ID A0A0G2EDS0_9PEZI Unreviewed; 528 AA.
AC A0A0G2EDS0;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-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=UCDDS831_g04436 {ECO:0000313|EMBL:KKY21062.1};
OS Diplodia seriata.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC Diplodia.
OX NCBI_TaxID=420778 {ECO:0000313|EMBL:KKY21062.1, ECO:0000313|Proteomes:UP000034182};
RN [1] {ECO:0000313|EMBL:KKY21062.1, ECO:0000313|Proteomes:UP000034182}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS831 {ECO:0000313|EMBL:KKY21062.1};
RA Morales-Cruz A., Amrine K.C., Cantu D.;
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KKY21062.1, ECO:0000313|Proteomes:UP000034182}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS831 {ECO:0000313|EMBL:KKY21062.1};
RA Lawrence D.P., Travadon R., Rolshausen P.E., Baumgartner K.;
RT "Distinctive expansion of gene families associated with plant cell wall
RT degradation and secondary metabolism in the genomes of grapevine trunk
RT pathogens.";
RL Submitted (MAY-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:KKY21062.1}.
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DR EMBL; LAQI01000088; KKY21062.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G2EDS0; -.
DR UniPathway; UPA00528; UER00586.
DR Proteomes; UP000034182; 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:KKY21062.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KKY21062.1}.
FT DOMAIN 142..510
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 528 AA; 58156 MW; 2AFCBAB513A0F442 CRC64;
MTATSPVLSR IYIASAAAFV GAQPGHPHSP PHFPAVTART YSSTPAKMKA LSINNINPHV
KEAKYAVRGE LAVKSEEYRA RLAKGDKGDL PFDTVISANI GNPQQLDQKP LTFFRQVASL
IENPLLLDHE DVLKNSLGYR QDVIDRARKL LKDVGSVGAY SQSQGSPAVR EEVAKYIERR
DGYPADPTNI FLSGGASSGV NALLHIICEN EKSGVLVPIP QYPLYTATLS VLNAQAVPYY
LDEASHWGTS LEDIKTGYEK AVADGIDVRA IVVINPGNPT GSSLSAEDIR SVLKFAAEKN
LVVMADEVYQ TNVFSGKFIS FKKALRDLQK AEPGKYDELE LASLHSISKG MVGECGHRGG
YYEMVGFDPQ VKAEIYKFVS IQLCAPVIGQ CFVEMMVNPP KEGEPSYPLY KEEHDGIYKN
YHDRAMALFE AFKKMEGVEC ASPAGSMYLF PTINLPKKAI EQAEKEGRQA DEFYALRMLD
ATGVCTVPGS GFGQKEGTYH FRTTFLAPGT DWVGRIVEFH RKFMEEFR
//
