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Database: UniProt
Entry: A0A072PDE3_9EURO
LinkDB: A0A072PDE3_9EURO
Original site: A0A072PDE3_9EURO 
ID   A0A072PDE3_9EURO        Unreviewed;       374 AA.
AC   A0A072PDE3;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=Threonine aldolase {ECO:0000313|EMBL:KEF57881.1};
GN   ORFNames=A1O9_05802 {ECO:0000313|EMBL:KEF57881.1};
OS   Exophiala aquamarina CBS 119918.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX   NCBI_TaxID=1182545 {ECO:0000313|EMBL:KEF57881.1, ECO:0000313|Proteomes:UP000027920};
RN   [1] {ECO:0000313|EMBL:KEF57881.1, ECO:0000313|Proteomes:UP000027920}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 119918 {ECO:0000313|EMBL:KEF57881.1,
RC   ECO:0000313|Proteomes:UP000027920};
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 Exophiala aquamarina CBS 119918.";
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:KEF57881.1}.
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DR   EMBL; AMGV01000004; KEF57881.1; -; Genomic_DNA.
DR   RefSeq; XP_013260471.1; XM_013405017.1.
DR   AlphaFoldDB; A0A072PDE3; -.
DR   STRING; 1182545.A0A072PDE3; -.
DR   GeneID; 25280724; -.
DR   VEuPathDB; FungiDB:A1O9_05802; -.
DR   HOGENOM; CLU_029381_1_1_1; -.
DR   OrthoDB; 178754at2759; -.
DR   Proteomes; UP000027920; 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; 3.40.640.10; 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   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:UP000027920}.
FT   DOMAIN          24..316
FT                   /note="Aromatic amino acid beta-eliminating lyase/threonine
FT                   aldolase"
FT                   /evidence="ECO:0000259|Pfam:PF01212"
FT   MOD_RES         221
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR017617-1"
SQ   SEQUENCE   374 AA;  40403 MW;  75A17AF2C53AB904 CRC64;
     MAGGPWNKGG SAHLAEAAAD VAFDFRSDVV TVPTESMLRA VWHTTYKDDV HREDATTESF
     QRDMAAMTGH EAGLFVLSGT MGNGLALRSL LSQPPYAILV DARSNVLNWE TGHVASSTGA
     LVQPVEARRN GKYLTLEDIL DHVVLDESVT SCPTRVIALE NTLHGMIMPL IEVRRIASFA
     REHGVKLHLD GARLFDASVA GAGSLADYCR EFDTVSLCFS KGLGAPVGSM LVAGEQVIRQ
     ARKLRQSIGG GLHQAGILTA MARVALFEIF GDGADGQHSV LATCHQKAAQ IAELWVRSGG
     KLLKPAETCM VFLDLQSAGL SKPDLVSMAA EQGLRIMSER LVVHHRKYSP HSTYCCLTLT
     DHPRRDHQRG DPTS
//
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