ID   SDC1_ORYSJ              Reviewed;         482 AA.
AC   Q6ESZ9; Q0E0L0;
DT   09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=Serine decarboxylase 1;
DE            EC=4.1.1.-;
GN   Name=SDC1; OrderedLocusNames=Os02g0541325, LOC_Os02g33710;
GN   ORFNames=OJ1298_H07.24, OsJ_07054, P0472F10.2;
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA   Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA   Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA   Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA   Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA   Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA   Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA   Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA   Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA   Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA   Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA   Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA   Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA   Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA   McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT   "The genomes of Oryza sativa: a history of duplications.";
RL   PLoS Biol. 3:266-281(2005).
CC   -!- FUNCTION: Catalyzes the biosynthesis of ethanolamine from serine.
CC       Decarboxylation of free serine is the major source of ethanolamine
CC       production in plants and ethanolamine metabolism is crucial for the
CC       synthesis of choline, phosphatidylethanolamine (PE) and
CC       phosphatidylcholine (PC), and thus for plant growth (By similarity).
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + L-serine = CO2 + ethanolamine; Xref=Rhea:RHEA:45824,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:33384,
CC         ChEBI:CHEBI:57603;
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250};
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAF08978.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AP004847; BAD28070.1; -; Genomic_DNA.
DR   EMBL; AP004877; BAD28221.1; -; Genomic_DNA.
DR   EMBL; AP008208; BAF08978.2; ALT_SEQ; Genomic_DNA.
DR   EMBL; AP014958; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CM000139; EAZ23358.1; -; Genomic_DNA.
DR   RefSeq; XP_015626683.1; XM_015771197.1.
DR   AlphaFoldDB; Q6ESZ9; -.
DR   SMR; Q6ESZ9; -.
DR   STRING; 4530.OS02T0541325-00; -.
DR   PaxDb; Q6ESZ9; -.
DR   PRIDE; Q6ESZ9; -.
DR   GeneID; 4329593; -.
DR   KEGG; osa:4329593; -.
DR   eggNOG; KOG0629; Eukaryota.
DR   HOGENOM; CLU_028929_0_1_1; -.
DR   InParanoid; Q6ESZ9; -.
DR   OrthoDB; 810772at2759; -.
DR   PlantReactome; R-OSA-1119556; Choline biosynthesis I.
DR   Proteomes; UP000000763; Chromosome 2.
DR   Proteomes; UP000007752; Chromosome 2.
DR   Proteomes; UP000059680; Chromosome 2.
DR   Genevisible; Q6ESZ9; OS.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0102705; F:serine decarboxylase activity; IEA:RHEA.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR   GO; GO:0006807; P:nitrogen compound metabolic process; IEA:UniProt.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 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   Pfam; PF00282; Pyridoxal_deC; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   PROSITE; PS00392; DDC_GAD_HDC_YDC; 1.
PE   3: Inferred from homology;
KW   Decarboxylase; Lyase; Pyridoxal phosphate; Reference proteome.
FT   CHAIN           1..482
FT                   /note="Serine decarboxylase 1"
FT                   /id="PRO_0000429508"
FT   REGION          36..55
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        40..54
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         200
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         312
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   482 AA;  53874 MW;  466FD9FE63C75D08 CRC64;
     MVGSVGNGLV DLGGAAVAVN GVGKGMRPEA VAVAMEVESP PRPAEEEGEG SPTRREIVLG
     RNVHTASFAV KEPDADDEET GEREAAMASV LALYRRNLVE RTKHHLGYPY NLDFDYGALG
     QLQHFSINNL GDPFIESNYG VHSRQFEVGV LDWFARIWEL EKNEYWGYIT NCGTEGNLHG
     ILVGREVFPD GILYASRESH YSVFKAARMY RMDCVKVDTL ISGEIDCEDF QRKLLLNRDK
     PAIINVNIGT TVKGAVDDLD LVIKTLEEGG FKDRFYIHCD GALFGLMIPF VKKAPKVSFK
     KPIGSVSVSG HKFVGCPMPC GVQITRLEHI NRLSSNVEYL ASRDATIMGS RNGHAPIFLW
     YTLNRKGYRG FQKEVQKCLR NAHYLKDRLK EAGIGAMLNE LSSTVVFERP KDEEFVRRWQ
     LACEGNIAHV VVMPSVTIDK LDYFLNELTE KRATWYQDGS CQPPCLAKDV GEENCLCSIH
     KK