ID A0A135LSR2_PENPA Unreviewed; 389 AA.
AC A0A135LSR2;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=Aromatic amino acid beta-eliminating lyase/threonine aldolase {ECO:0000313|EMBL:KXG52000.1};
GN ORFNames=PGRI_082840 {ECO:0000313|EMBL:KXG52000.1};
OS Penicillium patulum (Penicillium griseofulvum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=5078 {ECO:0000313|EMBL:KXG52000.1, ECO:0000313|Proteomes:UP000070168};
RN [1] {ECO:0000313|EMBL:KXG52000.1, ECO:0000313|Proteomes:UP000070168}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PG3 {ECO:0000313|EMBL:KXG52000.1,
RC ECO:0000313|Proteomes:UP000070168};
RX PubMed=26729047; DOI=10.1186/s12864-015-2347-x;
RA Banani H., Marcet-Houben M., Ballester A.R., Abbruscato P.,
RA Gonzalez-Candelas L., Gabaldon T., Spadaro D.;
RT "Genome sequencing and secondary metabolism of the postharvest pathogen
RT Penicillium griseofulvum.";
RL BMC Genomics 17:19-19(2016).
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:KXG52000.1}.
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DR EMBL; LHQR01000027; KXG52000.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A135LSR2; -.
DR STRING; 5078.A0A135LSR2; -.
DR OMA; MIDFRSD; -.
DR OrthoDB; 178754at2759; -.
DR Proteomes; UP000070168; Unassembled WGS sequence.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
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 Lyase {ECO:0000313|EMBL:KXG52000.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000070168}.
FT DOMAIN 34..325
FT /note="Aromatic amino acid beta-eliminating lyase/threonine
FT aldolase"
FT /evidence="ECO:0000259|Pfam:PF01212"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 230
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR017617-1"
SQ SEQUENCE 389 AA; 41812 MW; B64974CFBC3A36A1 CRC64;
MSQLSTDAMA HGSAAIGNNK KPTAWHGAGA AEFDLRSDTM TKPTPSMLEA ICQTTLLDDV
FNEDPVTNDL QSYVAEIAKH EASLLVLSGT MGNQVAIRSH LAQPPHSVLC DHRSHIICYE
AGGVSAWTGA TVSPVIPQNG VYLTLEDIKK HAVLSDNIHY CPTKLISLEN TLDGMIMPLA
EVKRIVEWAH AHDIKVHLDG ARLWEAVVAG AGSLPEYTSL FDSVSLCFSK GLGAPIGSII
VGSQEFINKA RWFRKSIGGG ARQTGVIAAA ARVALTETFG TDPKGQTGKL AATHEKAKHV
ANLWTSRGGK LQYPLHTNMV WLDLEASGVG PNDLAEIGQQ KGLKLMGGRV VVHYQVSDEA
IARLEQVFDT ALKGDFKRSE DTSKPYGTK
//
