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Database: UniProt
Entry: P55217
LinkDB: P55217
Original site: P55217 
ID   CGS1_ARATH              Reviewed;         563 AA.
AC   P55217; P92944; P93038; Q42550;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   20-JUN-2002, sequence version 3.
DT   01-APR-2015, entry version 120.
DE   RecName: Full=Cystathionine gamma-synthase 1, chloroplastic {ECO:0000305};
DE            Short=AtCGS1 {ECO:0000305};
DE            EC=2.5.1.48 {ECO:0000269|PubMed:9531508};
DE   AltName: Full=METHIONINE OVERACCUMULATION 1 {ECO:0000303|PubMed:10558994};
DE   AltName: Full=O-succinylhomoserine (thiol)-lyase;
DE   Flags: Precursor;
GN   Name=CGS1 {ECO:0000305};
GN   Synonyms=CYS1 {ECO:0000305}, MTO1 {ECO:0000303|PubMed:10558994};
GN   OrderedLocusNames=At3g01120; ORFNames=T4P13.19;
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], AND VARIANTS SER-8; GLY-55; GLY-91 AND
RP   ALA-459.
RC   STRAIN=cv. Landsberg erecta;
RX   PubMed=9002610; DOI=10.1007/BF00041395;
RA   Kim J., Leustek T.;
RT   "Cloning and analysis of the gene for cystathionine gamma-synthase
RT   from Arabidopsis thaliana.";
RL   Plant Mol. Biol. 32:1117-1124(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 69-76, FUNCTION,
RP   CATALYTIC ACTIVITY, COFACTOR, ENZYME REGULATION, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=9531508;
RA   Ravanel S., Gakiere B., Job D., Douce R.;
RT   "Cystathionine gamma-synthase from Arabidopsis thaliana: purification
RT   and biochemical characterization of the recombinant enzyme
RT   overexpressed in Escherichia coli.";
RL   Biochem. J. 331:639-648(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS SER-8; GLY-55; GLY-91
RP   AND PRO-412.
RC   STRAIN=cv. Columbia, and cv. Landsberg erecta;
RA   Kim J., Chiba Y., Yamamoto A., Naito S., Leustek T.;
RT   "Nucleotide sequence polymorphisms in the cystathionine gamma-synthase
RT   gene of Arabidopsis thaliana.";
RL   (er) Plant Gene Register PGR99-087.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Columbia;
RA   Lessard P., Kreis M., Thomas M.;
RL   Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130713; DOI=10.1038/35048706;
RA   Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M.,
RA   Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B.,
RA   Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P.,
RA   De Simone V., Choisne N., Artiguenave F., Robert C., Brottier P.,
RA   Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V.,
RA   Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S.,
RA   Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G.,
RA   Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B.,
RA   Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G.,
RA   Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J.,
RA   Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D.,
RA   Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA   de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA   Monfort A., Argiriou A., Flores M., Liguori R., Vitale D.,
RA   Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W.,
RA   Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J.,
RA   Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P.,
RA   Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S.,
RA   Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V.,
RA   Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C.,
RA   Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E.,
RA   Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y.,
RA   Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A.,
RA   Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence and analysis of chromosome 3 of the plant Arabidopsis
RT   thaliana.";
RL   Nature 408:820-822(2000).
RN   [6]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RG   The Arabidopsis Information Resource (TAIR);
RL   Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
RN   [7]
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   [8]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 340-563, AND VARIANT PRO-412.
RC   STRAIN=cv. Columbia;
RX   PubMed=7816049; DOI=10.1007/BF00290120;
RA   le Guen L., Thomas M., Kreis M.;
RT   "Gene density and organization in a small region of the Arabidopsis
RT   thaliana genome.";
RL   Mol. Gen. Genet. 245:390-396(1994).
RN   [9]
RP   INDUCTION, AND MUTAGENESIS OF ARG-77; SER-81 AND GLY-84.
RX   PubMed=10558994; DOI=10.1126/science.286.5443.1371;
RA   Chiba Y., Ishikawa M., Kijima F., Tyson R.H., Kim J., Yamamoto A.,
RA   Nambara E., Leustek T., Wallsgrove R.M., Naito S.;
RT   "Evidence for autoregulation of cystathionine gamma-synthase mRNA
RT   stability in Arabidopsis.";
RL   Science 286:1371-1374(1999).
RN   [10]
RP   MUTAGENESIS OF ARG-78 AND ALA-86.
RX   PubMed=12121993; DOI=10.1074/jbc.M204645200;
RA   Ominato K., Akita H., Suzuki A., Kijima F., Yoshino T., Yoshino M.,
RA   Chiba Y., Onouchi H., Naito S.;
RT   "Identification of a short highly conserved amino acid sequence as the
RT   functional region required for posttranscriptional autoregulation of
RT   the cystathionine gamma-synthase gene in Arabidopsis.";
RL   J. Biol. Chem. 277:36380-36386(2002).
RN   [11]
RP   SUBCELLULAR LOCATION.
RX   PubMed=25146485; DOI=10.1093/pcp/pcu110;
RA   Hagiwara-Komoda Y., Sugiyama T., Yamashita Y., Onouchi H., Naito S.;
RT   "The N-terminal cleavable pre-sequence encoded in the first exon of
RT   cystathionine gamma-synthase contains two different functional domains
RT   for chloroplast targeting and regulation of gene expression.";
RL   Plant Cell Physiol. 55:1779-1792(2014).
CC   -!- FUNCTION: Catalyzes the first committed step of methionine (Met)
CC       biosynthesis. Catalyzes the formation of L-cystathionine from
CC       homoserine esters and L-cysteine, via a gamma-replacement
CC       reaction. Substrate preference for cystathionine synthesis is O-
CC       phospho-L-homoserine (OPH) > O(4)-succinyl-L-homoserine (OSH) >>
CC       O-acetyl-L-homoserine (OAH). Is able, at extremely low rate, to
CC       catalyze a gamma-elimination of OPH in the absence of cysteine to
CC       produce inorganic phosphate (Pi), 2-oxobutanoate and ammonia.
CC       {ECO:0000269|PubMed:9531508}.
CC   -!- CATALYTIC ACTIVITY: O(4)-succinyl-L-homoserine + L-cysteine = L-
CC       cystathionine + succinate. {ECO:0000269|PubMed:9531508}.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000269|PubMed:9531508};
CC       Note=Binds 1 pyridoxal 5'-phosphate per subunit.
CC       {ECO:0000269|PubMed:9531508};
CC   -!- ENZYME REGULATION: Inhibited by propargylglycine.
CC       {ECO:0000269|PubMed:9531508}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.46 mM for L-cysteine {ECO:0000269|PubMed:9531508};
CC         KM=2.5 mM for O-phospho-L-homoserine
CC         {ECO:0000269|PubMed:9531508};
CC         Vmax=33.6 umol/min/mg enzyme with L-cysteine as substrate
CC         {ECO:0000269|PubMed:9531508};
CC         Note=kcat is 30 sec(-1) with L-cysteine as substrate.
CC         {ECO:0000269|PubMed:9531508};
CC       pH dependence:
CC         Optimum pH is 7.5. {ECO:0000269|PubMed:9531508};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de
CC       novo pathway; L-cystathionine from O-succinyl-L-homoserine: step
CC       1/1. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC       {ECO:0000269|PubMed:25146485}.
CC   -!- INDUCTION: Down-regulated by methionine.
CC       {ECO:0000269|PubMed:10558994}.
CC   -!- MISCELLANEOUS: A DNA region of the first exon coding for a
CC       conserved motif of 11 amino acids in CGS1 (positions 77-87) is
CC       required for post-transcriptional autoregulation and acts in cis
CC       to down-regulate its own mRNA stability in response to excess
CC       methionine. This conserved motif is dispensable for CGS enzymatic
CC       activity and only found in plant CGSs (PubMed:10558994,
CC       PubMed:12121993). It is unclear whether the transit peptide
CC       cleavage site is between Phe-68 and Val-69 (PubMed:9531508) or
CC       Ala-90 and Ala-91 (PubMed:25146485). {ECO:0000269|PubMed:10558994,
CC       ECO:0000269|PubMed:12121993, ECO:0000269|PubMed:25146485,
CC       ECO:0000269|PubMed:9531508}.
CC   -!- SIMILARITY: Belongs to the trans-sulfuration enzymes family.
CC       {ECO:0000305}.
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DR   EMBL; U43709; AAC49574.1; -; mRNA.
DR   EMBL; U83500; AAB41235.1; -; mRNA.
DR   EMBL; AB010888; BAA24699.1; -; Genomic_DNA.
DR   EMBL; AF039206; AAC25687.1; -; Genomic_DNA.
DR   EMBL; X94756; CAA64383.1; -; mRNA.
DR   EMBL; AC008261; AAF26162.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE73612.1; -; Genomic_DNA.
DR   EMBL; AY094438; AAM19810.1; -; mRNA.
DR   EMBL; AY091062; AAM13883.1; -; mRNA.
DR   EMBL; BT002753; AAO22582.1; -; mRNA.
DR   EMBL; X79707; CAA56143.1; -; Genomic_DNA.
DR   PIR; S51579; S51579.
DR   PIR; S71228; S71228.
DR   RefSeq; NP_186761.1; NM_110977.2.
DR   UniGene; At.20198; -.
DR   ProteinModelPortal; P55217; -.
DR   SMR; P55217; 170-563.
DR   PaxDb; P55217; -.
DR   PRIDE; P55217; -.
DR   EnsemblPlants; AT3G01120.1; AT3G01120.1; AT3G01120.
DR   GeneID; 821292; -.
DR   KEGG; ath:AT3G01120; -.
DR   TAIR; AT3G01120; -.
DR   eggNOG; COG0626; -.
DR   HOGENOM; HOG000246415; -.
DR   InParanoid; P55217; -.
DR   KO; K01739; -.
DR   OMA; NAEHGAN; -.
DR   PhylomeDB; P55217; -.
DR   BioCyc; ARA:AT3G01120-MONOMER; -.
DR   BioCyc; MetaCyc:AT3G01120-MONOMER; -.
DR   BRENDA; 2.5.1.48; 399.
DR   SABIO-RK; P55217; -.
DR   UniPathway; UPA00051; UER00077.
DR   Proteomes; UP000006548; Chromosome 3.
DR   Genevestigator; P55217; -.
DR   GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR   GO; GO:0009570; C:chloroplast stroma; IDA:TAIR.
DR   GO; GO:0003962; F:cystathionine gamma-synthase activity; IDA:TAIR.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IDA:UniProtKB.
DR   GO; GO:0009086; P:methionine biosynthetic process; IMP:TAIR.
DR   GO; GO:0001887; P:selenium compound metabolic process; IDA:TAIR.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR000277; Cys/Met-Metab_PyrdxlP-dep_enz.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2.
DR   PANTHER; PTHR11808; PTHR11808; 1.
DR   Pfam; PF01053; Cys_Met_Meta_PP; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   PROSITE; PS00868; CYS_MET_METAB_PP; 1.
PE   1: Evidence at protein level;
KW   Amino-acid biosynthesis; Chloroplast; Complete proteome;
KW   Direct protein sequencing; Methionine biosynthesis; Plastid;
KW   Polymorphism; Pyridoxal phosphate; Reference proteome; Transferase;
KW   Transit peptide.
FT   TRANSIT       1     68       Chloroplast.
FT                                {ECO:0000305|PubMed:9531508}.
FT   CHAIN        69    563       Cystathionine gamma-synthase 1,
FT                                chloroplastic.
FT                                /FTId=PRO_0000033455.
FT   COMPBIAS    104    136       Ala-rich. {ECO:0000255}.
FT   MOD_RES     379    379       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000250|UniProtKB:P53780}.
FT   VARIANT       8      8       C -> S. {ECO:0000269|PubMed:9002610,
FT                                ECO:0000269|Ref.3, ECO:0000269|Ref.4}.
FT   VARIANT      55     55       A -> G. {ECO:0000269|PubMed:9002610,
FT                                ECO:0000269|Ref.3, ECO:0000269|Ref.4}.
FT   VARIANT      91     91       A -> G. {ECO:0000269|PubMed:9002610,
FT                                ECO:0000269|Ref.3, ECO:0000269|Ref.4}.
FT   VARIANT     412    412       T -> P. {ECO:0000269|PubMed:7816049,
FT                                ECO:0000269|Ref.3, ECO:0000269|Ref.4}.
FT   VARIANT     459    459       G -> A. {ECO:0000269|PubMed:9002610}.
FT   MUTAGEN      77     77       R->H: In mto1-4; over-accumulation of
FT                                soluble methionine.
FT                                {ECO:0000269|PubMed:10558994}.
FT   MUTAGEN      78     78       R->K: In mto1-7; over-accumulation of
FT                                soluble methionine.
FT                                {ECO:0000269|PubMed:12121993}.
FT   MUTAGEN      81     81       S->N: In mto1-2; over-accumulation of
FT                                soluble methionine.
FT                                {ECO:0000269|PubMed:10558994}.
FT   MUTAGEN      84     84       G->D: In mto1-3 and mto1-5; over-
FT                                accumulation of soluble methionine.
FT                                {ECO:0000269|PubMed:10558994}.
FT   MUTAGEN      84     84       G->S: In mto1-1; over-accumulation of
FT                                soluble methionine.
FT                                {ECO:0000269|PubMed:10558994}.
FT   MUTAGEN      86     86       A->V: In mto1-6; over-accumulation of
FT                                soluble methionine.
FT                                {ECO:0000269|PubMed:12121993}.
FT   CONFLICT    102    102       P -> T (in Ref. 4; CAA64383).
FT                                {ECO:0000305}.
FT   CONFLICT    177    177       S -> Q (in Ref. 4; CAA64383).
FT                                {ECO:0000305}.
FT   CONFLICT    547    547       E -> K (in Ref. 7; AAM13883).
FT                                {ECO:0000305}.
SQ   SEQUENCE   563 AA;  59919 MW;  4FB902896C062860 CRC64;
     MAVSSFQCPT IFSSSSISGF QCRSDPDLVG SPVGGSSRRR VHASAGISSS FTGDAGLSSR
     ILRFPPNFVR QLSIKARRNC SNIGVAQIVA AKWSNNPSSA LPSAAAAAAT SSASAVSSAA
     SAAAASSAAA APVAAAPPVV LKSVDEEVVV AEEGIREKIG SVQLTDSKHS FLSSDGSLTV
     HAGERLGRGI VTDAITTPVV NTSAYFFKKT AELIDFKEKR SVSFEYGRYG NPTTVVLEDK
     ISALEGAEST LVMASGMCAS TVMLLALVPA GGHIVTTTDC YRKTRIFMEN FLPKLGITVT
     VIDPADIAGL EAAVNEFKVS LFFTESPTNP FLRCVDIELV SKICHKRGTL VCIDGTFATP
     LNQKALALGA DLVVHSATKY IGGHNDVLAG CICGSLKLVS EIRNLHHVLG GTLNPNAAYL
     IIRGMKTLHL RVQQQNSTAF RMAEILEAHP KVSHVYYPGL PSHPEHELAK RQMTGFGGVV
     SFEIDGDIET TIKFVDSLKI PYIAPSFGGC ESIVDQPAIM SYWDLPQEER LKYGIKDNLV
     RFSFGVEDFE DVKADILQAL EAI
//
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