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Database: UniProt/TrEMBL
Entry: A0A010QKR6_9PEZI
LinkDB: A0A010QKR6_9PEZI
Original site: A0A010QKR6_9PEZI 
ID   A0A010QKR6_9PEZI        Unreviewed;       485 AA.
AC   A0A010QKR6;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=alanine transaminase {ECO:0000256|ARBA:ARBA00026106};
DE            EC=2.6.1.2 {ECO:0000256|ARBA:ARBA00026106};
GN   ORFNames=CFIO01_06338 {ECO:0000313|EMBL:EXF80632.1};
OS   Colletotrichum fioriniae PJ7.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum acutatum species complex.
OX   NCBI_TaxID=1445577 {ECO:0000313|EMBL:EXF80632.1, ECO:0000313|Proteomes:UP000020467};
RN   [1] {ECO:0000313|EMBL:EXF80632.1, ECO:0000313|Proteomes:UP000020467}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PJ7 {ECO:0000313|EMBL:EXF80632.1,
RC   ECO:0000313|Proteomes:UP000020467};
RA   Baroncelli R., Thon M.R.;
RT   "The genome sequence of Colletotrichum fioriniae PJ7.";
RL   Submitted (FEB-2014) 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:EXF80632.1}.
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DR   EMBL; JARH01000421; EXF80632.1; -; Genomic_DNA.
DR   RefSeq; XP_007595708.1; XM_007595646.1.
DR   AlphaFoldDB; A0A010QKR6; -.
DR   STRING; 1445577.A0A010QKR6; -.
DR   KEGG; cfj:CFIO01_06338; -.
DR   eggNOG; KOG0258; Eukaryota.
DR   HOGENOM; CLU_014254_3_0_1; -.
DR   OrthoDB; 5472891at2759; -.
DR   UniPathway; UPA00528; UER00586.
DR   Proteomes; UP000020467; 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; AT04676P; 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:EXF80632.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000020467};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EXF80632.1}.
FT   DOMAIN          100..467
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   485 AA;  53097 MW;  6E26F7AA3123A249 CRC64;
     MSTTPSRRLN VHNINQHVVA AEYAVRGELA VKSEEYRAKL SKGDKDLPFD AVISANIGNP
     QQLDQKPITF FRQVVSLLEN PLLLEHEDVL QNQLGYKSDA IARAKFLLSK VGSVGAYSAS
     AGVPAIKESI AQFIERRDGF PADPAHIYLS GGASSGVNTL LHIIAQNAQS GVLVPIPQYP
     LYTATLSVLN ATCVPYYLDE AAGWGTDLNT IKAAYEKATS EGTDVRAIVI INPGNPTGAS
     LSEDDIRAVY DYAAEKQLVV MADEVYQTNV FVGKFHSFKS VLRKLQKESP GKYDGVELAS
     LHSISKGMVG ECGHRGGYFE LVNFDPEVEA NIYKFVSITL CAPVIGQCIV ELMVNPPKEG
     EPSYELYKKE YDGIFNGLKE RATALHKAFD QMEGVECGAP QGSMYLFPTI KLPAKATEAA
     QKEGRTADEF YCMRMLEATG VCVVPGSGFG QKEGTLHFRT TFLAPGTDWV GRIINFHKDF
     IEKYR
//
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