ID R0GWD0_9BRAS Unreviewed; 542 AA.
AC R0GWD0;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE RecName: Full=Serine decarboxylase {ECO:0008006|Google:ProtNLM};
DE Flags: Fragment;
GN ORFNames=CARUB_v10008789mg {ECO:0000313|EMBL:EOA40096.1};
OS Capsella rubella.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Capsella.
OX NCBI_TaxID=81985 {ECO:0000313|EMBL:EOA40096.1, ECO:0000313|Proteomes:UP000029121};
RN [1] {ECO:0000313|Proteomes:UP000029121}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Monte Gargano {ECO:0000313|Proteomes:UP000029121};
RX PubMed=23749190; DOI=10.1038/ng.2669;
RA Slotte T., Hazzouri K.M., Agren J.A., Koenig D., Maumus F., Guo Y.L.,
RA Steige K., Platts A.E., Escobar J.S., Newman L.K., Wang W., Mandakova T.,
RA Vello E., Smith L.M., Henz S.R., Steffen J., Takuno S., Brandvain Y.,
RA Coop G., Andolfatto P., Hu T.T., Blanchette M., Clark R.M., Quesneville H.,
RA Nordborg M., Gaut B.S., Lysak M.A., Jenkins J., Grimwood J., Chapman J.,
RA Prochnik S., Shu S., Rokhsar D., Schmutz J., Weigel D., Wright S.I.;
RT "The Capsella rubella genome and the genomic consequences of rapid mating
RT system evolution.";
RL Nat. Genet. 45:831-835(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; KB870805; EOA40096.1; -; Genomic_DNA.
DR RefSeq; XP_006307198.1; XM_006307136.1.
DR AlphaFoldDB; R0GWD0; -.
DR STRING; 81985.R0GWD0; -.
DR GeneID; 17897012; -.
DR KEGG; crb:17897012; -.
DR eggNOG; KOG0629; Eukaryota.
DR OrthoDB; 750275at2759; -.
DR Proteomes; UP000029121; 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: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:UP000029121}.
FT REGION 87..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 374
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EOA40096.1"
SQ SEQUENCE 542 AA; 61526 MW; 3EEF03560E291ED5 CRC64;
NQFCLFLLYK LKKINQRRSV SLSLSHHFHR FSSNHSLFFF FSQIYRFFRF LFVYLNAMVG
SFESDQILSM TNLNDILTST VIAEPLPSPV TNGTGDEENL KKPNGAGGRG GGGGDREMVL
GRNIHTTSLA VTEPEVNDEF TGDKEAYMAS VLARYRKTLV ERTKYHLGYP YNLDFDYGAL
GQLQHFSINN LGDPFIESNY GVHSRPFEVG VLDWFARLWE IERDDYWGYI TNCGTEGNLH
GILVGREMFP DGILYASRES HYSVFKAARM YRMECEKVDT LISGEIDCDD FRKKLLANKD
KPAILNVNIG TTVKGAVDDL DLVIKTLEEC GFSHDRFYIH CDGALFGLMM PFVKRAPKVT
FNKPIGSVSV SGHKFVGCPM PCGVQITRME HIKVLSNNVE YLASRDATIM GSRNGHAPLF
LWYTLNRKGY KGFQKEVQKC LRNAHYLKDK LREAGISAML NELSSTVVFE RPKDEEFVRR
WQLACQGDIA HVVVMPSVTI EKLDDFLKDL VKHRLVWYED GTQPPCLASE VGTNNCICPA
HK
//