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Q07703 (METC_BORAV) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 72. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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 beta-lyase

Short name=CBL
EC=4.4.1.8
Alternative name(s):
Beta-cystathionase
Cysteine lyase
Osteotoxin
Gene names
Name:metC
OrganismBordetella avium
Taxonomic identifier521 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesAlcaligenaceaeBordetella

Protein attributes

Sequence length396 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Also has cytotoxic activity toward osteogenic, osteosarcoma and tracheal cells, in vitro. The chemical basis for cell toxicity might be the formation and subsequent transfer of sulfane-sulfur to proteins, derived via beta-cystathionase cleavage of L-cystine.

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

Homodimer.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the trans-sulfuration enzymes family.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Methionine biosynthesis
   Cellular componentCytoplasm
   LigandPyridoxal phosphate
   Molecular functionLyase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological_processmethionine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncystathionine beta-lyase activity

Inferred from electronic annotation. Source: EC

pyridoxal phosphate binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.1
Chain2 – 396395Cystathionine beta-lyase
PRO_0000114767

Amino acid modifications

Modified residue2141N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q07703 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: F0D11DA6E108F064

FASTA39642,610
        10         20         30         40         50         60 
MSDTSAKHID TLLQHLGSAP FNPDTGAAPV NLPSVRASTV RFQSLAKLED AQRRKAAGER 

        70         80         90        100        110        120 
ASTYGRMGMD THAALEQVFA ELEGGTHCYL ASSGLAGISM VFLSLLSAGE HALVADCAYG 

       130        140        150        160        170        180 
PVHELHEAVL SRLGIDVTFF DAKADLASLV RPTTRLIFAE APGSLLFEML DMPALARFAK 

       190        200        210        220        230        240 
QHDLILATDN TWGSGYIYRP LTLGAQVSVI AGTKYVGGHS DLMLGAVVTN DEAIAKRLNR 

       250        260        270        280        290        300 
TQYALGYSVS ADDAWLALRG VRTMPVRMAQ HARHALEVCE FLQNRPEVVR LYHPAWPADP 

       310        320        330        340        350        360 
GHALWQRDCS GSNGMLAVQL GLSPQAARDF VNALTLFGIG FSWGGFESLV QLVTPGELAR 

       370        380        390 
HQYWQGGSDA LVRLHIGLES PADLIADLAQ ALDRAA 

« Hide

References

[1]"Toxicity of Bordetella avium beta-cystathionase toward MC3T3-E1 osteogenic cells."
Gentry-Weeks C.R., Keith J.M., Thompson J.
J. Biol. Chem. 268:7298-7314(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-33.
Strain: 197.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L10425 Genomic DNA. Translation: AAA22978.1.
PIRA46084.

3D structure databases

ProteinModelPortalQ07703.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00051; UER00078.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProIPR000277. Cys/Met-Metab_PyrdxlP-dep_enz.
IPR006233. Cys_b_lyase_bac.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PANTHERPTHR11808. PTHR11808. 1 hit.
PTHR11808:SF8. PTHR11808:SF8. 1 hit.
PfamPF01053. Cys_Met_Meta_PP. 1 hit.
[Graphical view]
PIRSFPIRSF001434. CGS. 1 hit.
SUPFAMSSF53383. PyrdxlP-dep_Trfase_major. 1 hit.
TIGRFAMsTIGR01324. cysta_beta_ly_B. 1 hit.
PROSITEPS00868. CYS_MET_METAB_PP. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMETC_BORAV
AccessionPrimary (citable) accession number: Q07703
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: January 23, 2007
Last modified: April 3, 2013
This is version 72 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families