Entry sw: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   30-NOV-2016, entry version 114.
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 Resource (TAIR);
RL   Submitted (APR-2011) 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}.
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   TAIR; 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   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   InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
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
//