ID METB_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-MAY-2013, entry version 107.
DE RecName: Full=Cystathionine gamma-synthase, chloroplastic;
DE Short=CGS;
DE EC=2.5.1.48;
DE AltName: Full=O-succinylhomoserine (thiol)-lyase;
DE Flags: Precursor;
GN Name=CGS1; Synonyms=CYS1; OrderedLocusNames=At3g01120;
GN ORFNames=T4P13.19;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. Columbia;
RA Gakiere B., Ravanel S., Job D., Douce R.;
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE, AND VARIANTS SER-8; GLY-55; GLY-91 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 [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).
CC -!- FUNCTION: Catalyzes the formation of L-cystathionine from O-
CC succinyl-L-homoserine (OSHS) and L-cysteine, via a gamma-
CC replacement reaction. In the absence of thiol, catalyzes gamma-
CC elimination to form 2-oxobutanoate, succinate and ammonia (By
CC similarity).
CC -!- CATALYTIC ACTIVITY: O(4)-succinyl-L-homoserine + L-cysteine = L-
CC cystathionine + succinate.
CC -!- COFACTOR: Pyridoxal phosphate.
CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de
CC novo pathway; L-cystathionine from O-succinyl-L-homoserine: step
CC 1/1.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC -!- SIMILARITY: Belongs to the trans-sulfuration enzymes family.
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DR EMBL; X94756; CAA64383.1; -; mRNA.
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; 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 IPI; IPI00534631; -.
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 ProtClustDB; CLSN2679254; -.
DR BioCyc; ARA:AT3G01120-MONOMER; -.
DR BioCyc; MetaCyc:AT3G01120-MONOMER; -.
DR UniPathway; UPA00051; UER00077.
DR Genevestigator; P55217; -.
DR GermOnline; AT3G01120; Arabidopsis thaliana.
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; IEA:InterPro.
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; PyrdxlP-dep_Trfase_major; 1.
DR PROSITE; PS00868; CYS_MET_METAB_PP; 1.
PE 2: Evidence at transcript level;
KW Amino-acid biosynthesis; Chloroplast; Complete proteome;
KW Methionine biosynthesis; Plastid; Polymorphism; Pyridoxal phosphate;
KW Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1 182 Chloroplast (Potential).
FT CHAIN 183 563 Cystathionine gamma-synthase,
FT chloroplastic.
FT /FTId=PRO_0000033455.
FT COMPBIAS 13 18 Poly-Ser.
FT COMPBIAS 104 109 Poly-Ala.
FT COMPBIAS 119 125 Poly-Ala.
FT COMPBIAS 128 131 Poly-Ala.
FT MOD_RES 379 379 N6-(pyridoxal phosphate)lysine (By
FT similarity).
FT VARIANT 8 8 C -> S.
FT VARIANT 55 55 A -> G.
FT VARIANT 91 91 A -> G.
FT VARIANT 412 412 T -> P.
FT VARIANT 459 459 G -> A.
FT CONFLICT 102 102 P -> T (in Ref. 1; CAA64383).
FT CONFLICT 177 177 S -> Q (in Ref. 1; CAA64383).
FT CONFLICT 547 547 E -> K (in Ref. 7; AAM13883).
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
//
