ID B8M8B3_TALSN Unreviewed; 448 AA.
AC B8M8B3;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 13-SEP-2023, entry version 57.
DE SubName: Full=L-allo-threonine aldolase, putative {ECO:0000313|EMBL:EED20426.1};
GN ORFNames=TSTA_036510 {ECO:0000313|EMBL:EED20426.1};
OS Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL
OS 1006) (Penicillium stipitatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=441959 {ECO:0000313|EMBL:EED20426.1, ECO:0000313|Proteomes:UP000001745};
RN [1] {ECO:0000313|Proteomes:UP000001745}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006
RC {ECO:0000313|Proteomes:UP000001745};
RX PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT (ATCC10500).";
RL Genome Announc. 3:E0155914-E0155914(2015).
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; EQ962654; EED20426.1; -; Genomic_DNA.
DR RefSeq; XP_002480860.1; XM_002480815.1.
DR AlphaFoldDB; B8M8B3; -.
DR STRING; 441959.B8M8B3; -.
DR GeneID; 8101922; -.
DR VEuPathDB; FungiDB:TSTA_036510; -.
DR eggNOG; KOG1368; Eukaryota.
DR HOGENOM; CLU_029381_1_1_1; -.
DR InParanoid; B8M8B3; -.
DR OMA; RAHVHCW; -.
DR OrthoDB; 178754at2759; -.
DR PhylomeDB; B8M8B3; -.
DR Proteomes; UP000001745; 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 SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000001745}.
FT DOMAIN 89..381
FT /note="Aromatic amino acid beta-eliminating lyase/threonine
FT aldolase"
FT /evidence="ECO:0000259|Pfam:PF01212"
FT REGION 1..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..24
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..40
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 448 AA; 49381 MW; B0AA989590B0FA4D CRC64;
MAPGIREFAE VEVPEQRIEV SKSSKLDASK PLNQNEYNKG GREEMNGWSD KTSAAGKNSN
TTDDDDETPV FTMPSMHKLR EAQRRVERDF RSDTVTVPTV NMIQAMIESS FQDDMYDATG
DESVNRLQQR LIELTGKEAA MWALSGTMGN QICLRTHLTQ PPHTVLLDYR AHVHCWETGA
MPVMSQASVT QVHPKNGLHL TVDDVKKHII ADGNIHFPPT RVVSLENSLS GTILPLKDAK
EISEFVRNFP VEEGEKPIAM HLDGARLFDA VAAEGVDLKD YCACFDSISI CLAKGLGAPM
GSVIVGSKKF IHRARLFRKM FGGGTRQPGM MAAAALSALE YTMPLLPKVH ALTKRTADTL
RQAGYKISLP VQTNMIVLDL EEVGIPPAAF VAYAKRAGVT VFPTGRLVFH HQITPEAAAR
LVEAMRLLME DKKAGKQLEN HKVTGGYM
//
