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
//