ID   A0A178AY44_9PLEO        Unreviewed;       381 AA.
AC   A0A178AY44;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   SubName: Full=Threonine aldolase {ECO:0000313|EMBL:OAL02765.1};
GN   ORFNames=IQ06DRAFT_217711 {ECO:0000313|EMBL:OAL02765.1};
OS   Stagonospora sp. SRC1lsM3a.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Massarineae; Massarinaceae; Stagonospora.
OX   NCBI_TaxID=765868 {ECO:0000313|EMBL:OAL02765.1, ECO:0000313|Proteomes:UP000077206};
RN   [1] {ECO:0000313|EMBL:OAL02765.1, ECO:0000313|Proteomes:UP000077206}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SRC1lsM3a {ECO:0000313|EMBL:OAL02765.1,
RC   ECO:0000313|Proteomes:UP000077206};
RG   DOE Joint Genome Institute;
RA   Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA   Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT   "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT   ascomycete fungi.";
RL   Submitted (MAY-2016) 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}.
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DR   EMBL; KV441709; OAL02765.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A178AY44; -.
DR   STRING; 765868.A0A178AY44; -.
DR   InParanoid; A0A178AY44; -.
DR   OrthoDB; 178754at2759; -.
DR   Proteomes; UP000077206; 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; 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   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:UP000077206}.
FT   DOMAIN          29..319
FT                   /note="Aromatic amino acid beta-eliminating lyase/threonine
FT                   aldolase"
FT                   /evidence="ECO:0000259|Pfam:PF01212"
FT   MOD_RES         225
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR017617-1"
SQ   SEQUENCE   381 AA;  41255 MW;  2B0BF7B442D99314 CRC64;
     MRKEQAIEQL LRDHTGSIAW KSAGPAATDF RSDVITTPTL RMLAAIVNTS LRDDVFGEDT
     TTREFESDIA ARCGQESGLF TITGTMANQL GLRTLLTQPP HAILANAQAH IITHEAGGPA
     FMSGAMIQAV EPSNGKYLTV ADIEANAVLT DNIHKCPTRV IALENTIGGV IVPLSEMVKI
     SAWARRNNVK LYLDGARLFE AVAAGAGSLR DYCQLVDVIA LDFSKGLGAP MGAMLLGRKE
     HIAQARWIRK SIGGGMRQAG VLTAAARVAF EEQFGPGEHG QATKLSRVHE MAKNVSNMWK
     SKGGRVTKDV ETNQVWIDLN TLGITREEWN EIGESHGISL DGPRLVLHHQ ISEEALQKLE
     QAFDTAISRA AKPDKGETCR S
//