Reviewed, UniProtKB/Swiss-Prot Q9N0V7 (CBS_RABIT)

Names and origin

Protein names

Recommended name:
    Cystathionine beta-synthase
    EC=4.2.1.22
Alternative name(s):
    Serine sulfhydrase
    Beta-thionase

Gene names

Name:

CBS

Organism

Oryctolagus cuniculus (Rabbit)

Taxonomic identifier

9986 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Lagomorpha › Leporidae › Oryctolagus

Protein attributes

Sequence length	551 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

General annotation (Comments)

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.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Cysteine biosynthesis
Cellular component	Cytoplasm Nucleus
Domain	CBS domain
Ligand	Heme Iron Metal-binding Pyridoxal phosphate
Molecular function	Lyase
PTM	Isopeptide bond Phosphoprotein Ubl conjugation
Gene Ontology (GO)
Biological process	cysteine biosynthetic process from serine Inferred from electronic annotation. Source: InterPro cysteine biosynthetic process via cystathionine Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	cystathionine beta-synthase activity Inferred from electronic annotation. Source: EC iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 551	550	Cystathionine beta-synthase		PRO_0000263004
Regions
	Domain	418 – 476	59	CBS
	Region	256 – 260	5	Pyridoxal phosphate binding By similarity
Sites
	Metal binding	52	1	Iron (heme axial ligand) By similarity
	Metal binding	65	1	Iron (heme axial ligand) By similarity
	Binding site	149	1	Pyridoxal phosphate By similarity
	Binding site	349	1	Pyridoxal phosphate By similarity
Amino acid modifications
	Modified residue	19	1	Phosphoserine By similarity
	Modified residue	119	1	N6-(pyridoxal phosphate)lysine By similarity
	Cross-link	211		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9N0V7-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: AE14CC7EDA6BA2AD	FASTA	551	60,212
	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

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.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF248039 mRNA. Translation: AAF64226.1.
RefSeq	NP_001075551.1.
UniGene	Ocu.2436
3D structure databases
HSSP	HSSP built from PDB template 1JBQ based on UniProtKB P35520.
SMR	Q9N0V7. Positions 47-397, 412-544.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9N0V7.
Genome annotation databases
GeneID	100008766.
Organism-specific databases
CTD	100008766.
Phylogenomic databases
eggNOG	maNOG07428.
HOVERGEN	Q9N0V7.
Enzyme and pathway databases
BRENDA	4.2.1.22. 255.
Family and domain databases
InterPro	IPR001216. Cys_synth_BS. IPR005857. Cysta_beta_synth. IPR000644. Cysta_beta_synth_core. IPR001926. PyrdxlP-dep_enz_bsu. [Graphical view]
Pfam	PF00571. CBS. 1 hit. PF00291. PALP. 1 hit. [Graphical view]
SMART	SM00116. CBS. 1 hit. [Graphical view]
TIGRFAMs	TIGR01137. cysta_beta. 1 hit.
PROSITE	PS51371. CBS. 1 hit. PS00901. CYS_SYNTHASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CBS_RABIT

Accession

Primary (citable) accession number: Q9N0V7

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 28, 2006
Last sequence update:	January 23, 2007
Last modified:	February 9, 2010
This is version 46 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)