CGS1_ARATH
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 03-AUG-2022, entry version 154.
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; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS SER-8; GLY-55; GLY-91 AND 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 from
RT Arabidopsis thaliana.";
RL Plant Mol. Biol. 32:1117-1124(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 69-76, FUNCTION, CATALYTIC
RP ACTIVITY, COFACTOR, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=9531508; DOI=10.1042/bj3310639;
RA Ravanel S., Gakiere B., Job D., Douce R.;
RT "Cystathionine gamma-synthase from Arabidopsis thaliana: purification and
RT biochemical characterization of the recombinant enzyme overexpressed in
RT Escherichia coli.";
RL Biochem. J. 331:639-648(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS SER-8; GLY-55; GLY-91 AND
RP 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 gene
RT of Arabidopsis thaliana.";
RL (er) Plant Gene Register PGR99-087(1999).
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., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., 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., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., 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 thaliana.";
RL Nature 408:820-822(2000).
RN [6]
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 [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., 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 [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 stability
RT 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 the
RT 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 for
RT 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 reaction.
CC Substrate preference for cystathionine synthesis is O-phospho-L-
CC homoserine (OPH) > O(4)-succinyl-L-homoserine (OSH) >> O-acetyl-L-
CC homoserine (OAH). Is able, at extremely low rate, to catalyze a gamma-
CC elimination of OPH in the absence of cysteine to produce inorganic
CC phosphate (Pi), 2-oxobutanoate and ammonia.
CC {ECO:0000269|PubMed:9531508}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-cysteine + O-succinyl-L-homoserine = H(+) + L,L-
CC cystathionine + succinate; Xref=Rhea:RHEA:20397, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:35235, ChEBI:CHEBI:57661,
CC ChEBI:CHEBI:58161; EC=2.5.1.48;
CC Evidence={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 -!- ACTIVITY 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 {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 novo
CC pathway; L-cystathionine from O-succinyl-L-homoserine: step 1/1.
CC {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:25146485}.
CC -!- INDUCTION: Down-regulated by methionine. {ECO:0000269|PubMed:10558994}.
CC -!- MISCELLANEOUS: A DNA region of the first exon coding for a conserved
CC motif of 11 amino acids in CGS1 (positions 77-87) is required for post-
CC transcriptional autoregulation and acts in cis to down-regulate its own
CC mRNA stability in response to excess methionine. This conserved motif
CC is dispensable for CGS enzymatic activity and only found in plant CGSs
CC (PubMed:10558994, PubMed:12121993). It is unclear whether the transit
CC peptide 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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_110977.3.
DR AlphaFoldDB; P55217; -.
DR SMR; P55217; -.
DR BioGRID; 6625; 1.
DR STRING; 3702.AT3G01120.1; -.
DR PaxDb; P55217; -.
DR PRIDE; P55217; -.
DR ProteomicsDB; 224398; -.
DR EnsemblPlants; AT3G01120.1; AT3G01120.1; AT3G01120.
DR GeneID; 821292; -.
DR Gramene; AT3G01120.1; AT3G01120.1; AT3G01120.
DR KEGG; ath:AT3G01120; -.
DR Araport; AT3G01120; -.
DR TAIR; locus:2102072; AT3G01120.
DR eggNOG; KOG0053; Eukaryota.
DR HOGENOM; CLU_018986_1_2_1; -.
DR InParanoid; P55217; -.
DR OMA; LRMERAN; -.
DR OrthoDB; 572061at2759; -.
DR PhylomeDB; P55217; -.
DR BioCyc; ARA:AT3G01120-MON; -.
DR BioCyc; MetaCyc:AT3G01120-MON; -.
DR BRENDA; 2.5.1.48; 399.
DR SABIO-RK; P55217; -.
DR UniPathway; UPA00051; UER00077.
DR PRO; PR:P55217; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; P55217; baseline and differential.
DR Genevisible; P55217; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0003962; F:cystathionine gamma-synthase activity; IDA:TAIR.
DR GO; GO:0102028; F:cystathionine gamma-synthase activity (acts on O-phosphohomoserine); IEA:UniProtKB-EC.
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 GO; GO:0019346; P:transsulfuration; IEA:InterPro.
DR CDD; cd00614; CGS_like; 1.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR044639; CGS1/2.
DR InterPro; IPR000277; Cys/Met-Metab_PyrdxlP-dep_enz.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR43379; PTHR43379; 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; Direct protein sequencing;
KW Methionine biosynthesis; Plastid; Pyridoxal phosphate; Reference proteome;
KW Transferase; Transit peptide.
FT TRANSIT 1..68
FT /note="Chloroplast"
FT /evidence="ECO:0000305|PubMed:9531508"
FT CHAIN 69..563
FT /note="Cystathionine gamma-synthase 1, chloroplastic"
FT /id="PRO_0000033455"
FT MOD_RES 379
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P53780"
FT VARIANT 8
FT /note="C -> S"
FT /evidence="ECO:0000269|PubMed:9002610, ECO:0000269|Ref.3,
FT ECO:0000269|Ref.4"
FT VARIANT 55
FT /note="A -> G"
FT /evidence="ECO:0000269|PubMed:9002610, ECO:0000269|Ref.3,
FT ECO:0000269|Ref.4"
FT VARIANT 91
FT /note="A -> G"
FT /evidence="ECO:0000269|PubMed:9002610, ECO:0000269|Ref.3,
FT ECO:0000269|Ref.4"
FT VARIANT 412
FT /note="T -> P"
FT /evidence="ECO:0000269|PubMed:7816049, ECO:0000269|Ref.3,
FT ECO:0000269|Ref.4"
FT VARIANT 459
FT /note="G -> A"
FT /evidence="ECO:0000269|PubMed:9002610"
FT MUTAGEN 77
FT /note="R->H: In mto1-4; over-accumulation of soluble
FT methionine."
FT /evidence="ECO:0000269|PubMed:10558994"
FT MUTAGEN 78
FT /note="R->K: In mto1-7; over-accumulation of soluble
FT methionine."
FT /evidence="ECO:0000269|PubMed:12121993"
FT MUTAGEN 81
FT /note="S->N: In mto1-2; over-accumulation of soluble
FT methionine."
FT /evidence="ECO:0000269|PubMed:10558994"
FT MUTAGEN 84
FT /note="G->D: In mto1-3 and mto1-5; over-accumulation of
FT soluble methionine."
FT /evidence="ECO:0000269|PubMed:10558994"
FT MUTAGEN 84
FT /note="G->S: In mto1-1; over-accumulation of soluble
FT methionine."
FT /evidence="ECO:0000269|PubMed:10558994"
FT MUTAGEN 86
FT /note="A->V: In mto1-6; over-accumulation of soluble
FT methionine."
FT /evidence="ECO:0000269|PubMed:12121993"
FT CONFLICT 102
FT /note="P -> T (in Ref. 4; CAA64383)"
FT /evidence="ECO:0000305"
FT CONFLICT 177
FT /note="S -> Q (in Ref. 4; CAA64383)"
FT /evidence="ECO:0000305"
FT CONFLICT 547
FT /note="E -> K (in Ref. 7; AAM13883)"
FT /evidence="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
