ID   A0A0F4GTJ0_9PEZI        Unreviewed;       511 AA.
AC   A0A0F4GTJ0;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=alanine transaminase {ECO:0000256|ARBA:ARBA00026106};
DE            EC=2.6.1.2 {ECO:0000256|ARBA:ARBA00026106};
GN   ORFNames=TI39_contig315g00009 {ECO:0000313|EMBL:KJY00727.1};
OS   Zymoseptoria brevis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Zymoseptoria.
OX   NCBI_TaxID=1047168 {ECO:0000313|EMBL:KJY00727.1, ECO:0000313|Proteomes:UP000033647};
RN   [1] {ECO:0000313|EMBL:KJY00727.1, ECO:0000313|Proteomes:UP000033647}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Zb18110 {ECO:0000313|EMBL:KJY00727.1,
RC   ECO:0000313|Proteomes:UP000033647};
RA   Grandaubert J., Bhattacharyya A., Stukenbrock E.H.;
RT   "RNA-seq based gene annotation and comparative genomics of four
RT   Zymoseptoria species reveal species-specific pathogenicity related genes
RT   and transposable element activity.";
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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:KJY00727.1}.
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DR   EMBL; LAFY01000307; KJY00727.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F4GTJ0; -.
DR   STRING; 1047168.A0A0F4GTJ0; -.
DR   OrthoDB; 5472891at2759; -.
DR   UniPathway; UPA00528; UER00586.
DR   Proteomes; UP000033647; 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:KJY00727.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033647};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KJY00727.1}.
FT   DOMAIN          122..493
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   511 AA;  56398 MW;  91CC21B5FFA428DB CRC64;
     MSVAGVLSSV PLPTFVQKRL FTQNTPADRS LGIDNINPHV KEAKYAVRGE LAIKSEEYRA
     QLAKGEGKDL PFDSVISANI GNPQQLDQKP ITFFRQVASL VENPLLLEHE DVLKNSLGYN
     SDAIQRAQKL LKDVKSVGAY SQSQGAPGIR QSVADFIERR DGFPADPANI YLCGGASAGV
     NALMTVICSS PQTGILVPIP QYPLYTATLS LLNAQVVPYY LEEESNWSTN VDGMRTALKE
     AQAKGIDVRA VVVINPGNPT GGSLESSNIK SVIELAAEEK LVVLADEVYQ TNVFEGEFNS
     FKKCLRELQK SEKNNEGKFD NIEMASLHSI SKGMVGECGH RGGYYEMVGF DEKVVEQVYK
     FVSIMLCPPV IGQCLVELMV NPPKEGEPSY AQYREEYDTT FNNLKERANA LYHAFKEMEG
     VECQEPQGSM YLYPTIKLPQ KAIEAAKEAG KSADEFYCLR LLDATGVCIV PGAGFGQKEG
     TLHFRTTFLA PGTEWVKRIT KFHAEFLEKY R
//