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P53780 (METC_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 112. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Cystathionine beta-lyase, chloroplastic

Short name=CBL
EC=4.4.1.8
Alternative name(s):
Beta-cystathionase
Cysteine lyase
Gene names
Ordered Locus Names:At3g57050
ORF Names:F24I3.130
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length464 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

L-cystathionine + H2O = L-homocysteine + NH3 + pyruvate.

Cofactor

Pyridoxal phosphate.

Pathway

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

Subunit structure

Homotetramer. Ref.5

Subcellular location

Plastidchloroplast.

Sequence similarities

Belongs to the trans-sulfuration enzymes family.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P53780-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P53780-2)

The sequence of this isoform differs from the canonical sequence as follows:
     63-78: GQTHSTVNNTTDSLNT → A
Note: May be due to a competing donor splice site.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – ?Chloroplast Potential
Chain? – 464Cystathionine beta-lyase, chloroplasticPRO_0000033454

Amino acid modifications

Modified residue2781N6-(pyridoxal phosphate)lysine

Natural variations

Alternative sequence63 – 7816GQTHS…DSLNT → A in isoform 2.
VSP_008894

Secondary structure

....................................................................... 464
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: DE756848549D2CA6

FASTA46450,430
        10         20         30         40         50         60 
MTSSLSLHSS FVPSFADLSD RGLISKNSPT SVSISKVPTW EKKQISNRNS FKLNCVMEKS 

        70         80         90        100        110        120 
VDGQTHSTVN NTTDSLNTMN IKEEASVSTL LVNLDNKFDP FDAMSTPLYQ TATFKQPSAI 

       130        140        150        160        170        180 
ENGPYDYTRS GNPTRDALES LLAKLDKADR AFCFTSGMAA LSAVTHLIKN GEEIVAGDDV 

       190        200        210        220        230        240 
YGGSDRLLSQ VVPRSGVVVK RVNTTKLDEV AAAIGPQTKL VWLESPTNPR QQISDIRKIS 

       250        260        270        280        290        300 
EMAHAQGALV LVDNSIMSPV LSRPLELGAD IVMHSATKFI AGHSDVMAGV LAVKGEKLAK 

       310        320        330        340        350        360 
EVYFLQNSEG SGLAPFDCWL CLRGIKTMAL RIEKQQENAR KIAMYLSSHP RVKKVYYAGL 

       370        380        390        400        410        420 
PDHPGHHLHF SQAKGAGSVF SFITGSVALS KHLVETTKYF SIAVSFGSVK SLISMPCFMS 

       430        440        450        460 
HASIPAEVRE ARGLTEDLVR ISAGIEDVDD LISDLDIAFK TFPL 

« Hide

Isoform 2 [UniParc].

Checksum: BBE2BE332C25314B
Show »

FASTA44948,829

References

« Hide 'large scale' references
[1]"Cloning of an Arabidopsis thaliana cDNA encoding cystathionine beta-lyase by functional complementation in Escherichia coli."
Ravanel S., Ruffet M.L., Douce R.
Plant Mol. Biol. 29:875-882(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Strain: cv. Columbia.
[2]"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.
[3]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[4]"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] (ISOFORM 2).
Strain: cv. Columbia.
[5]"The three-dimensional structure of cystathionine beta-lyase from Arabidopsis and its substrate specificity."
Breitinger U., Clausen T., Ehlert S., Huber R., Laber B., Schmidt F., Pohl E., Messerschmidt A.
Plant Physiol. 126:631-642(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 85-464, SUBUNIT, PYRIDOXAL PHOSPHATE AT LYS-278.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L40511 mRNA. Translation: AAA99176.1.
AL138655 Genomic DNA. Translation: CAB72175.1.
CP002686 Genomic DNA. Translation: AEE79603.1.
CP002686 Genomic DNA. Translation: AEE79605.1.
AY064018 mRNA. Translation: AAL36374.1.
AY114051 mRNA. Translation: AAM45099.1.
IPIIPI00528229.
IPI00532593.
PIRS61429.
RefSeqNP_191264.1. NM_115564.3.
NP_850712.1. NM_180381.2.
UniGeneAt.24673.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1IBJX-ray2.30A/C1-464[»]
ProteinModelPortalP53780.
SMRP53780. Positions 85-464.
ModBaseSearch...

Protein-protein interaction databases

IntActP53780. 2 interactions.

Proteomic databases

PaxDbP53780.
PRIDEP53780.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT3G57050.1; AT3G57050.1; AT3G57050.
GeneID824872.
KEGGath:AT3G57050.

Organism-specific databases

TAIRAt3g57050.

Phylogenomic databases

eggNOGCOG0626.
HOGENOMHOG000246415.
InParanoidP53780.
KOK01760.
OMAALMTHGS.
PhylomeDBP53780.
ProtClustDBPLN02509.

Enzyme and pathway databases

BioCycMetaCyc:AT3G57050-MONOMER.
UniPathwayUPA00051; UER00078.

Gene expression databases

ArrayExpressP53780.
GenevestigatorP53780.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProIPR000277. Cys/Met-Metab_PyrdxlP-dep_enz.
IPR006238. Cys_b_lyase_euk.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PANTHERPTHR11808. PTHR11808. 1 hit.
PTHR11808:SF18. PTHR11808:SF18. 1 hit.
PfamPF01053. Cys_Met_Meta_PP. 1 hit.
[Graphical view]
PIRSFPIRSF001434. CGS. 1 hit.
SUPFAMSSF53383. PyrdxlP-dep_Trfase_major. 1 hit.
TIGRFAMsTIGR01329. cysta_beta_ly_E. 1 hit.
PROSITEPS00868. CYS_MET_METAB_PP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP53780.

Entry information

Entry nameMETC_ARATH
AccessionPrimary (citable) accession number: P53780
Secondary accession number(s): Q8VZL8
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: May 1, 2013
This is version 112 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families