SDC3_ORYSJ
ID SDC3_ORYSJ Reviewed; 446 AA.
AC Q7X8D4;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 2.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Serine decarboxylase 3;
DE EC=4.1.1.-;
GN OrderedLocusNames=LOC_Os04g04640;
GN ORFNames=OSJNBa0059H15.18, OSJNBa0070D17.5;
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=12447439; DOI=10.1038/nature01183;
RA Feng Q., Zhang Y., Hao P., Wang S., Fu G., Huang Y., Li Y., Zhu J., Liu Y.,
RA Hu X., Jia P., Zhang Y., Zhao Q., Ying K., Yu S., Tang Y., Weng Q.,
RA Zhang L., Lu Y., Mu J., Lu Y., Zhang L.S., Yu Z., Fan D., Liu X., Lu T.,
RA Li C., Wu Y., Sun T., Lei H., Li T., Hu H., Guan J., Wu M., Zhang R.,
RA Zhou B., Chen Z., Chen L., Jin Z., Wang R., Yin H., Cai Z., Ren S., Lv G.,
RA Gu W., Zhu G., Tu Y., Jia J., Zhang Y., Chen J., Kang H., Chen X., Shao C.,
RA Sun Y., Hu Q., Zhang X., Zhang W., Wang L., Ding C., Sheng H., Gu J.,
RA Chen S., Ni L., Zhu F., Chen W., Lan L., Lai Y., Cheng Z., Gu M., Jiang J.,
RA Li J., Hong G., Xue Y., Han B.;
RT "Sequence and analysis of rice chromosome 4.";
RL Nature 420:316-320(2002).
RN [2]
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 [3]
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 [4]
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).
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}.
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DR EMBL; AL731602; CAE05435.2; -; Genomic_DNA.
DR EMBL; AL731612; CAE04954.2; -; Genomic_DNA.
DR EMBL; AP008210; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP014960; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; Q7X8D4; -.
DR SMR; Q7X8D4; -.
DR STRING; 39947.Q7X8D4; -.
DR PRIDE; Q7X8D4; -.
DR InParanoid; Q7X8D4; -.
DR PlantReactome; R-OSA-1119556; Choline biosynthesis I.
DR Proteomes; UP000000763; Chromosome 4.
DR Proteomes; UP000059680; Chromosome 4.
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..446
FT /note="Serine decarboxylase 3"
FT /id="PRO_0000429510"
FT BINDING 162
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 274
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 446 AA; 50426 MW; 2F4E450A009C8316 CRC64;
MATFKEHLQE RSAHSIGRVN AHGYEDSNFL LTKLTENKMS CPMTISMLAP TLGTVGRINE
ESRTRRNAGY PINFEFDFGP VIEFLNMRLN NAGDPFMECN YGIHSKKFEI AVLDWFARLW
ELPKDQYWGY VTSGGTEGNM HGLLVGRELF PEGIIYTSCD SHYSIFKAAK MYRVQCIKID
TLFSGEMDYA DFRRKLLQNT RSPAIVNVNI GTTMKGAVDD LDEVVMILEN CGFANRFYIH
CDSALVGLMM PFIKQAPKLT FKKPIGSICI SGHKFIGCPI PCGVLITRLM DINHVMSTNI
EYISSNDTTI AGSRNGHAPI FLWYALKRIG YNGLCKTVEN CLKNAQYLAL RLREMGVSVF
LNALSITVVF ERPNDETFVR KWQLACQGKI AHVVVMPNVS LERINMFLEE FTKSRIALHQ
DKCVAGDVSQ ENCLCSLHLD RKKEAV