CBS_MACFA
ID CBS_MACFA Reviewed; 551 AA.
AC Q58H57;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Cystathionine beta-synthase {ECO:0000305};
DE EC=4.2.1.22 {ECO:0000250|UniProtKB:P35520};
DE AltName: Full=Beta-thionase;
DE AltName: Full=Serine sulfhydrase;
GN Name=CBS;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Zhu Y.Z., Wang Z.J., Duan W., Ling L.H., Zhu Y.C., Yang H., Huang S.H.,
RA Tan C.S., Whiteman M., Moore P.K.;
RT "Dual effects of hydrogen sulphide on vascular system in anesthetized
RT monkeys in vivo and cloning, characterization of cystathionine-beta-
RT synthase.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Hydro-lyase catalyzing the first step of the transsulfuration
CC pathway, where the hydroxyl group of L-serine is displaced by L-
CC homocysteine in a beta-replacement reaction to form L-cystathionine,
CC the precursor of L-cysteine. This catabolic route allows the
CC elimination of L-methionine and the toxic metabolite L-homocysteine (By
CC similarity). Also involved in the production of hydrogen sulfide, a
CC gasotransmitter with signaling and cytoprotective effects on neurons
CC (By similarity). {ECO:0000250|UniProtKB:P32232,
CC ECO:0000250|UniProtKB:P35520}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-homocysteine + L-serine = H2O + L,L-cystathionine;
CC Xref=Rhea:RHEA:10112, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384,
CC ChEBI:CHEBI:58161, ChEBI:CHEBI:58199; EC=4.2.1.22;
CC Evidence={ECO:0000250|UniProtKB:P35520};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250|UniProtKB:P35520};
CC -!- ACTIVITY REGULATION: Allosterically activated by S-adenosyl-
CC methionine/AdoMet. Activated by S-adenosylhomocysteine/AdoHcy. Binds
CC non-covalently to a heme group that may control the redox sensitivity
CC of the enzyme. {ECO:0000250|UniProtKB:P35520}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine
CC from L-homocysteine and L-serine: step 1/2.
CC {ECO:0000250|UniProtKB:P35520}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P35520}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P35520}. Nucleus
CC {ECO:0000250|UniProtKB:P35520}.
CC -!- SIMILARITY: Belongs to the cysteine synthase/cystathionine beta-
CC synthase family. {ECO:0000305}.
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DR EMBL; AY952460; AAX51303.1; -; mRNA.
DR RefSeq; NP_001270081.1; NM_001283152.1.
DR AlphaFoldDB; Q58H57; -.
DR SMR; Q58H57; -.
DR STRING; 9541.XP_005548649.1; -.
DR PRIDE; Q58H57; -.
DR GeneID; 102115084; -.
DR CTD; 875; -.
DR VEuPathDB; HostDB:ENSMFAG00000038794; -.
DR eggNOG; KOG1252; Eukaryota.
DR OMA; KFADDEW; -.
DR OrthoDB; 1016546at2759; -.
DR UniPathway; UPA00136; UER00201.
DR Proteomes; UP000233100; Chromosome 3.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0004122; F:cystathionine beta-synthase activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0030170; F:pyridoxal phosphate binding; ISS:UniProtKB.
DR GO; GO:0006535; P:cysteine biosynthetic process from serine; IEA:InterPro.
DR GO; GO:0019343; P:cysteine biosynthetic process via cystathionine; IEA:InterPro.
DR GO; GO:0043418; P:homocysteine catabolic process; ISS:UniProtKB.
DR GO; GO:0050667; P:homocysteine metabolic process; ISS:UniProtKB.
DR GO; GO:0070814; P:hydrogen sulfide biosynthetic process; ISS:UniProtKB.
DR GO; GO:0006563; P:L-serine metabolic process; ISS:UniProtKB.
DR CDD; cd04608; CBS_pair_CBS; 1.
DR Gene3D; 3.10.580.10; -; 1.
DR Gene3D; 3.40.50.1100; -; 2.
DR InterPro; IPR046353; CBS_C.
DR InterPro; IPR000644; CBS_dom.
DR InterPro; IPR046342; CBS_dom_sf.
DR InterPro; IPR005857; Cysta_beta_synth.
DR InterPro; IPR001216; P-phosphate_BS.
DR InterPro; IPR001926; PLP-dep.
DR InterPro; IPR036052; Trypto_synt_PLP_dependent.
DR Pfam; PF00571; CBS; 1.
DR Pfam; PF00291; PALP; 1.
DR SMART; SM00116; CBS; 1.
DR SUPFAM; SSF53686; SSF53686; 1.
DR SUPFAM; SSF54631; SSF54631; 1.
DR TIGRFAMs; TIGR01137; cysta_beta; 1.
DR PROSITE; PS51371; CBS; 1.
DR PROSITE; PS00901; CYS_SYNTHASE; 1.
PE 2: Evidence at transcript level;
KW Amino-acid biosynthesis; CBS domain; Cysteine biosynthesis; Cytoplasm;
KW Heme; Iron; Isopeptide bond; Lyase; Metal-binding; Nucleus; Phosphoprotein;
KW Pyridoxal phosphate; Reference proteome; Ubl conjugation.
FT CHAIN 1..551
FT /note="Cystathionine beta-synthase"
FT /id="PRO_0000263003"
FT DOMAIN 418..476
FT /note="CBS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT REGION 1..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 52
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P35520"
FT BINDING 65
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P35520"
FT BINDING 149
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P35520"
FT BINDING 256..260
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P35520"
FT BINDING 349
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P35520"
FT MOD_RES 27
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35520"
FT MOD_RES 119
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P35520"
FT MOD_RES 199
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35520"
FT CROSSLNK 211
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250|UniProtKB:P35520"
SQ SEQUENCE 551 AA; 60721 MW; DCFA5E0F1E68A45B CRC64;
MPSETPQAEV GPTGCPHLSG PHSAQGSLEK GLPGDKEAKE PLWIRPDAPS RCTWQLGRPA
SESPHHHTVP EKSPKILPDI LKKIGDTPMI RINKIGKKFG LKCELLAKCE FFNAGGSVKD
RISLRMIEDA ERAGTLKPGD TIIEPTSGNT GIGLALTAAV RGYRCIIVMP EKMSSEKVDV
LRALGAEIVR TPTNARFDSP ESHVGVAWRL KNEIPNSHIL DQYRNASNPL AHYDTTADEI
LRQCDGKLDM LVASVGTGGT ITGIARKLKE KCPGCRIIGV DPEGSILAEP EELNQTEQTT
YEVEGIGYDF IPTVLDRTVV DKWFKSNDEE AFTFARMLIA QEGLLCGGSA GSTMAVAVKA
AQELQEGQRC VVILPDSVRN YMTKFLSDRW MLQKGFLKEE DLMEKKPWWW HLRVQELSLS
APLTVLPTVS CEHTIEILRE KGFDQAPVVD EAGVILGMVT LGNMLSSLLA GKVQPSDQVG
KVIYTQFKQI RLTDTLGRLS HILEMDHFAL VVHEQIQYHS TGKSSQRQMV FGVVTAIDLL
NFVAAQERDQ K
