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Cystathionine beta-synthase (EC 4.2.1.22) (Beta-thionase) (Serine sulfhydrase)

 CBS_RABIT               Reviewed;         551 AA.
Q9N0V7;
28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
25-OCT-2017, entry version 89.
RecName: Full=Cystathionine beta-synthase {ECO:0000305};
EC=4.2.1.22 {ECO:0000250|UniProtKB:P35520};
AltName: Full=Beta-thionase;
AltName: Full=Serine sulfhydrase;
Name=CBS;
Oryctolagus cuniculus (Rabbit).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae;
Oryctolagus.
NCBI_TaxID=9986;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
Fujiwara K., Matsuda J., Tokunaga T.;
"Cloning and characterization of a cDNA clone of rabbit cystathionine
beta synthase.";
Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: 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).
{ECO:0000250|UniProtKB:P32232, ECO:0000250|UniProtKB:P35520}.
-!- CATALYTIC ACTIVITY: L-serine + L-homocysteine = L-cystathionine +
H(2)O. {ECO:0000250|UniProtKB:P35520}.
-!- COFACTOR:
Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
Evidence={ECO:0000250|UniProtKB:P35520};
-!- ENZYME REGULATION: 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. {ECO:0000250|UniProtKB:P35520}.
-!- PATHWAY: Amino-acid biosynthesis; L-cysteine biosynthesis; L-
cysteine from L-homocysteine and L-serine: step 1/2.
{ECO:0000250|UniProtKB:P35520}.
-!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P35520}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P35520}.
Nucleus {ECO:0000250|UniProtKB:P35520}.
-!- SIMILARITY: Belongs to the cysteine synthase/cystathionine beta-
synthase family. {ECO:0000305}.
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EMBL; AF248039; AAF64226.1; -; mRNA.
RefSeq; NP_001075551.1; NM_001082082.2.
UniGene; Ocu.2436; -.
ProteinModelPortal; Q9N0V7; -.
SMR; Q9N0V7; -.
STRING; 9986.ENSOCUP00000015163; -.
GeneID; 100008766; -.
KEGG; ocu:100008766; -.
CTD; 875; -.
eggNOG; KOG1252; Eukaryota.
eggNOG; COG0031; LUCA.
HOGENOM; HOG000217392; -.
HOVERGEN; HBG000918; -.
InParanoid; Q9N0V7; -.
KO; K01697; -.
UniPathway; UPA00136; UER00201.
Proteomes; UP000001811; Unplaced.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0004122; F:cystathionine beta-synthase activity; ISS:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
GO; GO:0030170; F:pyridoxal phosphate binding; ISS:UniProtKB.
GO; GO:0006535; P:cysteine biosynthetic process from serine; IEA:InterPro.
GO; GO:0019343; P:cysteine biosynthetic process via cystathionine; IEA:InterPro.
GO; GO:0043418; P:homocysteine catabolic process; ISS:UniProtKB.
GO; GO:0050667; P:homocysteine metabolic process; ISS:UniProtKB.
GO; GO:0070814; P:hydrogen sulfide biosynthetic process; ISS:UniProtKB.
GO; GO:0006563; P:L-serine metabolic process; ISS:UniProtKB.
InterPro; IPR000644; CBS_dom.
InterPro; IPR005857; Cysta_beta_synth.
InterPro; IPR001216; P-phosphate_BS.
InterPro; IPR001926; PLP-dep.
InterPro; IPR036052; Trypto_synt_PLP_dependent.
Pfam; PF00571; CBS; 1.
Pfam; PF00291; PALP; 1.
SMART; SM00116; CBS; 1.
SUPFAM; SSF53686; SSF53686; 1.
TIGRFAMs; TIGR01137; cysta_beta; 1.
PROSITE; PS51371; CBS; 1.
PROSITE; PS00901; CYS_SYNTHASE; 1.
2: Evidence at transcript level;
Amino-acid biosynthesis; CBS domain; Complete proteome;
Cysteine biosynthesis; Cytoplasm; Heme; Iron; Isopeptide bond; Lyase;
Metal-binding; Nucleus; Phosphoprotein; Pyridoxal phosphate;
Reference proteome; Ubl conjugation.
CHAIN 1 551 Cystathionine beta-synthase.
/FTId=PRO_0000263004.
DOMAIN 418 476 CBS. {ECO:0000255|PROSITE-
ProRule:PRU00703}.
REGION 256 260 Pyridoxal phosphate binding.
{ECO:0000250|UniProtKB:P35520}.
METAL 52 52 Iron (heme axial ligand).
{ECO:0000250|UniProtKB:P35520}.
METAL 65 65 Iron (heme axial ligand).
{ECO:0000250|UniProtKB:P35520}.
BINDING 149 149 Pyridoxal phosphate.
{ECO:0000250|UniProtKB:P35520}.
BINDING 349 349 Pyridoxal phosphate.
{ECO:0000250|UniProtKB:P35520}.
MOD_RES 27 27 Phosphoserine.
{ECO:0000250|UniProtKB:P35520}.
MOD_RES 119 119 N6-(pyridoxal phosphate)lysine.
{ECO:0000250|UniProtKB:P35520}.
MOD_RES 199 199 Phosphoserine.
{ECO:0000250|UniProtKB:P35520}.
CROSSLNK 211 211 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000250|UniProtKB:P35520}.
SEQUENCE 551 AA; 60212 MW; AE14CC7EDA6BA2AD CRC64;
MPSETAQAGE GPAGCPHLSG AQGSDRSLDQ RPPGNKDAPE RVWIRPDVPS RCTWELGRPV
ADSPHQHAAL AKSPKILPDI LQKIGDTPMV RINKIGKNFG LKCELLAKCE FFNAGGSVKD
RISLRMIEDA ERAGTLRPGD TIIEPTSGNT GIGLALAAAV KGYRCIIVMP EKMSLEKVDV
LRALGAEIVR TPTNARFDSP ESHVGVAWRL KQEIPNSHIL DQYRNASNPL AHYDTTAEEI
LQQCDGKLDM LVASAGTGGT ITGIARKLKE KCPGCQIIGV DPEGSILAEP EELNQTEVTA
YEVEGIGYDF IPTVLDRTVV DRWFKSTDKE AFAFARMLIA QEGLLCGGSA GSAVAVAVKA
AQELQEGQRC VVILPDSVRN YMSKFLSDRW MLQKGFLEEE ELSVKRPWWW HLRVQELSLS
VPLTVLPGVT CSDTIDILRG KGFDQAPVVD ETGEILGMVT LGNMLSSLLA GKVQPSDQVC
KVLYKQFKQI RLTDTLGALS HILEMDHFAL VVHEQIQYGG DEQPSKRQTV FGVVTAMDLL
HFVASRGQDQ Q


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