ID A0A2I0LD57_PUNGR Unreviewed; 364 AA.
AC A0A2I0LD57;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Tyrosine decarboxylase 1-like {ECO:0008006|Google:ProtNLM};
GN ORFNames=CRG98_000988 {ECO:0000313|EMBL:PKI78611.1};
OS Punica granatum (Pomegranate).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Myrtales; Lythraceae; Punica.
OX NCBI_TaxID=22663 {ECO:0000313|EMBL:PKI78611.1, ECO:0000313|Proteomes:UP000233551};
RN [1] {ECO:0000313|EMBL:PKI78611.1, ECO:0000313|Proteomes:UP000233551}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. AG2017 {ECO:0000313|Proteomes:UP000233551};
RC TISSUE=Leaf {ECO:0000313|EMBL:PKI78611.1};
RA Akparov Z., Amiraslanov A., Hajiyeva S., Abbasov M., Kaur K., Hamwieh A.,
RA Solovyev V., Salamov A., Braich B., Kosarev P., Mahmoud A., Hajiyev E.,
RA Babayeva S., Izzatullayeva V., Mammadov A., Mammadov A., Sharifova S.,
RA Ojaghi J., Eynullazada K., Bayramov B., Abdulazimova A., Shahmuradov I.;
RT "De-novo sequencing of pomegranate (Punica granatum L.) genome.";
RL Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|RuleBase:RU000382};
CC -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC {ECO:0000256|RuleBase:RU000382}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PKI78611.1}.
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DR EMBL; PGOL01000038; PKI78611.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2I0LD57; -.
DR STRING; 22663.A0A2I0LD57; -.
DR Proteomes; UP000233551; 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 GO; GO:1901564; P:organonitrogen compound metabolic process; IEA:UniProt.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
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 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 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|RuleBase:RU000382};
KW Reference proteome {ECO:0000313|Proteomes:UP000233551}.
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 364 AA; 39763 MW; 9310C79DBB0B55C1 CRC64;
MGSLKSEEAL ESNCTNPLDP DEFRRQGHMI IDFLADYYKT IEDHPSNAST AGILGEILCS
GFGVVGFSWV SSPAATELES LVMEWLGEML KLPRPFLFSG GGGGVIHGNT CEAIICTLAA
ARDKVLREIG EENITKLVVY CSDQTHCSFK KAAQVVGINA QNIRAINTTK VTEFGMCPSS
LKQAIARDIK EGLVPLFNAH KWLLTGLDCC CLWVKDSAAL RQALSSQAEC LRNKPAESKK
DDRFEVVCKR NFALVCFRIS PSALGKQVLS TGYLSGDASI DNDNIKDGHT VEEPVTTTAN
INDVNKRLLE EINGTGRVFM THAVVGGVYA IRFAVGATLV QERHVRFAWK LVQGHADAIL
RDRP
//
