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Database: UniProt
Entry: A0A3B6IY51_WHEAT
LinkDB: A0A3B6IY51_WHEAT
Original site: A0A3B6IY51_WHEAT 
ID   A0A3B6IY51_WHEAT        Unreviewed;       515 AA.
AC   A0A3B6IY51;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=Aromatic-L-amino-acid decarboxylase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=CFC21_059830 {ECO:0000313|EMBL:KAF7051606.1};
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:TraesCS4B02G385700.1.cds1};
RN   [1] {ECO:0000313|EMBL:KAF7051606.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Leaf {ECO:0000313|EMBL:KAF7051606.1};
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:TraesCS4B02G385700.1.cds1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Chinese Spring
RC   {ECO:0000313|EnsemblPlants:TraesCS4B02G385700.1.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:TraesCS4B02G385700.1.cds1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (OCT-2018) to UniProtKB.
RN   [4] {ECO:0000313|EMBL:KAF7051606.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Leaf {ECO:0000313|EMBL:KAF7051606.1};
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; CM022221; KAF7051606.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3B6IY51; -.
DR   SMR; A0A3B6IY51; -.
DR   STRING; 4565.A0A3B6IY51; -.
DR   EnsemblPlants; TraesCS4B02G385700.1; TraesCS4B02G385700.1.cds1; TraesCS4B02G385700.
DR   Gramene; TraesCS4B02G385700.1; TraesCS4B02G385700.1.cds1; TraesCS4B02G385700.
DR   Gramene; TraesCS4B03G0985700.1; TraesCS4B03G0985700.1.CDS1; TraesCS4B03G0985700.
DR   Proteomes; UP000019116; Chromosome 4B.
DR   Proteomes; UP000815260; Chromosome 4B.
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   CDD; cd06450; DOPA_deC_like; 1.
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:SF93; 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         328
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   515 AA;  56801 MW;  1E419039B0CC5C96 CRC64;
     MDPAAFASPS FDACVQGSSF QPLNPEDVRA YLYKAADFIM DYYTSVESMP VLPDVKPGYL
     RDELRASPPE HSAPFDVTMK ELRTSVVRGM THWASPSFFA FFPSTNSAAA IAGELIASAM
     NTVGFTWQAA PAATEMEVLV LDWLAQLLRL PTSFMNRTSV GRGTGGGVIL GTTSEAMLVT
     LVAARDAALR RIASNGMSYI TRLTVYATGQ THSTFFKACR LAGFDPANLR SIPTEPETDY
     GLDPAKLLEI MQVDFDAGLV PTYICATVGT TSSNAVDPVS TVASVAAMFN AWVHVDAAYA
     GSACICPEFR HHIDGVERVD SISMSPHKWL LTCLDCTCLW VRDTNRLTDA LQTNPEYLKN
     DATESGEVID LKDMQVGVGR RFRGLKLWMV MRTYGTAKLQ QHIRSDVAMA KAFEDLVRAD
     DRFEIVVPRN FALVCFRIRA RGTMTEEATD EVNRVLINRL NISRKAYLAH TVVGNRFVLR
     FAVGSSLQED RHVRSAWELI KKTTAKIIDG EEIVQ
//
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