ID I3LW54_ICTTR Unreviewed; 405 AA.
AC I3LW54;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 2.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=Cystathionine gamma-lyase {ECO:0000256|ARBA:ARBA00017343};
DE EC=4.4.1.1 {ECO:0000256|ARBA:ARBA00012085};
DE AltName: Full=Cysteine-protein sulfhydrase {ECO:0000256|ARBA:ARBA00031772};
DE AltName: Full=Gamma-cystathionase {ECO:0000256|ARBA:ARBA00029853};
GN Name=CTH {ECO:0000313|Ensembl:ENSSTOP00000000178.3};
OS Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) (Spermophilus
OS tridecemlineatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC Xerinae; Marmotini; Ictidomys.
OX NCBI_TaxID=43179 {ECO:0000313|Ensembl:ENSSTOP00000000178.3, ECO:0000313|Proteomes:UP000005215};
RN [1] {ECO:0000313|Proteomes:UP000005215}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Assembly & Analysis Group;
RG Computational R&D Group;
RG and Sequencing Platform;
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lindblad-Toh K.;
RT "The Draft Genome of Spermophilus tridecemlineatus.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSTOP00000000178.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|RuleBase:RU362118};
CC -!- PATHWAY: Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine
CC from L-homocysteine and L-serine: step 2/2.
CC {ECO:0000256|ARBA:ARBA00005038}.
CC -!- SIMILARITY: Belongs to the trans-sulfuration enzymes family.
CC {ECO:0000256|ARBA:ARBA00009077, ECO:0000256|RuleBase:RU362118}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AGTP01069676; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01069677; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_005332400.1; XM_005332343.2.
DR AlphaFoldDB; I3LW54; -.
DR STRING; 43179.ENSSTOP00000000178; -.
DR Ensembl; ENSSTOT00000000201.3; ENSSTOP00000000178.3; ENSSTOG00000000202.3.
DR GeneID; 101970948; -.
DR CTD; 1491; -.
DR eggNOG; KOG0053; Eukaryota.
DR GeneTree; ENSGT00390000000312; -.
DR HOGENOM; CLU_018986_2_3_1; -.
DR InParanoid; I3LW54; -.
DR OrthoDB; 6018at2759; -.
DR TreeFam; TF300720; -.
DR UniPathway; UPA00136; UER00202.
DR Proteomes; UP000005215; Unassembled WGS sequence.
DR GO; GO:0004123; F:cystathionine gamma-lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEA:Ensembl.
DR GO; GO:0019343; P:cysteine biosynthetic process via cystathionine; IEA:Ensembl.
DR GO; GO:0070814; P:hydrogen sulfide biosynthetic process; IEA:Ensembl.
DR GO; GO:2001234; P:negative regulation of apoptotic signaling pathway; IEA:Ensembl.
DR GO; GO:1904831; P:positive regulation of aortic smooth muscle cell differentiation; IEA:Ensembl.
DR GO; GO:0043123; P:positive regulation of canonical NF-kappaB signal transduction; IEA:Ensembl.
DR GO; GO:0051289; P:protein homotetramerization; IEA:Ensembl.
DR GO; GO:0019346; P:transsulfuration; IEA:Ensembl.
DR CDD; cd00614; CGS_like; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 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:SF15; CYSTATHIONINE GAMMA-LYASE; 1.
DR PANTHER; PTHR11808; TRANS-SULFURATION ENZYME FAMILY MEMBER; 1.
DR Pfam; PF01053; Cys_Met_Meta_PP; 1.
DR PIRSF; PIRSF001434; CGS; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00868; CYS_MET_METAB_PP; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00023192};
KW Cysteine biosynthesis {ECO:0000256|ARBA:ARBA00023192};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000005215}.
FT MOD_RES 212
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 405 AA; 44577 MW; D2488F3EAD12AC12 CRC64;
MQKKDASSLG FLPSFQHFAT QAIHAGQEPE QWNFQDVVPP ISLSTTFKQK APGQHSGFEY
SRSGNPTRNC LEKAVAALDG AKYSLAFASG LAATMTITHL LKAGDQIICM DDVYGGTNRY
FRQVAPKFGL KLSFVDCSKT KLLEAAITPE TKMVWIETPT NPNLKLIDIE ACAHTVHKYG
NIILVVDNTF MSAYFQRPLA LGADICMYSA TKYMNGHSDV VMGIVSVNSE DIHDRLRFLQ
NALGAVPSPM DCYLCIRGLK TLQIRMEKHF KNGMAVAQFL ESNPLIEKVI YPGLPSHPQH
ELAKRQCTGC SGMITFFIKG TLQHAETFLK NLKLFTLAES LGGYESLVEL PAIMTHASVP
KSDRDILGIS DTLIRLSVGL EDEKDLLEDL DQALKAAHPS SGNCD
//
