CGL2_CAEEL
ID CGL2_CAEEL Reviewed; 392 AA.
AC P55216;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Putative cystathionine gamma-lyase 2;
DE EC=4.4.1.1;
DE AltName: Full=Gamma-cystathionase;
GN Name=cth-2; ORFNames=ZK1127.10;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the trans-sulfuration enzymes family.
CC {ECO:0000305}.
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DR EMBL; FO081697; CCD73724.1; -; Genomic_DNA.
DR PIR; C88197; C88197.
DR RefSeq; NP_495449.1; NM_063048.5.
DR AlphaFoldDB; P55216; -.
DR SMR; P55216; -.
DR BioGRID; 39492; 19.
DR IntAct; P55216; 3.
DR STRING; 6239.ZK1127.10.1; -.
DR World-2DPAGE; 0011:P55216; -.
DR EPD; P55216; -.
DR PaxDb; P55216; -.
DR PeptideAtlas; P55216; -.
DR EnsemblMetazoa; ZK1127.10.1; ZK1127.10.1; WBGene00022856.
DR GeneID; 174155; -.
DR KEGG; cel:CELE_ZK1127.10; -.
DR UCSC; ZK1127.10.1; c. elegans.
DR CTD; 174155; -.
DR WormBase; ZK1127.10; CE07648; WBGene00022856; cth-2.
DR eggNOG; KOG0053; Eukaryota.
DR GeneTree; ENSGT00390000000312; -.
DR HOGENOM; CLU_018986_2_3_1; -.
DR InParanoid; P55216; -.
DR OMA; YKQDGVG; -.
DR OrthoDB; 572061at2759; -.
DR PhylomeDB; P55216; -.
DR Reactome; R-CEL-1614558; Degradation of cysteine and homocysteine.
DR Reactome; R-CEL-1614603; Cysteine formation from homocysteine.
DR SignaLink; P55216; -.
DR UniPathway; UPA00136; UER00202.
DR PRO; PR:P55216; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00022856; Expressed in larva and 4 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:WormBase.
DR GO; GO:0016846; F:carbon-sulfur lyase activity; IBA:GO_Central.
DR GO; GO:0004123; F:cystathionine gamma-lyase activity; IBA:GO_Central.
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: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.
DR PROSITE; PS00868; CYS_MET_METAB_PP; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Cysteine biosynthesis; Cytoplasm; Lyase;
KW Pyridoxal phosphate; Reference proteome.
FT CHAIN 1..392
FT /note="Putative cystathionine gamma-lyase 2"
FT /id="PRO_0000114753"
FT REGION 32..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 51
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 103
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 108
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 330
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 203
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 392 AA; 43094 MW; DA90B3353AD1004D CRC64;
MATFPHFGTA AIHVGQEPEQ WDMNQVVPPI SLSSTYKQDN PGEPKGHDYS RAGNPTRDVL
QKNLAALEDA KHCQVFSSGL AATSAIINLL KYGDHIVCSD DVYGGTQRYI RRVAVPNHGL
EVDSVDLTDV QNLEKAIKPN TKMVWFESPS NPLLKVVDIA AVVQTAKKAN PEIVVVVDNT
FMSPYFQRPI SLGADVVVHS ITKYINGHSD VVMGAVITDN DEFQQHLFFM QLAVGAVPSP
FDCFLVNRGL KTLHIRMRAH YENALAVAKY LEANDRIESV LYPALPSHPQ HEVHEKQTKG
MSGMISFYLK GELQESRAFL SALKVFTLAE SLGGYESLAE LPSIMTHASV PAETRIVLGI
TDNLIRISVG IEDLDDLVAD LDQALKIAIP KV
