ID M7SF23_EUTLA Unreviewed; 523 AA.
AC M7SF23;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Putative aromatic-l-amino-acid decarboxylase protein {ECO:0000313|EMBL:EMR62818.1};
GN ORFNames=UCREL1_10234 {ECO:0000313|EMBL:EMR62818.1};
OS Eutypa lata (strain UCR-EL1) (Grapevine dieback disease fungus) (Eutypa
OS armeniacae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Diatrypaceae; Eutypa.
OX NCBI_TaxID=1287681 {ECO:0000313|EMBL:EMR62818.1, ECO:0000313|Proteomes:UP000012174};
RN [1] {ECO:0000313|Proteomes:UP000012174}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCR-EL1 {ECO:0000313|Proteomes:UP000012174};
RX PubMed=23723393; DOI=10.1128/genomeA.00228-13;
RA Blanco-Ulate B., Rolshausen P.E., Cantu D.;
RT "Draft genome sequence of the grapevine dieback fungus Eutypa lata UCR-
RT EL1.";
RL Genome Announc. 1:E0022813-E0022813(2013).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR602129-50, ECO:0000256|RuleBase:RU000382};
CC -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC {ECO:0000256|ARBA:ARBA00009533, ECO:0000256|RuleBase:RU000382}.
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DR EMBL; KB707370; EMR62818.1; -; Genomic_DNA.
DR RefSeq; XP_007798073.1; XM_007799882.1.
DR AlphaFoldDB; M7SF23; -.
DR STRING; 1287681.M7SF23; -.
DR KEGG; ela:UCREL1_10234; -.
DR eggNOG; KOG0628; Eukaryota.
DR HOGENOM; CLU_011856_3_1_1; -.
DR OMA; NPGFNWS; -.
DR OrthoDB; 47798at2759; -.
DR Proteomes; UP000012174; Unassembled WGS sequence.
DR GO; GO:0016831; F:carboxy-lyase activity; IEA:InterPro.
DR GO; GO:0030170; F:pyridoxal phosphate binding; 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; 1.20.1340.10; dopa decarboxylase, N-terminal domain; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR010977; Aromatic_deC.
DR InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR InterPro; IPR021115; Pyridoxal-P_BS.
DR PANTHER; PTHR11999:SF70; AROMATIC-L-AMINO-ACID DECARBOXYLASE; 1.
DR PANTHER; PTHR11999; GROUP II PYRIDOXAL-5-PHOSPHATE DECARBOXYLASE; 1.
DR Pfam; PF00282; Pyridoxal_deC; 1.
DR PRINTS; PR00800; YHDCRBOXLASE.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00392; DDC_GAD_HDC_YDC; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000382};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW ECO:0000256|RuleBase:RU000382};
KW Reference proteome {ECO:0000313|Proteomes:UP000012174}.
FT MOD_RES 330
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 523 AA; 56627 MW; 142C7E6A30A1606A CRC64;
MDSKQFKEAA ISSIDDIVNY YETIEERRVA STVEPGYLRK LLPDEAPQDG EAWADIQKDI
EAKILPGITH WQSPNFAAWF PSSSSYPAML GEMYSTALTG AAFNWICSPA VTELETIVLD
WLARAFGLPE CYLSTGPTNG GGVIHGTASE AIATVIVAAR DKYLREATSH IAADDEEGRE
DAWAERRGRL VALGSAATHS ATKKGAQIAG VRYRSVPVHA ADGYKMTGAS LRTTILELRA
RGLEPFFLTA TMGTTDTCAV DDMDSIADVL AELGPAAGGG GGGGGPHGGE VWVHVDAAYA
GVALLCPEHR GLVGERALGR FHSFNTNLHK WLLVNFDCSV LYVRDRRPLV DALSVTLPIL
RNRHTDAGLV TDYRDWQIPF GRRFRSLKVW FVVRTYGVRG LQAHIRKHVG FAEAFAGLLE
GRPDLFEIVT GPRFALTVFK LKGGGGGGGG GGEGASTTLE EQNALTKKAY ELILAEGKIF
LSSTVVGGVY AIRHNPATPF VEERHVREHF EIFVEAAEKV LSQ
//
