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Database: UniProt
Entry: W9XTS1_9EURO
LinkDB: W9XTS1_9EURO
Original site: W9XTS1_9EURO 
ID   W9XTS1_9EURO            Unreviewed;       360 AA.
AC   W9XTS1;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   SubName: Full=Threonine aldolase {ECO:0000313|EMBL:EXJ83937.1};
GN   ORFNames=A1O3_04604 {ECO:0000313|EMBL:EXJ83937.1};
OS   Capronia epimyces CBS 606.96.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Capronia.
OX   NCBI_TaxID=1182542 {ECO:0000313|EMBL:EXJ83937.1, ECO:0000313|Proteomes:UP000019478};
RN   [1] {ECO:0000313|EMBL:EXJ83937.1, ECO:0000313|Proteomes:UP000019478}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 606.96 {ECO:0000313|EMBL:EXJ83937.1,
RC   ECO:0000313|Proteomes:UP000019478};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Capronia epimyces CBS 606.96.";
RL   Submitted (MAR-2013) 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:EXJ83937.1}.
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DR   EMBL; AMGY01000004; EXJ83937.1; -; Genomic_DNA.
DR   RefSeq; XP_007732922.1; XM_007734732.1.
DR   AlphaFoldDB; W9XTS1; -.
DR   STRING; 1182542.W9XTS1; -.
DR   GeneID; 19168722; -.
DR   eggNOG; ENOG502S3GG; Eukaryota.
DR   HOGENOM; CLU_049619_1_0_1; -.
DR   OrthoDB; 143891at2759; -.
DR   Proteomes; UP000019478; Unassembled WGS sequence.
DR   GO; GO:0016829; F:lyase activity; IEA:InterPro.
DR   GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
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; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR48097; L-THREONINE ALDOLASE-RELATED; 1.
DR   PANTHER; PTHR48097:SF5; LOW SPECIFICITY L-THREONINE ALDOLASE; 1.
DR   Pfam; PF01212; Beta_elim_lyase; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000019478}.
FT   DOMAIN          16..291
FT                   /note="Aromatic amino acid beta-eliminating lyase/threonine
FT                   aldolase"
FT                   /evidence="ECO:0000259|Pfam:PF01212"
SQ   SEQUENCE   360 AA;  39511 MW;  AC250EC7E6EFF97C CRC64;
     MSKYNFLDDY SEGAHPRIIE ALARTNMTQQ TAYGNDEFSQ DAREAIRNKI GADEATIHFV
     PSGTAANLLS IASCLRPHEA IIAASSAHIV MKETAAIEAT GHKIITQPAV DGKLTPDKIR
     LAFDQNSIFA HQAKPKMVYI SNATEIGTVY TRSELAAIAA ICKSLDLLIL MDGARLGAAL
     ASSETDMTLN DIYHLTDLFW IGGTKTGALI GEAVVIKDKS LGADFPYHMK QRGALLAKGR
     ILGIQFSTLL QDDLFLHLAR HANSTAAEIS SSLVKMGFNL WAKTETNQVF PILPSALVQE
     LQKEFDFYIW DRLCDGSLVV RVVTSWATEL SKVRRFITMA EEWKAGSQEI AVLEKQKPVV
//
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