ID   A0A022RJM5_ERYGU        Unreviewed;       300 AA.
AC   A0A022RJM5;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=Serine decarboxylase {ECO:0008006|Google:ProtNLM};
DE   Flags: Fragment;
GN   ORFNames=MIMGU_mgv1a026369mg {ECO:0000313|EMBL:EYU40386.1};
OS   Erythranthe guttata (Yellow monkey flower) (Mimulus guttatus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Lamiales; Phrymaceae; Erythranthe.
OX   NCBI_TaxID=4155 {ECO:0000313|EMBL:EYU40386.1, ECO:0000313|Proteomes:UP000030748};
RN   [1] {ECO:0000313|EMBL:EYU40386.1, ECO:0000313|Proteomes:UP000030748}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. DUN x IM62 {ECO:0000313|Proteomes:UP000030748};
RX   PubMed=24225854; DOI=10.1073/pnas.1319032110;
RA   Hellsten U., Wright K.M., Jenkins J., Shu S., Yuan Y., Wessler S.R.,
RA   Schmutz J., Willis J.H., Rokhsar D.S.;
RT   "Fine-scale variation in meiotic recombination in Mimulus inferred from
RT   population shotgun sequencing.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:19478-19482(2013).
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; KI630402; EYU40386.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A022RJM5; -.
DR   STRING; 4155.A0A022RJM5; -.
DR   Proteomes; UP000030748; Unassembled WGS sequence.
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:1901566; P:organonitrogen compound biosynthetic 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:SF9; HISTIDINE 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:UP000030748}.
FT   MOD_RES         129
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EYU40386.1"
SQ   SEQUENCE   300 AA;  33784 MW;  3E4E7E0B2C13F166 CRC64;
     RDLLPDGILY ASKESHYSIF KASRMYRMEC QIIDTLITGE INCTELREKL FLNKDKPAIV
     NVNIGTTFKG GVDNLDLIIK TLEECGFSHD RFYIHCDAAL NGLISPFLEY GPKLSFKKPI
     RSISVSAHKL LGSSIPCGVL MTRKGRITNN LSENVEYIDT LDTTISGSRN GHAPIFIWYG
     LKMKGRSGLH TEVNKCLTNA KYLRDGFKNA GISAMLNESS IVVVFERPLS REFIDYWQLS
     LLEKMAHVVV MPHVTVKMLD DFLDDLVQNR EIWYGNGKVQ PLCLAEEIGV SNCACLVHMN
//