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 12-APR-2017, entry version 117.
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; Magnoliophyta; eudicotyledons; Gunneridae;
OC Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP ENZYME 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.,
RA Voelker D.R., Basset G., Hanson A.D.;
RT "Plants synthesize ethanolamine by direct decarboxylation of serine
RT using a 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.,
RA White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
RA Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
RA Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
RA Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
RA Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
RA Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
RA Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
RA Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
RA Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
RA Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
RA Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
RA Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
RA 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.,
RA Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis
RT thaliana.";
RL Nature 408:816-820(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RG The Arabidopsis Information Portal (Araport);
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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.,
RA Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA Yuan S., Shinozaki K., Davis R.W., Theologis A., 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
RT major 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-
CC tyrosine or L-tryptophan. Decarboxylation of free serine is the
CC major source of ethanolamine production in plants and ethanolamine
CC metabolism is crucial for the synthesis of choline,
CC phosphatidylethanolamine (PE) and phosphatidylcholine (PC), and
CC thus for plant growth. {ECO:0000269|PubMed:11461929,
CC ECO:0000269|PubMed:14634155, ECO:0000269|PubMed:22489147}.
CC -!- CATALYTIC ACTIVITY: L-serine = ethanolamine + CO(2).
CC {ECO:0000269|PubMed:11461929}.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:11461929};
CC -!- ENZYME 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
CC {ECO:0000305|PubMed:22489147}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves, flowers and
CC siliques. {ECO:0000269|PubMed:22489147}.
CC -!- INDUCTION: By nickel and manganese ions.
CC {ECO:0000269|PubMed:12784636}.
CC -!- DISRUPTION PHENOTYPE: Dwarf plants with necrosis along the edges
CC of the 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 UniGene; At.21345; -.
DR ProteinModelPortal; Q9MA74; -.
DR STRING; 3702.AT1G43710.1; -.
DR iPTMnet; Q9MA74; -.
DR PaxDb; Q9MA74; -.
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 eggNOG; COG0076; LUCA.
DR HOGENOM; HOG000239145; -.
DR InParanoid; Q9MA74; -.
DR KO; K01590; -.
DR OMA; PPCLAKD; -.
DR OrthoDB; EOG093608GR; -.
DR PhylomeDB; Q9MA74; -.
DR BioCyc; ARA:AT1G43710-MONOMER; -.
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:0016831; F:carboxy-lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
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_sub1.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_sub2.
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 Complete proteome; Cytoplasm; Decarboxylase; Lyase;
KW Pyridoxal phosphate; Reference proteome.
FT CHAIN 1 482 Serine decarboxylase.
FT /FTId=PRO_0000429507.
FT BINDING 201 201 Substrate. {ECO:0000250}.
FT MOD_RES 314 314 N6-(pyridoxal phosphate)lysine.
FT {ECO:0000250}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 307 328 ipat:DDC_GAD_HDC_YDC [T]
FT MYHIT 193 406 ipfam:Pyridoxal_deC [T]
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
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