CGL_BOVIN
ID CGL_BOVIN Reviewed; 405 AA.
AC Q58DW2;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Cystathionine gamma-lyase;
DE EC=4.4.1.1;
DE AltName: Full=Cysteine-protein sulfhydrase;
DE AltName: Full=Gamma-cystathionase;
GN Name=CTH;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
CC -!- FUNCTION: Catalyzes the last step in the trans-sulfuration pathway from
CC methionine to cysteine. Has broad substrate specificity. Converts
CC cystathionine to cysteine, ammonia and 2-oxobutanoate. Converts two
CC cysteine molecules to lanthionine and hydrogen sulfide. Can also accept
CC homocysteine as substrate. Specificity depends on the levels of the
CC endogenous substrates. Generates the endogenous signaling molecule
CC hydrogen sulfide (H2S), and so contributes to the regulation of blood
CC pressure. Acts as a cysteine-protein sulfhydrase by mediating
CC sulfhydration of target proteins: sulfhydration consists of converting
CC -SH groups into -SSH on specific cysteine residues of target proteins
CC such as GAPDH, PTPN1 and NF-kappa-B subunit RELA, thereby regulating
CC their function (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L,L-cystathionine = 2-oxobutanoate + L-cysteine +
CC NH4(+); Xref=Rhea:RHEA:14005, ChEBI:CHEBI:15377, ChEBI:CHEBI:16763,
CC ChEBI:CHEBI:28938, ChEBI:CHEBI:35235, ChEBI:CHEBI:58161; EC=4.4.1.1;
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250};
CC -!- PATHWAY: Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine
CC from L-homocysteine and L-serine: step 2/2.
CC -!- SUBUNIT: Homotetramer. Interacts with CALM in a calcium-dependent
CC manner (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the trans-sulfuration enzymes family.
CC {ECO:0000305}.
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DR EMBL; BT021485; AAX46332.1; -; mRNA.
DR RefSeq; NP_001019738.1; NM_001024567.1.
DR AlphaFoldDB; Q58DW2; -.
DR SMR; Q58DW2; -.
DR PaxDb; Q58DW2; -.
DR PRIDE; Q58DW2; -.
DR GeneID; 539159; -.
DR KEGG; bta:539159; -.
DR CTD; 1491; -.
DR eggNOG; KOG0053; Eukaryota.
DR InParanoid; Q58DW2; -.
DR UniPathway; UPA00136; UER00202.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0016846; F:carbon-sulfur lyase activity; IBA:GO_Central.
DR GO; GO:0004123; F:cystathionine gamma-lyase activity; ISS:UniProtKB.
DR GO; GO:0080146; F:L-cysteine desulfhydrase activity; IEA:UniProtKB-EC.
DR GO; GO:0044540; F:L-cystine L-cysteine-lyase (deaminating); ISS:UniProtKB.
DR GO; GO:0030170; F:pyridoxal phosphate binding; ISS:UniProtKB.
DR GO; GO:0019344; P:cysteine biosynthetic process; ISS:UniProtKB.
DR GO; GO:0019343; P:cysteine biosynthetic process via cystathionine; IBA:GO_Central.
DR GO; GO:0070814; P:hydrogen sulfide biosynthetic process; ISS:UniProtKB.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; ISS:UniProtKB.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISS:UniProtKB.
DR GO; GO:0044524; P:protein sulfhydration; ISS:UniProtKB.
DR GO; GO:0018272; P:protein-pyridoxal-5-phosphate linkage via peptidyl-N6-pyridoxal phosphate-L-lysine; ISS:UniProtKB.
DR GO; GO:0019346; P:transsulfuration; IBA:GO_Central.
DR CDD; cd00614; CGS_like; 1.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR000277; Cys/Met-Metab_PyrdxlP-dep_enz.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR11808; PTHR11808; 1.
DR Pfam; PF01053; Cys_Met_Meta_PP; 1.
DR PIRSF; PIRSF001434; CGS; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
PE 2: Evidence at transcript level;
KW Amino-acid biosynthesis; Calmodulin-binding; Cysteine biosynthesis;
KW Cytoplasm; Lipid metabolism; Lyase; Pyridoxal phosphate;
KW Reference proteome.
FT CHAIN 1..405
FT /note="Cystathionine gamma-lyase"
FT /id="PRO_0000245576"
FT BINDING 62
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 114
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 119
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 339
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 212
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 405 AA; 44406 MW; 53B1E2AF2A6C194A CRC64;
MQEKEASPHG FLPRFQHFAT QAIHVGQEPE QWTSQAVVPP ISLSTTFKQG APGQHSGFEY
SRSGNPTRNC LEKAVAALDG AKYSLAFASG LAATVTITHL LKAGDQIICM DDVYGGTNRY
FRQVATEFGL KISFVDCSKP KLLEAAITPE TKLVWIETPT NPSLKMIDIE ACAHTVHKHG
DIILVVDNTF MSAYFQRPLS LGADICMYSA TKYMNGYSDV VMGLVSLNSE SLHDRLRFLQ
NSLGAVPSPI DCYLCNRGLK TLQVRMEKHF ENGMAVAQFL ESNPQVEKVI YPGLPSHPQH
ELAKRQCTGC PGMVTFYIKG SLQHAETFLQ NLKLFTLAES LGGYESLAEL PAIMTHASVP
KSDREVLGIS DTLIRLSVGL EDKQDLLDDL DQALKAANPP NASSN
