ID Q0CJX9_ASPTN Unreviewed; 385 AA.
AC Q0CJX9;
DT 17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 17-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=Tyrosine decarboxylase {ECO:0008006|Google:ProtNLM};
GN ORFNames=ATEG_06005 {ECO:0000313|EMBL:EAU33766.1};
OS Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=341663 {ECO:0000313|EMBL:EAU33766.1, ECO:0000313|Proteomes:UP000007963};
RN [1] {ECO:0000313|Proteomes:UP000007963}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIH 2624 / FGSC A1156 {ECO:0000313|Proteomes:UP000007963};
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA Nierman W.C., Milne T., Madden K.;
RT "Annotation of the Aspergillus terreus NIH2624 genome.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|PIRSR:PIRSR602129-50,
CC ECO:0000256|RuleBase:RU000382};
CC -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC {ECO:0000256|RuleBase:RU000382}.
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DR EMBL; CH476601; EAU33766.1; -; Genomic_DNA.
DR RefSeq; XP_001215183.1; XM_001215183.1.
DR AlphaFoldDB; Q0CJX9; -.
DR STRING; 341663.Q0CJX9; -.
DR EnsemblFungi; EAU33766; EAU33766; ATEG_06005.
DR GeneID; 4321580; -.
DR VEuPathDB; FungiDB:ATEG_06005; -.
DR eggNOG; KOG0629; Eukaryota.
DR HOGENOM; CLU_011856_6_0_1; -.
DR OMA; RRDKEFP; -.
DR OrthoDB; 51460at2759; -.
DR Proteomes; UP000007963; Unassembled WGS sequence.
DR GO; GO:0016830; F:carbon-carbon lyase activity; IEA:InterPro.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR PANTHER; PTHR11999:SF165; DECARBOXYLASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_2G04980)-RELATED; 1.
DR PANTHER; PTHR11999; GROUP II PYRIDOXAL-5-PHOSPHATE DECARBOXYLASE; 1.
DR Pfam; PF00282; Pyridoxal_deC; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 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:UP000007963}.
FT MOD_RES 325
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 385 AA; 40829 MW; 294E20531862AFA0 CRC64;
MEIKDIDATA MAHGHLQEEL WRTAQGPWKS GVLPTAENLA RARASLPDRL SQDGVGFEAS
KNHILDDIVP AFNGSSISPN YYGFVTGGVT PAALFADNVV SAYDQNVQVH LPEHSIATDV
ESNALGLVVD LLDLDRGAWH HGTFTTGATA SNILGLACGR EYILRVAGRK KGVAFNSVGE
LGLFEAMQAA GLSGVQVLST LPHSSVAKAA GILGIGRSNV KNVCLHDNPL KFDMGKLEDE
LQKSDRATII AVSCGEVNTG QFSTGGMQQM QALRKLCDKY GAWLHVDGAF GVFARVLGNN
EEFSSIRKGS DGMELADSIT GDGHKLLNVP YDCGFFLCRH PDEANNVFQN ANAAYLTGGS
GAQPSIPSPL NIGIENSRRP GIAAL
//
