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Database: UniProt
Entry: T0LHA3_COLGC
LinkDB: T0LHA3_COLGC
Original site: T0LHA3_COLGC 
ID   T0LHA3_COLGC            Unreviewed;       322 AA.
AC   T0LHA3;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Threonine ammonia-lyase {ECO:0000313|EMBL:EQB50931.1};
GN   ORFNames=CGLO_09577 {ECO:0000313|EMBL:EQB50931.1};
OS   Colletotrichum gloeosporioides (strain Cg-14) (Anthracnose fungus)
OS   (Glomerella cingulata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum gloeosporioides species complex.
OX   NCBI_TaxID=1237896 {ECO:0000313|EMBL:EQB50931.1, ECO:0000313|Proteomes:UP000015530};
RN   [1] {ECO:0000313|Proteomes:UP000015530}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Cg-14 {ECO:0000313|Proteomes:UP000015530};
RX   PubMed=23902260; DOI=10.1094/MPMI-03-13-0080-R;
RA   Alkan N., Meng X., Friedlander G., Reuveni E., Sukno S., Sherman A.,
RA   Thon M., Fluhr R., Prusky D.;
RT   "Global aspects of pacC regulation of pathogenicity genes in Colletotrichum
RT   gloeosporioides as revealed by transcriptome analysis.";
RL   Mol. Plant Microbe Interact. 26:1345-1358(2013).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
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:EQB50931.1}.
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DR   EMBL; AMYD01001926; EQB50931.1; -; Genomic_DNA.
DR   AlphaFoldDB; T0LHA3; -.
DR   STRING; 1237896.T0LHA3; -.
DR   HOGENOM; CLU_021152_4_2_1; -.
DR   OMA; IRHHIYQ; -.
DR   OrthoDB; 5476420at2759; -.
DR   Proteomes; UP000015530; Unassembled WGS sequence.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.50.1100; -; 2.
DR   InterPro; IPR000634; Ser/Thr_deHydtase_PyrdxlP-BS.
DR   InterPro; IPR001926; TrpB-like_PALP.
DR   InterPro; IPR036052; TrpB-like_PALP_sf.
DR   PANTHER; PTHR48078:SF6; ACT DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR48078; THREONINE DEHYDRATASE, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF00291; PALP; 1.
DR   SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1.
DR   PROSITE; PS00165; DEHYDRATASE_SER_THR; 1.
PE   4: Predicted;
KW   Lyase {ECO:0000313|EMBL:EQB50931.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015530}.
FT   DOMAIN          19..306
FT                   /note="Tryptophan synthase beta chain-like PALP"
FT                   /evidence="ECO:0000259|Pfam:PF00291"
SQ   SEQUENCE   322 AA;  33540 MW;  7C3B1ED00E044E83 CRC64;
     MSLSYVETAA AAVQARGRIR DHIYETPLIP ARKAGQKHGI KVLFKGENFQ LTGSFKLRGA
     TSKLSAQGAG GRLITASSGN HGIGAACAAR ALSRDVTVVL PETVVPAKLE KIKSYGVEVI
     LHGAETGLAE QYAQKLAASG TYEYISPYND PDIVAGQGTI GLEILEQCSN VDNIFISMGG
     GGLISGIGSV IKAFSPKTKI FGVSAINSKA LAESMAAGHV VETEHFPTLA EAVAGGMDED
     SITLPLAMAV VDQVIECSEE EIAEAMRTIA FEENMIVEGS AALALAGFNK VAKDLAGNTS
     VILLCGANVD QQAIKKILYG ES
//
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