ID G0PGP9_CAEBE Unreviewed; 480 AA.
AC G0PGP9;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=cystathionine gamma-lyase {ECO:0000256|ARBA:ARBA00012085};
DE EC=4.4.1.1 {ECO:0000256|ARBA:ARBA00012085};
DE AltName: Full=Gamma-cystathionase {ECO:0000256|ARBA:ARBA00029853};
GN ORFNames=CAEBREN_31370 {ECO:0000313|EMBL:EGT55409.1};
OS Caenorhabditis brenneri (Nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=135651 {ECO:0000313|Proteomes:UP000008068};
RN [1] {ECO:0000313|Proteomes:UP000008068}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PB2801 {ECO:0000313|Proteomes:UP000008068};
RG Caenorhabditis brenneri Sequencing and Analysis Consortium;
RA Wilson R.K.;
RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
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|RuleBase:RU362118}.
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DR EMBL; GL380434; EGT55409.1; -; Genomic_DNA.
DR AlphaFoldDB; G0PGP9; -.
DR STRING; 135651.G0PGP9; -.
DR EnsemblMetazoa; CBN31370.1; CBN31370.1; WBGene00193335.
DR eggNOG; KOG0053; Eukaryota.
DR HOGENOM; CLU_018986_2_0_1; -.
DR InParanoid; G0PGP9; -.
DR UniPathway; UPA00136; UER00202.
DR Proteomes; UP000008068; Unassembled WGS sequence.
DR GO; GO:0004123; F:cystathionine gamma-lyase activity; IEA:UniProtKB-EC.
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:InterPro.
DR GO; GO:0019344; P:cysteine biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0019346; P:transsulfuration; IEA:InterPro.
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); 2.
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:SF90; 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; 2.
DR SUPFAM; SSF53383; PLP-dependent transferases; 2.
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:UP000008068}.
FT MOD_RES 296
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 480 AA; 52323 MW; 979F43C9B8C460D1 CRC64;
MSGHFDWPVG NNEAKERLGE RFSSLHLDTK ISASHAKPLA NADPVVVPIY HSSTYRFKTI
DQFSEPNHGS NFVYRRCGNP TTENVEVVIN EIEGGAGSLL YNSGLAAISA VFLEFLGSGS
HLISMSPIYS GTSSFINETL KRFGVEVTFV DVEKEEDFAK AVENSIRPNT KLIYFETIAN
PTMAVPDVLG TIGVAKKHKI RTCIDATFSS PYNIQPLGLG ADISLHSCSK YIGGHTDVIA
GVVTVASYDD WKRLKLQQLT TGSSLIPTAI DATFASPINI QPLKLGADVS IHSCSKYIGG
HSDVIAGVVT VANYEHWKKL KLQQFTTGSS LSPFDASLVT RGLKTLALRV DRISENAQKT
AEFLESHPKV TRVFYPGLPS HPQHKYAKQV MKQFSGMIAF DVGTAENAIK LVETVKLITH
AVSLGGTESL IEHPLTMTHG KEEIRDERRP DVAPGLLRFS VGLENVSDII GDLRDALDNL
//
