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Q9N0V7 (CBS_RABIT) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 60. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Cystathionine beta-synthase
EC=4.2.1.22
Alternative name(s):
Beta-thionase
Serine sulfhydrase
Gene names
Name:CBS
OrganismOryctolagus cuniculus (Rabbit) [Complete proteome]
Taxonomic identifier9986 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Lagomorpha › Leporidae › Oryctolagus

Protein attributes

Sequence length551 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Only known pyridoxal phosphate-dependent enzyme that contains heme. Important regulator of hydrogen sulfide, especially in the brain, utilizing cysteine instead of serine to catalyze the formation of hydrogen sulfide. Hydrogen sulfide is a gastratransmitter with signaling and cytoprotective effects such as acting as a neuromodulator in the brain to protect neurons against hypoxic injury By similarity.

Catalytic activity

L-serine + L-homocysteine = L-cystathionine + H2O.

Cofactor

Pyridoxal phosphate By similarity.

Pathway

Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine from L-homocysteine and L-serine: step 1/2.

Subunit structure

Homotetramer By similarity.

Subcellular location

Nucleus By similarity. Cytoplasm By similarity.

Post-translational modification

Binds covalently to a heme group through a thiolate ligand By similarity.

Sequence similarities

Belongs to the cysteine synthase/cystathionine beta-synthase family.

Contains 1 CBS domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 551550Cystathionine beta-synthase
PRO_0000263004

Regions

Domain418 – 47659CBS
Region256 – 2605Pyridoxal phosphate binding By similarity

Sites

Metal binding521Iron (heme axial ligand) By similarity
Metal binding651Iron (heme axial ligand) By similarity
Binding site1491Pyridoxal phosphate By similarity
Binding site3491Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue191Phosphoserine By similarity
Modified residue1191N6-(pyridoxal phosphate)lysine By similarity
Cross-link211Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9N0V7 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: AE14CC7EDA6BA2AD

FASTA55160,212
        10         20         30         40         50         60 
MPSETAQAGE GPAGCPHLSG AQGSDRSLDQ RPPGNKDAPE RVWIRPDVPS RCTWELGRPV 

        70         80         90        100        110        120 
ADSPHQHAAL AKSPKILPDI LQKIGDTPMV RINKIGKNFG LKCELLAKCE FFNAGGSVKD 

       130        140        150        160        170        180 
RISLRMIEDA ERAGTLRPGD TIIEPTSGNT GIGLALAAAV KGYRCIIVMP EKMSLEKVDV 

       190        200        210        220        230        240 
LRALGAEIVR TPTNARFDSP ESHVGVAWRL KQEIPNSHIL DQYRNASNPL AHYDTTAEEI 

       250        260        270        280        290        300 
LQQCDGKLDM LVASAGTGGT ITGIARKLKE KCPGCQIIGV DPEGSILAEP EELNQTEVTA 

       310        320        330        340        350        360 
YEVEGIGYDF IPTVLDRTVV DRWFKSTDKE AFAFARMLIA QEGLLCGGSA GSAVAVAVKA 

       370        380        390        400        410        420 
AQELQEGQRC VVILPDSVRN YMSKFLSDRW MLQKGFLEEE ELSVKRPWWW HLRVQELSLS 

       430        440        450        460        470        480 
VPLTVLPGVT CSDTIDILRG KGFDQAPVVD ETGEILGMVT LGNMLSSLLA GKVQPSDQVC 

       490        500        510        520        530        540 
KVLYKQFKQI RLTDTLGALS HILEMDHFAL VVHEQIQYGG DEQPSKRQTV FGVVTAMDLL 

       550 
HFVASRGQDQ Q

« Hide

References

[1]"Cloning and characterization of a cDNA clone of rabbit cystathionine beta synthase."
Fujiwara K., Matsuda J., Tokunaga T.
Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF248039 mRNA. Translation: AAF64226.1.
RefSeqNP_001075551.1. NM_001082082.1.
UniGeneOcu.2436.

3D structure databases

HSSPHSSP built from PDB template 1JBQ based on UniProtKB P35520.
ProteinModelPortalQ9N0V7.
SMRQ9N0V7. Positions 47-397.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ9N0V7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100008766.

Organism-specific databases

CTD875.

Phylogenomic databases

eggNOGmaNOG07428.
GeneTreeENSGT00510000047027.
HOVERGENHBG000918.
OrthoDBEOG4Z36DG.

Family and domain databases

InterProIPR001216. Cys_synth_BS.
IPR005857. Cysta_beta_synth.
IPR000644. Cysta_beta_synth_core.
IPR001926. PyrdxlP-dep_enz_bsu.
[Graphical view]
PfamPF00571. CBS. 1 hit.
PF00291. PALP. 1 hit.
[Graphical view]
SMARTSM00116. CBS. 1 hit.
[Graphical view]
SUPFAMSSF53686. PyrdxlP-dep_enz_bsu. 1 hit.
TIGRFAMsTIGR01137. Cysta_beta. 1 hit.
PROSITEPS51371. CBS. 1 hit.
PS00901. CYS_SYNTHASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCBS_RABIT
AccessionPrimary (citable) accession number: Q9N0V7
Entry history
Integrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: January 23, 2007
Last modified: November 16, 2011
This is version 60 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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