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Database: UniProt
Entry: A0A094BQW4_9PEZI
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ID   A0A094BQW4_9PEZI        Unreviewed;       391 AA.
AC   A0A094BQW4;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   13-SEP-2023, entry version 27.
DE   RecName: Full=Aromatic amino acid beta-eliminating lyase/threonine aldolase domain-containing protein {ECO:0000259|Pfam:PF01212};
GN   ORFNames=V494_01654 {ECO:0000313|EMBL:KFY44079.1};
OS   Pseudogymnoascus sp. VKM F-4513 (FW-928).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1420907 {ECO:0000313|EMBL:KFY44079.1, ECO:0000313|Proteomes:UP000029288};
RN   [1] {ECO:0000313|EMBL:KFY44079.1, ECO:0000313|Proteomes:UP000029288}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-4513 (FW-928) {ECO:0000313|Proteomes:UP000029288};
RA   Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA   Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA   Ozerskaya S.M.;
RT   "Population genomics of a fungus Geomyces pannorum provides evidence of
RT   horizontal gene transfer but not of sexual reproduction.";
RL   Submitted (JUL-2014) 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:KFY44079.1}.
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DR   EMBL; JPJW01000548; KFY44079.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A094BQW4; -.
DR   STRING; 1420907.A0A094BQW4; -.
DR   HOGENOM; CLU_029381_1_0_1; -.
DR   OrthoDB; 178754at2759; -.
DR   Proteomes; UP000029288; 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:UP000029288}.
FT   DOMAIN          51..345
FT                   /note="Aromatic amino acid beta-eliminating lyase/threonine
FT                   aldolase"
FT                   /evidence="ECO:0000259|Pfam:PF01212"
FT   MOD_RES         247
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR017617-1"
SQ   SEQUENCE   391 AA;  42205 MW;  6A06D6525CB49DFB CRC64;
     MCSSRRYIST AAHADVRLSS ENPCEDAVTQ ALRHLAVAPI AWNGSGSAAF DFRSDVVTKP
     TLSTLAAIIR SSLDDDVYRE DAATLSLESH MASLTGFADA IFVNSGTMAN QLALRTHLTQ
     PPHAILADSR SHILHWEAGG IASLTGAMIQ TVRPSNGEFL TVEDIKKKVV LSDDVHKCPT
     RLISLENTIG GIVQPLEETR KISAWARENG LLLHLDGARL WEAVAAGKGN LREYATCFDS
     VGLDFSKGLG APMGAVIVGG ADFVARARRI RKGMGGAMRQ VGVLSSAARE SMESIFGPGV
     SGYKDGGLLR RSHRLASKVA GMWTQKGGRL SRRTETNIVW VDLKAAKVEE HLFNEMGTEY
     GLRLDGSRIV LHYQISEAAI AKLGELFNRV L
//
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