ID K4BG32_SOLLC Unreviewed; 476 AA.
AC K4BG32;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=Tyrosine decarboxylase {ECO:0008006|Google:ProtNLM};
OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC Solanum subgen. Lycopersicon.
OX NCBI_TaxID=4081 {ECO:0000313|EnsemblPlants:Solyc03g044120.1.1};
RN [1] {ECO:0000313|EnsemblPlants:Solyc03g044120.1.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Heinz 1706 {ECO:0000313|EnsemblPlants:Solyc03g044120.1.1};
RX PubMed=22660326; DOI=10.1038/nature11119;
RG Tomato Genome Consortium;
RT "The tomato genome sequence provides insights into fleshy fruit
RT evolution.";
RL Nature 485:635-641(2012).
RN [2] {ECO:0000313|EnsemblPlants:Solyc03g044120.1.1}
RP IDENTIFICATION.
RC STRAIN=cv. Heinz 1706 {ECO:0000313|EnsemblPlants:Solyc03g044120.1.1};
RG EnsemblPlants;
RL Submitted (JUN-2015) to UniProtKB.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC 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 AlphaFoldDB; K4BG32; -.
DR STRING; 4081.K4BG32; -.
DR PaxDb; 4081-Solyc03g044120-1-1; -.
DR EnsemblPlants; Solyc03g044120.1.1; Solyc03g044120.1.1; Solyc03g044120.1.
DR Gramene; Solyc03g044120.1.1; Solyc03g044120.1.1; Solyc03g044120.1.
DR eggNOG; KOG0628; Eukaryota.
DR HOGENOM; CLU_011856_3_1_1; -.
DR InParanoid; K4BG32; -.
DR OMA; ETIVCDW; -.
DR PhylomeDB; K4BG32; -.
DR Proteomes; UP000004994; Chromosome 3.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016831; F:carboxy-lyase activity; IBA:GO_Central.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
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 PANTHER; PTHR11999; GROUP II PYRIDOXAL-5-PHOSPHATE DECARBOXYLASE; 1.
DR PANTHER; PTHR11999:SF96; TYROSINE DECARBOXYLASE; 1.
DR Pfam; PF00282; Pyridoxal_deC; 1.
DR PRINTS; PR00800; YHDCRBOXLASE.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Decarboxylase {ECO:0000256|ARBA:ARBA00022793};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000382};
KW Pyridoxal phosphate {ECO:0000256|RuleBase:RU000382};
KW Reference proteome {ECO:0000313|Proteomes:UP000004994}.
SQ SEQUENCE 476 AA; 53231 MW; 5E248F83C8BD01D6 CRC64;
MGTLNINHEL DDQIFNTINP LDPEEFRRQG HKIVNFLADY YQNIEQYPVC SQVNPGYLQN
IVPNSAPNNP ESLDKILKDV QNDIIPGLTH WQSPNFFAYF PSSGSTVGFV GEMLSVGFNV
VGFNWISSPA ATELESIVMD WFGKMLNLPN CFLFASGGGG VLQGTTCEAI LCTIVAARDQ
MLRKISRENF GKLVVYASGQ THFSLKKSAH IAGIDPGNFR VIPTIKAKEY TLCPKSLRLA
ILNDLKEGNV PLFLCATIGT TSTTSVDPLR LLCDISKEFG IWVHVDAAYV GSACICPEFQ
VFLDGVENAN SFSLNDPSAL TNALSTNLEF LRNKATELNQ VIDYKDWQIA LSRRFRALKL
WLVLRSYGVT NLRNLIRSHV NMTKHFEGLI AMDKRFEIFV PRKFAMVCFR ISPLVLSQVS
IKFDDEKEVN MFNTKLLESI NSCSKLYLTH GIVGGTYIIR FAIGASLTHY RHVDIA
//
