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Database: UniProt
Entry: A0A428TQY2_9HYPO
LinkDB: A0A428TQY2_9HYPO
Original site: A0A428TQY2_9HYPO 
ID   A0A428TQY2_9HYPO        Unreviewed;       408 AA.
AC   A0A428TQY2;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=Aromatic amino acid beta-eliminating lyase/threonine aldolase domain-containing protein {ECO:0000259|Pfam:PF01212};
GN   ORFNames=CEP52_006859 {ECO:0000313|EMBL:RSM04453.1};
OS   Fusarium oligoseptatum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium solani species complex.
OX   NCBI_TaxID=2604345 {ECO:0000313|EMBL:RSM04453.1, ECO:0000313|Proteomes:UP000287144};
RN   [1] {ECO:0000313|EMBL:RSM04453.1, ECO:0000313|Proteomes:UP000287144}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL62579 {ECO:0000313|EMBL:RSM04453.1,
RC   ECO:0000313|Proteomes:UP000287144};
RA   Stajich J.E., Carrillo J., Kijimoto T., Eskalen A., O'Donnell K.,
RA   Kasson M.;
RT   "Comparative genomic analysis of Ambrosia Fusariam Clade fungi.";
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- SIMILARITY: Belongs to the threonine aldolase family.
CC       {ECO:0000256|ARBA:ARBA00006966}.
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:RSM04453.1}.
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DR   EMBL; NKCK01000059; RSM04453.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A428TQY2; -.
DR   STRING; 1325735.A0A428TQY2; -.
DR   Proteomes; UP000287144; Unassembled WGS sequence.
DR   GO; GO:0016829; F:lyase activity; IEA:InterPro.
DR   GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR   CDD; cd06502; TA_like; 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; IPR001597; ArAA_b-elim_lyase/Thr_aldolase.
DR   InterPro; IPR023603; Low_specificity_L-TA-like.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   NCBIfam; NF041359; GntG_guanitoxin; 1.
DR   PANTHER; PTHR48097:SF9; L-THREONINE ALDOLASE; 1.
DR   PANTHER; PTHR48097; L-THREONINE ALDOLASE-RELATED; 1.
DR   Pfam; PF01212; Beta_elim_lyase; 1.
DR   PIRSF; PIRSF017617; Thr_aldolase; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000287144}.
FT   DOMAIN          25..316
FT                   /note="Aromatic amino acid beta-eliminating lyase/threonine
FT                   aldolase"
FT                   /evidence="ECO:0000259|Pfam:PF01212"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         221
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR017617-1"
SQ   SEQUENCE   408 AA;  44808 MW;  8E215D0A79B2E8C5 CRC64;
     MGSMTRDIPC NNWAQNGRTN PASVDLRSDT ITIPTASMLN AIQSCTLGDD VFGEDDNTTQ
     LETYVARRTG KEAGLYVLSG TMGNQLALRS LLTQPPYSVL CDYRSHIFAH EAGGTSSLSG
     AQPQPVVPKN GKYLTLEDLH EHVVLGQDIH TCLTRVISLE NTIHGLVMPL HEIERISTFA
     KEHGIKMHLD GARLWEACVA KAGTLTEFCR HFDTVSLCLS KGLGAPVGSV LVGTEPIIRH
     ARWVRKSIGG GIRQAGILTS AGLVAIRQHF GESDFGEDGL LPATHEMARR VEALWINMGG
     RVIEPAETNM CWLDLKAAGC STERFVELGK EAGLVFMSHR LVTHYQVAQN ADDVLRRLKT
     GLQEGTGRRR EDGWESHWED QHLLVNVGSL RYVQKKPSIT ISKNLLVS
//
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