ID   A0A0E0K0T4_ORYPU        Unreviewed;       481 AA.
AC   A0A0E0K0T4;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   RecName: Full=Serine decarboxylase {ECO:0008006|Google:ProtNLM};
OS   Oryza punctata (Red rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=4537 {ECO:0000313|EnsemblPlants:OPUNC02G17530.1};
RN   [1] {ECO:0000313|EnsemblPlants:OPUNC02G17530.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Wing R.;
RT   "Oryza genome evolution.";
RL   Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblPlants:OPUNC02G17530.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (APR-2015) 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   AlphaFoldDB; A0A0E0K0T4; -.
DR   STRING; 4537.A0A0E0K0T4; -.
DR   EnsemblPlants; OPUNC02G17530.1; OPUNC02G17530.1; OPUNC02G17530.
DR   Gramene; OPUNC02G17530.1; OPUNC02G17530.1; OPUNC02G17530.
DR   eggNOG; KOG0629; Eukaryota.
DR   HOGENOM; CLU_028929_0_1_1; -.
DR   OMA; ASRETHY; -.
DR   Proteomes; UP000026962; Chromosome 2.
DR   GO; GO:0016831; F:carboxy-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   InterPro; IPR021115; Pyridoxal-P_BS.
DR   PANTHER; PTHR46101; -; 1.
DR   PANTHER; PTHR46101:SF2; SERINE DECARBOXYLASE; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00392; DDC_GAD_HDC_YDC; 1.
PE   3: Inferred from homology;
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:UP000026962}.
FT   MOD_RES         311
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   481 AA;  53672 MW;  641425B74E5E3342 CRC64;
     MVGSVGNDLV DLGAAAAVNG VGKGVMHPEA AAVAAMEVES PPAEEGGEGS PTRREIVLGR
     NVHTASFAVK EPDADDEETG EREAAMASVL ALYRRNLVER TKHHLGYPYN LDFDYGALGQ
     LQHFSINNLG DPFIESNYGV HSRQFEVGVL DWFARIWELE KNEYWGYITN CGTEGNLHGI
     LVGREVFPDG ILYASRESHY SVFKAARMYR MDCVKVDTLI SGEIDCADFQ RKLLLNRDKP
     AIINVNIGTT VKGAVDDLDL VIKTLEEGGF KDRFYIHCDG ALFGLMIPFV KKAPKVSFKK
     PIGSVSVSGH KFVGCPMPCG VQITRLEHIN RLSSNVEYLA SRDATIMGSR NGHAPIFLWY
     TLNRKGYRGF QKEVQKCLRN AHYLKDRLKE AGISAMLNEL SSTVVFERPK DEEFVRRWQL
     ACEGNIAHVV VMPSVTIDKL DYFLNELREK RATWYQDGSC QPPCIAKDVG EENCLCSLHK
     K
//