL
     PEDNIRAILA FAAEKNLVVL ADEVYQTNVF EGRFHSFKRV LRLLQQENPN KYDHVELASL
     HSVSKGMIGE CGHRGGYFEL VGFHPEVEAN IYKFVSITLC APVVGQCVVE LMVNPPQPGD
     PSYEQYNAEY SAIFQGLKER ADALHAAFSR MEGVECGPPQ GSMYLFPTIR LPPRAAEAAA
     AEGRSPDEYY CIRLLKATGI CVVPGSGFGQ KKDTLHFRTT FLAPGTDWVG RIVDFHKKFM
     DEHR
//