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Protein

Cystathionine gamma-lyase

Gene

Cth

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Catalyzes the last step in the trans-sulfuration pathway from methionine to cysteine. Has broad substrate specificity. Converts cystathionine to cysteine, ammonia and 2-oxobutanoate. Converts two cysteine molecules to lanthionine and hydrogen sulfide. Can also accept homocysteine as substrate. Specificity depends on the levels of the endogenous substrates. Generates the endogenous signaling molecule hydrogen sulfide (H2S), and so contributes to the regulation of blood pressure. Acts as a cysteine-protein sulfhydrase by mediating sulfhydration of target proteins: sulfhydration consists of converting -SH groups into -SSH on specific cysteine residues of target proteins such as GAPDH, PTPN1 and NF-kappa-B subunit RELA, thereby regulating their function (By similarity).By similarity

Catalytic activityi

L-cystathionine + H2O = L-cysteine + NH3 + 2-oxobutanoate.

Cofactori

Pathwayi: L-cysteine biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes L-cysteine from L-homocysteine and L-serine.
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)DescriptionActionsGraphical viewLength
Binding sitei61SubstrateBy similarity1
Binding sitei113SubstrateBy similarity1
Binding sitei118SubstrateBy similarity1
Binding sitei338SubstrateBy similarity1

GO - Molecular functioni

GO - Biological processi

  • 'de novo' L-methionine biosynthetic process Source: GO_Central
  • cysteine biosynthetic process Source: RGD
  • cysteine biosynthetic process via cystathionine Source: GO_Central
  • glutathione metabolic process Source: RGD
  • homocysteine metabolic process Source: RGD
  • hydrogen sulfide biosynthetic process Source: UniProtKB
  • negative regulation of apoptotic process Source: UniProtKB
  • negative regulation of cell growth Source: RGD
  • negative regulation of cell proliferation Source: RGD
  • positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
  • positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
  • protein-pyridoxal-5-phosphate linkage via peptidyl-N6-pyridoxal phosphate-L-lysine Source: UniProtKB
  • protein sulfhydration Source: UniProtKB
  • transsulfuration Source: RGD

Keywordsi

Molecular functionCalmodulin-binding, Lyase
Biological processAmino-acid biosynthesis, Cysteine biosynthesis
LigandPyridoxal phosphate

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-8584
UniPathwayiUPA00136; UER00202

Names & Taxonomyi

Protein namesi
Recommended name:
Cystathionine gamma-lyase (EC:4.4.1.1)
Alternative name(s):
Cysteine-protein sulfhydrase
Gamma-cystathionase
Probasin-related antigen
Short name:
PRB-RA
Gene namesi
Name:Cth
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi2443 Cth

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001147521 – 398Cystathionine gamma-lyaseAdd BLAST398

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei50PhosphoserineCombined sources1
Modified residuei211N6-(pyridoxal phosphate)lysine1

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP18757
PRIDEiP18757

PTM databases

iPTMnetiP18757
PhosphoSitePlusiP18757

Interactioni

Subunit structurei

Homotetramer. Interacts with CALM in a calcium-dependent manner (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000058914

Structurei

3D structure databases

ProteinModelPortaliP18757
SMRiP18757
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the trans-sulfuration enzymes family.Curated

Phylogenomic databases

eggNOGiKOG0053 Eukaryota
COG0626 LUCA
HOGENOMiHOG000246415
HOVERGENiHBG005322
InParanoidiP18757
KOiK01758
PhylomeDBiP18757

Family and domain databases

CDDicd00614 CGS_like, 1 hit
Gene3Di3.40.640.10, 1 hit
3.90.1150.10, 1 hit
InterProiView protein in InterPro
IPR000277 Cys/Met-Metab_PyrdxlP-dep_enz
IPR015424 PyrdxlP-dep_Trfase
IPR015422 PyrdxlP-dep_Trfase_dom1
IPR015421 PyrdxlP-dep_Trfase_major
PANTHERiPTHR11808 PTHR11808, 1 hit
PfamiView protein in Pfam
PF01053 Cys_Met_Meta_PP, 1 hit
PIRSFiPIRSF001434 CGS, 1 hit
SUPFAMiSSF53383 SSF53383, 1 hit
PROSITEiView protein in PROSITE
PS00868 CYS_MET_METAB_PP, 1 hit

Sequencei

Sequence statusi: Complete.

P18757-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQKDASSSGF LPSFQHFATQ AIHVGPEPEQ WSSRAVVLPI SLATTFKQDS
60 70 80 90 100
PGQSSGFVYS RSGNPTRNCL EKAVAALDGA KHCLTFARGL AATTTITHLL
110 120 130 140 150
KAGDEVICMD EVYGGTNRYF RRVASEFGLK ISFVDCSKTK LLEAAITPQT
160 170 180 190 200
KLVWIETPTN PTLKLADIKA CAQIVHKHKD IILVVDNTFM SAYFQRPLAL
210 220 230 240 250
GADICMCSAT KYMNGHSDVV MGLVSVTSDD LNERLRFLQN SLGAVPSPFD
260 270 280 290 300
CYLCCRGLKT LQIRMEKHFR NGMAVARFLE SNPRVEKVIY PGLPSHPQHE
310 320 330 340 350
LAKRQCTGCP GMVSFYIKGT LQHAQVFLKN IKLFALAESL GGYESLAELP
360 370 380 390
AIMTHASVPE KDRATLGISD TLIRLSVGLE DEKDLLEDLG QALKAAHP
Length:398
Mass (Da):43,605
Last modified:October 1, 1996 - v2
Checksum:iC6043988B03D725F
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti35 – 41AVVLPIS → CCGAAH AA sequence (PubMed:2201285).Curated7
Sequence conflicti227T → N in CAA37547 (PubMed:2201285).Curated1
Sequence conflicti260 – 271TLQIR…KHFRN → HCRSGWRNTFQD in CAA37547 (PubMed:2201285).CuratedAdd BLAST12
Sequence conflicti305 – 308QCTG → SARA in CAA37547 (PubMed:2201285).Curated4

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D17370 mRNA Translation: BAA04189.1
X53460 mRNA Translation: CAA37547.1
PIRiA49864
RefSeqiNP_058770.1, NM_017074.1
UniGeneiRn.3881

Genome annotation databases

GeneIDi24962
KEGGirno:24962

Similar proteinsi

Entry informationi

Entry nameiCGL_RAT
AccessioniPrimary (citable) accession number: P18757
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: October 1, 1996
Last modified: May 23, 2018
This is version 140 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

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