CGL_DICDI
ID CGL_DICDI Reviewed; 387 AA.
AC Q55DV9;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Cystathionine gamma-lyase;
DE Short=CGL;
DE Short=CSE;
DE EC=4.4.1.1 {ECO:0000250|UniProtKB:P32929};
DE AltName: Full=Cysteine desulfhydrase;
DE AltName: Full=Cysteine-protein sulfhydrase;
DE AltName: Full=Gamma-cystathionase;
DE AltName: Full=Homocysteine desulfhydrase;
DE EC=4.4.1.2 {ECO:0000250|UniProtKB:P32929};
GN Name=cysA; ORFNames=DDB_G0269122;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [2]
RP PROTEIN SEQUENCE OF 9-22 AND 357-365, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RA Bienvenut W.V., Veltman D.M., Insall R.H.;
RL Submitted (JAN-2010) to UniProtKB.
RN [3]
RP DEVELOPMENTAL STAGE.
RX PubMed=17259634; DOI=10.1099/mic.0.2006/000562-0;
RA Serafimidis I., Bloomfield G., Skelton J., Ivens A., Kay R.R.;
RT "A new environmentally resistant cell type from Dictyostelium.";
RL Microbiology 153:619-630(2007).
CC -!- FUNCTION: Catalyzes the last step in the trans-sulfuration pathway from
CC L-methionine to L-cysteine in a pyridoxal-5'-phosphate (PLP)-dependent
CC manner, which consists on cleaving the L,L-cystathionine molecule into
CC L-cysteine, ammonia and 2-oxobutanoate. Part of the L-cysteine derived
CC from the trans-sulfuration pathway is utilized for biosynthesis of the
CC ubiquitous antioxidant glutathione. Besides its role in the conversion
CC of L-cystathionine into L-cysteine, it utilizes L-cysteine and L-
CC homocysteine as substrates (at much lower rates than L,L-cystathionine)
CC to produce the endogenous gaseous signaling molecule hydrogen sulfide
CC (H2S). {ECO:0000250|UniProtKB:P32929, ECO:0000250|UniProtKB:Q8VCN5}.
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 Evidence={ECO:0000250|UniProtKB:P32929};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14006;
CC Evidence={ECO:0000250|UniProtKB:P32929};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-cysteine = H(+) + hydrogen sulfide + NH4(+) +
CC pyruvate; Xref=Rhea:RHEA:24931, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:29919,
CC ChEBI:CHEBI:35235; EC=4.4.1.1;
CC Evidence={ECO:0000250|UniProtKB:P32929};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24932;
CC Evidence={ECO:0000250|UniProtKB:P32929};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-homocysteine = 2-oxobutanoate + H(+) + hydrogen
CC sulfide + NH4(+); Xref=Rhea:RHEA:14501, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16763, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:29919, ChEBI:CHEBI:58199; EC=4.4.1.2;
CC Evidence={ECO:0000250|UniProtKB:P32929};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14502;
CC Evidence={ECO:0000250|UniProtKB:P32929};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-homoserine = 2-oxobutanoate + NH4(+); Xref=Rhea:RHEA:24923,
CC ChEBI:CHEBI:16763, ChEBI:CHEBI:28938, ChEBI:CHEBI:57476; EC=4.4.1.1;
CC Evidence={ECO:0000250|UniProtKB:P18757};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24924;
CC Evidence={ECO:0000250|UniProtKB:P18757};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250|UniProtKB:P32929};
CC -!- PATHWAY: Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine
CC from L-homocysteine and L-serine: step 2/2.
CC {ECO:0000250|UniProtKB:P32929}.
CC -!- SUBUNIT: Homotetramer (By similarity). Interacts with CALM in a
CC calcium-dependent manner (By similarity).
CC {ECO:0000250|UniProtKB:P32929, ECO:0000250|UniProtKB:Q8VCN5}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- DEVELOPMENTAL STAGE: Up-regulated in aspidocytes, a resistant cell type
CC induced by a range of toxins including heavy metals and antibiotics.
CC {ECO:0000269|PubMed:17259634}.
CC -!- SIMILARITY: Belongs to the trans-sulfuration enzymes family.
CC {ECO:0000305}.
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DR EMBL; AAFI02000005; EAL71911.1; -; Genomic_DNA.
DR RefSeq; XP_646022.1; XM_640930.1.
DR AlphaFoldDB; Q55DV9; -.
DR SMR; Q55DV9; -.
DR STRING; 44689.DDB0191318; -.
DR PaxDb; Q55DV9; -.
DR EnsemblProtists; EAL71911; EAL71911; DDB_G0269122.
DR GeneID; 8616970; -.
DR KEGG; ddi:DDB_G0269122; -.
DR dictyBase; DDB_G0269122; cysA.
DR eggNOG; KOG0053; Eukaryota.
DR HOGENOM; CLU_018986_2_0_1; -.
DR InParanoid; Q55DV9; -.
DR OMA; YKQDGVG; -.
DR PhylomeDB; Q55DV9; -.
DR Reactome; R-DDI-1614558; Degradation of cysteine and homocysteine.
DR Reactome; R-DDI-1614603; Cysteine formation from homocysteine.
DR UniPathway; UPA00136; UER00202.
DR PRO; PR:Q55DV9; -.
DR Proteomes; UP000002195; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016846; F:carbon-sulfur lyase activity; IBA:GO_Central.
DR GO; GO:0004123; F:cystathionine gamma-lyase activity; ISS:dictyBase.
DR GO; GO:0047982; F:homocysteine desulfhydrase activity; IEA:RHEA.
DR GO; GO:0080146; F:L-cysteine desulfhydrase activity; IEA:UniProtKB-EC.
DR GO; GO:0044540; F:L-cystine L-cysteine-lyase (deaminating); IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR GO; GO:0019343; P:cysteine biosynthetic process via cystathionine; IBA:GO_Central.
DR GO; GO:0006534; P:cysteine metabolic process; ISS:dictyBase.
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 1: Evidence at protein level;
KW Amino-acid biosynthesis; Cysteine biosynthesis; Cytoplasm;
KW Direct protein sequencing; Lyase; Pyridoxal phosphate; Reference proteome.
FT CHAIN 1..387
FT /note="Cystathionine gamma-lyase"
FT /id="PRO_0000327889"
FT BINDING 53
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 105
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 110
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 329
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 202
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P32929"
SQ SEQUENCE 387 AA; 42497 MW; 1A0D7EF1FE502434 CRC64;
MTQPNNYKIG TNVIHAGQSA DKNTGAVIVP ISLSTTFLQP SPGVLHSEYD YSRSGNPTRK
AFEECIAACE NAKYALSFAS GLATLTTITH LLKSGDEVIS IDDVYGGTRR YFTRVAANFD
LKFSFVDLST LDDLKNAFTD KTRLVWIETP TNPLLKVADI KAVADYVHSR GATLVVDNTF
MSPYFQNPLD LGADIVMHSV TKYINGHSDC VMGVLATNND ELYAKLKFLQ NSIGAVPSPF
DCFLALRGLK TLHVRMEAHQ KNAFAICNFL EKHPKVERVI YPGLPSHPQH EICKRQMKGY
GGMVVFFVKG SIDQSRSFLE NIKLFALAES LGGVESLIEL PSVMTHASVP AEERAKLGIS
DTLIRLSVGI EDINDLLADI SQALDKC
