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Database: UniProt
Entry: A0A2B7WWB4_9EURO
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ID   A0A2B7WWB4_9EURO        Unreviewed;       408 AA.
AC   A0A2B7WWB4;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=Threonine aldolase {ECO:0000313|EMBL:PGH00738.1};
GN   ORFNames=GX51_05619 {ECO:0000313|EMBL:PGH00738.1};
OS   Blastomyces parvus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Blastomyces.
OX   NCBI_TaxID=2060905 {ECO:0000313|EMBL:PGH00738.1, ECO:0000313|Proteomes:UP000224080};
RN   [1] {ECO:0000313|EMBL:PGH00738.1, ECO:0000313|Proteomes:UP000224080}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH130 {ECO:0000313|EMBL:PGH00738.1,
RC   ECO:0000313|Proteomes:UP000224080};
RA   Munoz J.F., Mcewen J.G., Clay O.K., Cuomo C.A.;
RT   "Comparative genomics in systemic dimorphic fungi from Ajellomycetaceae.";
RL   Submitted (OCT-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:PGH00738.1}.
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DR   EMBL; PDNC01000081; PGH00738.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2B7WWB4; -.
DR   STRING; 2060905.A0A2B7WWB4; -.
DR   OrthoDB; 178754at2759; -.
DR   Proteomes; UP000224080; 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   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:UP000224080}.
FT   DOMAIN          47..339
FT                   /note="Aromatic amino acid beta-eliminating lyase/threonine
FT                   aldolase"
FT                   /evidence="ECO:0000259|Pfam:PF01212"
FT   MOD_RES         252
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR017617-1"
SQ   SEQUENCE   408 AA;  43867 MW;  CA52580AF097E936 CRC64;
     MPPSVSDIRS NLVSNIKSES MENDVNKPYT YSAMPNLKRA IQKAGGDFRS DVSTVPTENM
     MQAILEASVG DDIYDEAGDA SVNALQNKLI ELTGKEAALW ALSGTMGNQI CLRTHLMQPP
     HTVLLDHRAH VYCWESGALP ALSQASVSPV IPSNGIHLTL KDVKKHMVSG DNLHFPPTRV
     VSLENTLSGT ILPLKDAKEI SAFVRSFPVP EGQKPIAMHL DGARLFDGLA GEGVDPKEYC
     ACFDSISICL AKGLGAPMGS VILGSRAFIE RAKWFRKMFG GGTRQPGMMA AAAQAALTAS
     IPQVPRVHAL TKSTASKLAA CGYKFQLPVQ TNMILIDLEA SNDIPPAAFV SYCTAQGLQV
     FPSGRLVFHY QTSEEAVGRL VGALERLMLD KKGGKELENG EVKGGYRT
//
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