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Protein

Cystathionine beta-synthase

Gene

CBS

Organism
Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Hydro-lyase catalyzing the first step of the transsulfuration pathway, where the hydroxyl group of L-serine is displaced by L-homocysteine in a beta-replacement reaction to form L-cystathionine, the precursor of L-cysteine. This catabolic route allows the elimination of L-methionine and the toxic metabolite L-homocysteine (By similarity). Also involved in the production of hydrogen sulfide, a gasotransmitter with signaling and cytoprotective effects on neurons (By similarity).By similarity

Catalytic activityi

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

Cofactori

pyridoxal 5'-phosphateBy similarity

Enzyme regulationi

Allosterically activated by S-adenosyl-methionine/AdoMet. Activated by S-adenosylhomocysteine/AdoHcy. Binds non-covalently to a heme group that may control the redox sensitivity of the enzyme.By similarity

Pathwayi: L-cysteine biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes L-cysteine from L-homocysteine and L-serine.By similarity
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Cystathionine beta-synthase (CBS)
  2. Cystathionine gamma-lyase (CTH)
This subpathway is part of the pathway L-cysteine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-cysteine from L-homocysteine and L-serine, the pathway L-cysteine biosynthesis and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi52 – 521Iron (heme axial ligand)By similarity
Metal bindingi65 – 651Iron (heme axial ligand)By similarity
Binding sitei149 – 1491Pyridoxal phosphateBy similarity
Binding sitei349 – 3491Pyridoxal phosphateBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Amino-acid biosynthesis, Cysteine biosynthesis

Keywords - Ligandi

Heme, Iron, Metal-binding, Pyridoxal phosphate

Enzyme and pathway databases

UniPathwayiUPA00136; UER00201.

Names & Taxonomyi

Protein namesi
Recommended name:
Cystathionine beta-synthaseCurated (EC:4.2.1.22By similarity)
Alternative name(s):
Beta-thionase
Serine sulfhydrase
Gene namesi
Name:CBS
OrganismiMacaca fascicularis (Crab-eating macaque) (Cynomolgus monkey)
Taxonomic identifieri9541 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniCercopithecidaeCercopithecinaeMacaca

Subcellular locationi

  • Cytoplasm By similarity
  • Nucleus By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 551550Cystathionine beta-synthasePRO_0000263003Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei27 – 271PhosphoserineBy similarity
Modified residuei119 – 1191N6-(pyridoxal phosphate)lysineBy similarity
Cross-linki211 – 211Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PRIDEiQ58H57.

Interactioni

Subunit structurei

Homotetramer.By similarity

GO - Molecular functioni

Structurei

3D structure databases

ProteinModelPortaliQ58H57.
SMRiQ58H57. Positions 47-397.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini418 – 47659CBSPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni256 – 2605Pyridoxal phosphate bindingBy similarity

Sequence similaritiesi

Contains 1 CBS domain.PROSITE-ProRule annotation

Keywords - Domaini

CBS domain

Phylogenomic databases

HOVERGENiHBG000918.
KOiK01697.

Family and domain databases

InterProiIPR000644. CBS_dom.
IPR005857. Cysta_beta_synth.
IPR001216. P-phosphate_BS.
IPR001926. TrpB-like_PLP-dep.
[Graphical view]
PfamiPF00571. CBS. 1 hit.
PF00291. PALP. 1 hit.
[Graphical view]
SMARTiSM00116. CBS. 1 hit.
[Graphical view]
SUPFAMiSSF53686. SSF53686. 1 hit.
TIGRFAMsiTIGR01137. cysta_beta. 1 hit.
PROSITEiPS51371. CBS. 1 hit.
PS00901. CYS_SYNTHASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q58H57-1 [UniParc]FASTAAdd to basket

« Hide

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

K
Length:551
Mass (Da):60,721
Last modified:January 23, 2007 - v3
Checksum:iDCFA5E0F1E68A45B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY952460 mRNA. Translation: AAX51303.1.
RefSeqiNP_001270081.1. NM_001283152.1.
UniGeneiMfa.3905.

Genome annotation databases

GeneIDi102115084.
KEGGimcf:102115084.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY952460 mRNA. Translation: AAX51303.1.
RefSeqiNP_001270081.1. NM_001283152.1.
UniGeneiMfa.3905.

3D structure databases

ProteinModelPortaliQ58H57.
SMRiQ58H57. Positions 47-397.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiQ58H57.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi102115084.
KEGGimcf:102115084.

Organism-specific databases

CTDi875.

Phylogenomic databases

HOVERGENiHBG000918.
KOiK01697.

Enzyme and pathway databases

UniPathwayiUPA00136; UER00201.

Family and domain databases

InterProiIPR000644. CBS_dom.
IPR005857. Cysta_beta_synth.
IPR001216. P-phosphate_BS.
IPR001926. TrpB-like_PLP-dep.
[Graphical view]
PfamiPF00571. CBS. 1 hit.
PF00291. PALP. 1 hit.
[Graphical view]
SMARTiSM00116. CBS. 1 hit.
[Graphical view]
SUPFAMiSSF53686. SSF53686. 1 hit.
TIGRFAMsiTIGR01137. cysta_beta. 1 hit.
PROSITEiPS51371. CBS. 1 hit.
PS00901. CYS_SYNTHASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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].

Entry informationi

Entry nameiCBS_MACFA
AccessioniPrimary (citable) accession number: Q58H57
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: January 23, 2007
Last modified: December 9, 2015
This is version 60 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.