Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Cystathionine beta-synthase

Gene

CBS

Organism
Oryctolagus cuniculus (Rabbit)
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. no protein annotated in this organism
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)DescriptionActionsGraphical viewLength
Metal bindingi52Iron (heme axial ligand)By similarity1
Metal bindingi65Iron (heme axial ligand)By similarity1
Binding sitei149Pyridoxal phosphateBy similarity1
Binding sitei349Pyridoxal phosphateBy similarity1

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
OrganismiOryctolagus cuniculus (Rabbit)
Taxonomic identifieri9986 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
Proteomesi
  • UP000001811 Componenti: Unplaced

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)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00002630042 – 551Cystathionine beta-synthaseAdd BLAST550

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei27PhosphoserineBy similarity1
Modified residuei119N6-(pyridoxal phosphate)lysineBy similarity1
Modified residuei199PhosphoserineBy similarity1
Cross-linki211Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Interactioni

Subunit structurei

Homotetramer.By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000015163.

Structurei

3D structure databases

ProteinModelPortaliQ9N0V7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini418 – 476CBSPROSITE-ProRule annotationAdd BLAST59

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni256 – 260Pyridoxal phosphate bindingBy similarity5

Sequence similaritiesi

Contains 1 CBS domain.PROSITE-ProRule annotation

Keywords - Domaini

CBS domain

Phylogenomic databases

eggNOGiKOG1252. Eukaryota.
COG0031. LUCA.
HOGENOMiHOG000217392.
HOVERGENiHBG000918.
InParanoidiQ9N0V7.
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.

Q9N0V7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPSETAQAGE GPAGCPHLSG AQGSDRSLDQ RPPGNKDAPE RVWIRPDVPS
60 70 80 90 100
RCTWELGRPV ADSPHQHAAL AKSPKILPDI LQKIGDTPMV RINKIGKNFG
110 120 130 140 150
LKCELLAKCE FFNAGGSVKD RISLRMIEDA ERAGTLRPGD TIIEPTSGNT
160 170 180 190 200
GIGLALAAAV KGYRCIIVMP EKMSLEKVDV LRALGAEIVR TPTNARFDSP
210 220 230 240 250
ESHVGVAWRL KQEIPNSHIL DQYRNASNPL AHYDTTAEEI LQQCDGKLDM
260 270 280 290 300
LVASAGTGGT ITGIARKLKE KCPGCQIIGV DPEGSILAEP EELNQTEVTA
310 320 330 340 350
YEVEGIGYDF IPTVLDRTVV DRWFKSTDKE AFAFARMLIA QEGLLCGGSA
360 370 380 390 400
GSAVAVAVKA AQELQEGQRC VVILPDSVRN YMSKFLSDRW MLQKGFLEEE
410 420 430 440 450
ELSVKRPWWW HLRVQELSLS VPLTVLPGVT CSDTIDILRG KGFDQAPVVD
460 470 480 490 500
ETGEILGMVT LGNMLSSLLA GKVQPSDQVC KVLYKQFKQI RLTDTLGALS
510 520 530 540 550
HILEMDHFAL VVHEQIQYGG DEQPSKRQTV FGVVTAMDLL HFVASRGQDQ

Q
Length:551
Mass (Da):60,212
Last modified:January 23, 2007 - v3
Checksum:iAE14CC7EDA6BA2AD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF248039 mRNA. Translation: AAF64226.1.
RefSeqiNP_001075551.1. NM_001082082.2.
UniGeneiOcu.2436.

Genome annotation databases

GeneIDi100008766.
KEGGiocu:100008766.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF248039 mRNA. Translation: AAF64226.1.
RefSeqiNP_001075551.1. NM_001082082.2.
UniGeneiOcu.2436.

3D structure databases

ProteinModelPortaliQ9N0V7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000015163.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi100008766.
KEGGiocu:100008766.

Organism-specific databases

CTDi875.

Phylogenomic databases

eggNOGiKOG1252. Eukaryota.
COG0031. LUCA.
HOGENOMiHOG000217392.
HOVERGENiHBG000918.
InParanoidiQ9N0V7.
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...

Entry informationi

Entry nameiCBS_RABIT
AccessioniPrimary (citable) accession number: Q9N0V7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: January 23, 2007
Last modified: October 5, 2016
This is version 85 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

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.