SDC1_ARATH
ID SDC1_ARATH Reviewed; 482 AA.
AC Q9MA74;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Serine decarboxylase;
DE Short=AtSDC;
DE EC=4.1.1.-;
DE AltName: Full=Protein EMBRYO DEFECTIVE 1075;
DE AltName: Full=Serine decarboxylase 1;
DE Short=AtSDC1;
GN Name=SDC; Synonyms=EMB1075, SDC1; OrderedLocusNames=At1g43710;
GN ORFNames=F2J6.7;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RX PubMed=11461929; DOI=10.1074/jbc.m106038200;
RA Rontein D., Nishida I., Tashiro G., Yoshioka K., Wu W.I., Voelker D.R.,
RA Basset G., Hanson A.D.;
RT "Plants synthesize ethanolamine by direct decarboxylation of serine using a
RT pyridoxal phosphate enzyme.";
RL J. Biol. Chem. 276:35523-35529(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND INDUCTION.
RX PubMed=12784636; DOI=10.1271/bbb.67.896;
RA Fujimori K., Ohta D.;
RT "Heavy metal induction of Arabidopsis serine decarboxylase gene
RT expression.";
RL Biosci. Biotechnol. Biochem. 67:896-898(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [6]
RP FUNCTION.
RX PubMed=14634155; DOI=10.1093/pcp/pcg144;
RA Rontein D., Rhodes D., Hanson A.D.;
RT "Evidence from engineering that decarboxylation of free serine is the major
RT source of ethanolamine moieties in plants.";
RL Plant Cell Physiol. 44:1185-1191(2003).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=22489147; DOI=10.3390/ijms13033176;
RA Kwon Y., Yu S.I., Lee H., Yim J.H., Zhu J.K., Lee B.H.;
RT "Arabidopsis serine decarboxylase mutants implicate the roles of
RT ethanolamine in plant growth and development.";
RL Int. J. Mol. Sci. 13:3176-3188(2012).
CC -!- FUNCTION: Catalyzes the biosynthesis of ethanolamine from serine.
CC Highly specific for L-serine and does not attack D-serine, L-
CC phosphoserine, phosphatidylserine, L-histidine L-glutamate L-tyrosine
CC or L-tryptophan. Decarboxylation of free serine is the major source of
CC ethanolamine production in plants and ethanolamine metabolism is
CC crucial for the synthesis of choline, phosphatidylethanolamine (PE) and
CC phosphatidylcholine (PC), and thus for plant growth.
CC {ECO:0000269|PubMed:11461929, ECO:0000269|PubMed:14634155,
CC ECO:0000269|PubMed:22489147}.
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; Evidence={ECO:0000269|PubMed:11461929};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:11461929};
CC -!- ACTIVITY REGULATION: No inhibition by ethanolamine, choline or their
CC phosphoesters. {ECO:0000269|PubMed:11461929}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=10 mM for L-serine (at pH 8.0) {ECO:0000269|PubMed:11461929};
CC -!- SUBUNIT: Homotetramer. {ECO:0000305|PubMed:11461929}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000305|PubMed:22489147}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves, flowers and siliques.
CC {ECO:0000269|PubMed:22489147}.
CC -!- INDUCTION: By nickel and manganese ions. {ECO:0000269|PubMed:12784636}.
CC -!- DISRUPTION PHENOTYPE: Dwarf plants with necrosis along the edges of the
CC leaves, multiple inflorescences and sterile flowers.
CC {ECO:0000269|PubMed:22489147}.
CC -!- MISCELLANEOUS: The mutant phenotype can be rescue by exogenous
CC application of ethanolamine. {ECO:0000305|PubMed:22489147}.
CC -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC {ECO:0000305}.
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DR EMBL; AF389349; AAK77493.1; -; mRNA.
DR EMBL; AB030379; BAB79456.1; -; mRNA.
DR EMBL; AB036933; BAB79457.1; -; Genomic_DNA.
DR EMBL; AC009526; AAF63121.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE31989.1; -; Genomic_DNA.
DR EMBL; AF360233; AAK25943.1; -; mRNA.
DR EMBL; AY040033; AAK64091.1; -; mRNA.
DR PIR; E96500; E96500.
DR RefSeq; NP_175036.1; NM_103496.3.
DR AlphaFoldDB; Q9MA74; -.
DR SMR; Q9MA74; -.
DR STRING; 3702.AT1G43710.1; -.
DR iPTMnet; Q9MA74; -.
DR PaxDb; Q9MA74; -.
DR PRIDE; Q9MA74; -.
DR ProteomicsDB; 232945; -.
DR EnsemblPlants; AT1G43710.1; AT1G43710.1; AT1G43710.
DR GeneID; 840958; -.
DR Gramene; AT1G43710.1; AT1G43710.1; AT1G43710.
DR KEGG; ath:AT1G43710; -.
DR Araport; AT1G43710; -.
DR TAIR; locus:2031133; AT1G43710.
DR eggNOG; KOG0629; Eukaryota.
DR HOGENOM; CLU_028929_0_1_1; -.
DR InParanoid; Q9MA74; -.
DR OMA; GTENCAC; -.
DR OrthoDB; 810772at2759; -.
DR PhylomeDB; Q9MA74; -.
DR BioCyc; ARA:AT1G43710-MON; -.
DR SABIO-RK; Q9MA74; -.
DR PRO; PR:Q9MA74; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9MA74; baseline and differential.
DR Genevisible; Q9MA74; AT.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
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:0006580; P:ethanolamine metabolic process; IMP:TAIR.
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 1: Evidence at protein level;
KW Cytoplasm; Decarboxylase; Lyase; Pyridoxal phosphate; Reference proteome.
FT CHAIN 1..482
FT /note="Serine decarboxylase"
FT /id="PRO_0000429507"
FT BINDING 201
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 314
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 482 AA; 54077 MW; E7FEF612A8450826 CRC64;
MVGSLESDQT LSMATLIEKL DILSDDFDPT AVVTEPLPPP VTNGIGADKG GGGGEREMVL
GRNIHTTSLA VTEPEVNDEF TGDKEAYMAS VLARYRKTLV ERTKNHLGYP YNLDFDYGAL
GQLQHFSINN LGDPFIESNY GVHSRPFEVG VLDWFARLWE IERDDYWGYI TNCGTEGNLH
GILVGREMFP DGILYASRES HYSVFKAARM YRMECEKVDT LMSGEIDCDD LRKKLLANKD
KPAILNVNIG TTVKGAVDDL DLVIKTLEEC GFSHDRFYIH CDGALFGLMM PFVKRAPKVT
FNKPIGSVSV SGHKFVGCPM PCGVQITRME HIKVLSSNVE YLASRDATIM GSRNGHAPLF
LWYTLNRKGY KGFQKEVQKC LRNAHYLKDR LREAGISAML NELSSTVVFE RPKDEEFVRR
WQLACQGDIA HVVVMPSVTI EKLDNFLKDL VKHRLIWYED GSQPPCLASE VGTNNCICPA
HK
