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P55217 (METB_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 115. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cystathionine gamma-synthase, chloroplastic

Short name=CGS
EC=2.5.1.48
Alternative name(s):
O-succinylhomoserine (thiol)-lyase
Gene names
Name:CGS1
Synonyms:CYS1
Ordered Locus Names:At3g01120
ORF Names:T4P13.19
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length563 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Catalyzes the formation of L-cystathionine from O-succinyl-L-homoserine (OSHS) and L-cysteine, via a gamma-replacement reaction. In the absence of thiol, catalyzes gamma-elimination to form 2-oxobutanoate, succinate and ammonia By similarity.

Catalytic activity

O(4)-succinyl-L-homoserine + L-cysteine = L-cystathionine + succinate.

Cofactor

Pyridoxal phosphate.

Pathway

Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-cystathionine from O-succinyl-L-homoserine: step 1/1.

Subcellular location

Plastidchloroplast.

Sequence similarities

Belongs to the trans-sulfuration enzymes family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 182182Chloroplast Potential
Chain183 – 563381Cystathionine gamma-synthase, chloroplastic
PRO_0000033455

Regions

Compositional bias13 – 186Poly-Ser
Compositional bias104 – 1096Poly-Ala
Compositional bias119 – 1257Poly-Ala
Compositional bias128 – 1314Poly-Ala

Amino acid modifications

Modified residue3791N6-(pyridoxal phosphate)lysine By similarity

Natural variations

Natural variant81C → S. Ref.2 Ref.4
Natural variant551A → G. Ref.2 Ref.4
Natural variant911A → G. Ref.2 Ref.4
Natural variant4121T → P. Ref.4 Ref.8
Natural variant4591G → A. Ref.2

Experimental info

Sequence conflict1021P → T in CAA64383. Ref.1
Sequence conflict1771S → Q in CAA64383. Ref.1
Sequence conflict5471E → K in AAM13883. Ref.7

Sequences

Sequence LengthMass (Da)Tools
P55217 [UniParc].

Last modified June 20, 2002. Version 3.
Checksum: 4FB902896C062860

FASTA56359,919
        10         20         30         40         50         60 
MAVSSFQCPT IFSSSSISGF QCRSDPDLVG SPVGGSSRRR VHASAGISSS FTGDAGLSSR 

        70         80         90        100        110        120 
ILRFPPNFVR QLSIKARRNC SNIGVAQIVA AKWSNNPSSA LPSAAAAAAT SSASAVSSAA 

       130        140        150        160        170        180 
SAAAASSAAA APVAAAPPVV LKSVDEEVVV AEEGIREKIG SVQLTDSKHS FLSSDGSLTV 

       190        200        210        220        230        240 
HAGERLGRGI VTDAITTPVV NTSAYFFKKT AELIDFKEKR SVSFEYGRYG NPTTVVLEDK 

       250        260        270        280        290        300 
ISALEGAEST LVMASGMCAS TVMLLALVPA GGHIVTTTDC YRKTRIFMEN FLPKLGITVT 

       310        320        330        340        350        360 
VIDPADIAGL EAAVNEFKVS LFFTESPTNP FLRCVDIELV SKICHKRGTL VCIDGTFATP 

       370        380        390        400        410        420 
LNQKALALGA DLVVHSATKY IGGHNDVLAG CICGSLKLVS EIRNLHHVLG GTLNPNAAYL 

       430        440        450        460        470        480 
IIRGMKTLHL RVQQQNSTAF RMAEILEAHP KVSHVYYPGL PSHPEHELAK RQMTGFGGVV 

       490        500        510        520        530        540 
SFEIDGDIET TIKFVDSLKI PYIAPSFGGC ESIVDQPAIM SYWDLPQEER LKYGIKDNLV 

       550        560 
RFSFGVEDFE DVKADILQAL EAI 

« Hide

References

« Hide 'large scale' references
[1]Lessard P., Kreis M., Thomas M.
Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. Columbia.
[2]"Cloning and analysis of the gene for cystathionine gamma-synthase from Arabidopsis thaliana."
Kim J., Leustek T.
Plant Mol. Biol. 32:1117-1124(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS SER-8; GLY-55; GLY-91 AND ALA-459.
Strain: cv. Landsberg erecta.
[3]Gakiere B., Ravanel S., Job D., Douce R.
Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: cv. Columbia.
[4]"Nucleotide sequence polymorphisms in the cystathionine gamma-synthase gene of Arabidopsis thaliana."
Kim J., Chiba Y., Yamamoto A., Naito S., Leustek T.
Plant Gene Register PGR99-087
Cited for: NUCLEOTIDE SEQUENCE, VARIANTS SER-8; GLY-55; GLY-91 AND PRO-412.
Strain: cv. Columbia and cv. Landsberg erecta.
[5]"Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana."
Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F. expand/collapse author list , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
Nature 408:820-822(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[6]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[7]"Empirical analysis of transcriptional activity in the Arabidopsis genome."
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. expand/collapse author list , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[8]"Gene density and organization in a small region of the Arabidopsis thaliana genome."
le Guen L., Thomas M., Kreis M.
Mol. Gen. Genet. 245:390-396(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 340-563, VARIANT PRO-412.
Strain: cv. Columbia.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X94756 mRNA. Translation: CAA64383.1.
U43709 mRNA. Translation: AAC49574.1.
U83500 mRNA. Translation: AAB41235.1.
AB010888 Genomic DNA. Translation: BAA24699.1.
AF039206 Genomic DNA. Translation: AAC25687.1.
AC008261 Genomic DNA. Translation: AAF26162.1.
CP002686 Genomic DNA. Translation: AEE73612.1.
AY094438 mRNA. Translation: AAM19810.1.
AY091062 mRNA. Translation: AAM13883.1.
BT002753 mRNA. Translation: AAO22582.1.
X79707 Genomic DNA. Translation: CAA56143.1.
PIRS51579.
S71228.
RefSeqNP_186761.1. NM_110977.2.
UniGeneAt.20198.

3D structure databases

ProteinModelPortalP55217.
SMRP55217. Positions 170-563.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PaxDbP55217.
PRIDEP55217.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT3G01120.1; AT3G01120.1; AT3G01120.
GeneID821292.
KEGGath:AT3G01120.

Organism-specific databases

TAIRAT3G01120.

Phylogenomic databases

eggNOGCOG0626.
HOGENOMHOG000246415.
InParanoidP55217.
KOK01739.
OMAKFPLFTE.
PhylomeDBP55217.

Enzyme and pathway databases

BioCycARA:AT3G01120-MONOMER.
MetaCyc:AT3G01120-MONOMER.
SABIO-RKP55217.
UniPathwayUPA00051; UER00077.

Gene expression databases

GenevestigatorP55217.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProIPR000277. Cys/Met-Metab_PyrdxlP-dep_enz.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PANTHERPTHR11808. PTHR11808. 1 hit.
PfamPF01053. Cys_Met_Meta_PP. 1 hit.
[Graphical view]
SUPFAMSSF53383. SSF53383. 1 hit.
PROSITEPS00868. CYS_MET_METAB_PP. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMETB_ARATH
AccessionPrimary (citable) accession number: P55217
Secondary accession number(s): P92944, P93038, Q42550
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: June 20, 2002
Last modified: May 14, 2014
This is version 115 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names