Reviewed, UniProtKB/Swiss-Prot Q58H57 (CBS_MACFA)

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

Macaca fascicularis (Crab eating macaque) (Cynomolgus monkey)

Taxonomic identifier

9541 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Cercopithecidae › Cercopithecinae › Macaca

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 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_0000263003
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	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)
	Q58H57-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: DCFA5E0F1E68A45B	FASTA	551	60,721
	10 20 30 40 50 60 MPSETPQAEV GPTGCPHLSG PHSAQGSLEK GLPGDKEAKE PLWIRPDAPS RCTWQLGRPA 70 80 90 100 110 120 SESPHHHTVP EKSPKILPDI LKKIGDTPMI RINKIGKKFG LKCELLAKCE FFNAGGSVKD 130 140 150 160 170 180 RISLRMIEDA ERAGTLKPGD TIIEPTSGNT GIGLALTAAV RGYRCIIVMP EKMSSEKVDV 190 200 210 220 230 240 LRALGAEIVR TPTNARFDSP ESHVGVAWRL KNEIPNSHIL DQYRNASNPL AHYDTTADEI 250 260 270 280 290 300 LRQCDGKLDM LVASVGTGGT ITGIARKLKE KCPGCRIIGV DPEGSILAEP EELNQTEQTT 310 320 330 340 350 360 YEVEGIGYDF IPTVLDRTVV DKWFKSNDEE AFTFARMLIA QEGLLCGGSA GSTMAVAVKA 370 380 390 400 410 420 AQELQEGQRC VVILPDSVRN YMTKFLSDRW MLQKGFLKEE DLMEKKPWWW HLRVQELSLS 430 440 450 460 470 480 APLTVLPTVS CEHTIEILRE KGFDQAPVVD EAGVILGMVT LGNMLSSLLA GKVQPSDQVG 490 500 510 520 530 540 KVIYTQFKQI RLTDTLGRLS HILEMDHFAL VVHEQIQYHS TGKSSQRQMV FGVVTAIDLL 550 NFVAAQERDQ K

References

[1]

"Dual effects of hydrogen sulphide on vascular system in anesthetized monkeys in vivo and cloning, characterization of cystathionine-beta-synthase." Zhu Y.Z., Wang Z.J., Duan W., Ling L.H., Zhu Y.C., Yang H., Huang S.H., Tan C.S., Whiteman M., Moore P.K. Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AY952460 mRNA. Translation: AAX51303.1.
3D structure databases
SMR	Q58H57. Positions 43-399.
ModBase	Search...
Phylogenomic databases
HOVERGEN	Q58H57.
Enzyme and pathway databases
BRENDA	4.2.1.22. 3438.
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_MACFA

Accession

Primary (citable) accession number: Q58H57

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 28, 2006
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 28 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)