ID I1HBR6_BRADI Unreviewed; 543 AA.
AC I1HBR6;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=Tyrosine decarboxylase {ECO:0008006|Google:ProtNLM};
GN Name=100833161 {ECO:0000313|EnsemblPlants:KQK02568};
GN ORFNames=BRADI_2g02360v3 {ECO:0000313|EMBL:KQK02568.1};
OS Brachypodium distachyon (Purple false brome) (Trachynia distachya).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Stipodae; Brachypodieae; Brachypodium.
OX NCBI_TaxID=15368 {ECO:0000313|EMBL:KQK02568.1};
RN [1] {ECO:0000313|EMBL:KQK02568.1, ECO:0000313|EnsemblPlants:KQK02568}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bd21 {ECO:0000313|EMBL:KQK02568.1,
RC ECO:0000313|EnsemblPlants:KQK02568};
RX PubMed=20148030; DOI=10.1038/nature08747;
RG International Brachypodium Initiative;
RT "Genome sequencing and analysis of the model grass Brachypodium
RT distachyon.";
RL Nature 463:763-768(2010).
RN [2] {ECO:0000313|EMBL:KQK02568.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Bd21 {ECO:0000313|EMBL:KQK02568.1};
RG The International Brachypodium Initiative;
RA Lucas S., Harmon-Smith M., Lail K., Tice H., Grimwood J., Bruce D.,
RA Barry K., Shu S., Lindquist E., Wang M., Pitluck S., Vogel J.P.,
RA Garvin D.F., Mockler T.C., Schmutz J., Rokhsar D., Bevan M.W.;
RT "WGS assembly of Brachypodium distachyon.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblPlants:KQK02568}
RP IDENTIFICATION.
RC STRAIN=cv. Bd21 {ECO:0000313|EnsemblPlants:KQK02568};
RG EnsemblPlants;
RL Submitted (AUG-2018) to UniProtKB.
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; CM000881; KQK02568.1; -; Genomic_DNA.
DR RefSeq; XP_003565304.1; XM_003565256.1.
DR AlphaFoldDB; I1HBR6; -.
DR EnsemblPlants; KQK02568; KQK02568; BRADI_2g02360v3.
DR GeneID; 100833161; -.
DR Gramene; KQK02568; KQK02568; BRADI_2g02360v3.
DR KEGG; bdi:100833161; -.
DR eggNOG; KOG0628; Eukaryota.
DR HOGENOM; CLU_011856_3_1_1; -.
DR InParanoid; I1HBR6; -.
DR OMA; FITHTEV; -.
DR OrthoDB; 349065at2759; -.
DR Proteomes; UP000008810; Chromosome 2.
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 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|PIRSR:PIRSR602129-50,
KW ECO:0000256|RuleBase:RU000382};
KW Reference proteome {ECO:0000313|Proteomes:UP000008810}.
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..31
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 349
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 543 AA; 58361 MW; E74D0015C1F8A103 CRC64;
MAPASSKLHA ITDDKTQQQN SSCPAASNGA IEPSNAKCAA SSNHLLDADE FRRQGHKVID
FIADYYAGIA DYPVHPSVTP GFLLNQLPAD PPSRPEDHPD GAFGPALQDV RDVILPGMTH
WQSPRHFAHF PASSSVAGVL GEALAAGINA VPFTWAASPA AAELEMVAVD WLGKALHLPE
SLLFSGAGGG TLLGTSCEAI LCALVAARDR KLADIGTDRI GDLVVYGSDQ THFALRKAAR
IAGIRHDRCR ELQTCLADMF ALSPAALSAA MDADAGAGLV PLFLCATVGT TQTTAVDQVG
ALCAAAAPHG VWVHVDAAYA GSALVCPELA RDAIDGIEVV DSFSMNAHKW LLANTDCCAL
WVKQPKLLVV SLGTQNEELI LRDAAAEGHD VVDYKDWAIT LTRRFRALKL WLVFRCYGVE
GLREHIRAHV RMAALFEGLV KDDPRFEVVT ERRFALVCFR LRAPDQLMDE GNEKKKTTAA
ANELNRRLLR EVNGVALGPY MSAAVVGGIY ILRCAVGSTL TEERHVRQAW EVVQERATSI
LRG
//
