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Database: UniProt
Entry: A0A3B6TI96_WHEAT
LinkDB: A0A3B6TI96_WHEAT
Original site: A0A3B6TI96_WHEAT 
ID   A0A3B6TI96_WHEAT        Unreviewed;       510 AA.
AC   A0A3B6TI96;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Aromatic-L-amino-acid decarboxylase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=CFC21_110312 {ECO:0000313|EMBL:KAF7110164.1};
OS   Triticum aestivum (Wheat).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX   NCBI_TaxID=4565 {ECO:0000313|EnsemblPlants:TraesCS7D02G383500.1.cds1};
RN   [1] {ECO:0000313|EMBL:KAF7110164.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Leaf {ECO:0000313|EMBL:KAF7110164.1};
RX   PubMed=29069494;
RA   Zimin A.V., Puiu D., Hall R., Kingan S., Clavijo B.J., Salzberg S.L.;
RT   "The first near-complete assembly of the hexaploid bread wheat genome,
RT   Triticum aestivum.";
RL   Gigascience 6:1-7(2017).
RN   [2] {ECO:0000313|EnsemblPlants:TraesCS7D02G383500.1.cds1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Chinese Spring
RC   {ECO:0000313|EnsemblPlants:TraesCS7D02G383500.1.cds1};
RX   PubMed=30115783; DOI=10.1126/science.aar7191;
RG   International wheat genome sequencing consortium (IWGSC);
RT   "Shifting the limits in wheat research and breeding using a fully annotated
RT   reference genome.";
RL   Science 361:EAAR7191-EAAR7191(2018).
RN   [3] {ECO:0000313|EnsemblPlants:TraesCS7D02G383500.1.cds1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (OCT-2018) to UniProtKB.
RN   [4] {ECO:0000313|EMBL:KAF7110164.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Leaf {ECO:0000313|EMBL:KAF7110164.1};
RA   Zimin A.V., Puiu D., Shumante A., Alonge M., Salzberg S.L.;
RT   "The second near-complete assembly of the hexaploid bread wheat (Triticum
RT   aestivum) genome.";
RL   Submitted (MAR-2020) to the EMBL/GenBank/DDBJ databases.
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; CM022231; KAF7110164.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3B6TI96; -.
DR   SMR; A0A3B6TI96; -.
DR   STRING; 4565.A0A3B6TI96; -.
DR   EnsemblPlants; TraesCS7D02G383500.1; TraesCS7D02G383500.1.cds1; TraesCS7D02G383500.
DR   Gramene; TraesCAD_scaffold_103514_01G000100.1; TraesCAD_scaffold_103514_01G000100.1; TraesCAD_scaffold_103514_01G000100.
DR   Gramene; TraesCLE_scaffold_133293_01G000100.1; TraesCLE_scaffold_133293_01G000100.1; TraesCLE_scaffold_133293_01G000100.
DR   Gramene; TraesCS7D02G383500.1; TraesCS7D02G383500.1.cds1; TraesCS7D02G383500.
DR   Gramene; TraesCS7D03G0902600.1; TraesCS7D03G0902600.1.CDS1; TraesCS7D03G0902600.
DR   Gramene; TraesKAR7D01G0359460.1; cds.TraesKAR7D01G0359460.1; TraesKAR7D01G0359460.
DR   Gramene; TraesPAR_scaffold_110987_01G000100.1; TraesPAR_scaffold_110987_01G000100.1; TraesPAR_scaffold_110987_01G000100.
DR   Gramene; TraesROB_scaffold_108675_01G000100.1; TraesROB_scaffold_108675_01G000100.1; TraesROB_scaffold_108675_01G000100.
DR   Gramene; TraesWEE_scaffold_118708_01G000100.1; TraesWEE_scaffold_118708_01G000100.1; TraesWEE_scaffold_118708_01G000100.
DR   OMA; IWSAIRM; -.
DR   OrthoDB; 467615at2759; -.
DR   Proteomes; UP000019116; Chromosome 7D.
DR   Proteomes; UP000815260; Chromosome 7D.
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   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:SF163; 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   Decarboxylase {ECO:0000256|ARBA:ARBA00022793};
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:UP000019116}.
FT   MOD_RES         329
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   510 AA;  55579 MW;  81679385A340C344 CRC64;
     MGSLDTNPMS FSALPSDKAA FEPLNPEDVR AYLHKAVDFI SDYYTNIESM PVLPNVKPGY
     LQDELSASPP TYSAPFDVTM KELRTSVVPG MTHWASPNFF AFFPSTNSAA AIAGDLIASA
     MNTVGFTWQA SPAATEMEVL ALDWLAQLLR LPTTFMNRTS TGRGTGGGVI LGTTSEAMLV
     TLVAARDAAL RRSGSVGVSN ISRLVVYAAD QTHSTFFKAC RLAGFDPANI RSIPTGPETN
     YGLDPAKLLE VMQADANAGL VPTYVCATVG TTSSNAVDPV GAVADVAAMF NAWVHVDAAY
     AGSACICPEF RHHLDGVERV DSISMSPHKW LLTCLDCTCL YVRDAHRLSD SLETNPEYLK
     NDATDSGEVT DLKDMQVGVG RRFRGLKLWM VMRTYGTAKL QEHIRSDVAM AKMFEDFVRA
     DERFEVVVPR NFALVCFRIK ASGAMTEEDA NEANRVLMDN LNKTGKAYLA HTVVGDKFVL
     RFAVGSSLQE ERHIRSAWDL IKKTTSSIMD
//
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