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Database: UniProt
Entry: P55217
LinkDB: P55217
Original site: P55217 
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   19-FEB-2014, entry version 113.
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; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   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   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   SABIO-RK; P55217; -.
DR   UniPathway; UPA00051; UER00077.
DR   Genevestigator; P55217; -.
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; SSF53383; 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
//
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