ID A0A229YNV9_9EURO Unreviewed; 360 AA.
AC A0A229YNV9;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Aromatic amino acid beta-eliminating lyase/threonine aldolase domain-containing protein {ECO:0000259|Pfam:PF01212};
GN ORFNames=CDV55_100820 {ECO:0000313|EMBL:RHZ55711.1}, CFD26_103113
GN {ECO:0000313|EMBL:RLL95852.1};
OS Aspergillus turcosus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1245748 {ECO:0000313|EMBL:RHZ55711.1, ECO:0000313|Proteomes:UP000215394};
RN [1] {ECO:0000313|Proteomes:UP000215289, ECO:0000313|Proteomes:UP000215394}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HMR AF 1038 {ECO:0000313|EMBL:RLL95852.1}, and HMR AF 23
RC {ECO:0000313|EMBL:RHZ55711.1};
RA Parent-Michaud M., Dufresne P.J., Fournier E., Martineau C., Moreira S.,
RA Perkins V., De Repentigny L., Dufresne S.F.;
RT "Draft genome sequences of two Aspergillus turcosus clinical strains
RT isolated from bronchoalveolar lavage fluid: one azole-susceptible and the
RT other azole-resistant.";
RL Submitted (AUG-2018) 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:RHZ55711.1}.
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DR EMBL; NKHV02000156; RHZ55711.1; -; Genomic_DNA.
DR EMBL; NIDN02000134; RLL95852.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A229YNV9; -.
DR STRING; 1245748.A0A229YNV9; -.
DR OrthoDB; 143891at2759; -.
DR Proteomes; UP000215289; Unassembled WGS sequence.
DR Proteomes; UP000215394; 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:UP000215289}.
FT DOMAIN 43..305
FT /note="Aromatic amino acid beta-eliminating lyase/threonine
FT aldolase"
FT /evidence="ECO:0000259|Pfam:PF01212"
SQ SEQUENCE 360 AA; 40207 MW; 7352D16A109DCA9F CRC64;
MPASDIIDTE LPPRYNFMDD YSEGAHPQIL ESLLRTNTTQ QLSYGTDEFS NEARRLIREK
LNASEDEVAI HFVPSGTSAN LISIASCLRP YEAVMTVESG HIVSKEAGAI EATGHKMILV
PGVNGKMTPK NLERVFQQNQ FFPHMAKPRL VYISNATELG TIYTKAELSA LSAVCKRLGL
LILVDGARLG VALSAKNNDL TLRDMVDLTD IFWIGGTKMG ALLGEAIVVK QHLADGFVFH
LKQHGALLAK SRVMGIQFVE LFRTHLFFDL ATHANDMAAK ISANFEKLGY PLAAQTETNQ
VFAILPDRLV RRLQDRFGFY IWEKREDGHA VVRIVTSWAT DALQVDKFNS WVQQWTELDV
//
