ID A0A2G5VN26_9PELO Unreviewed; 197 AA.
AC A0A2G5VN26;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
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 Name=Cnig_chr_I.g298 {ECO:0000313|EMBL:PIC53164.1};
GN ORFNames=B9Z55_000298 {ECO:0000313|EMBL:PIC53164.1};
OS Caenorhabditis nigoni.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=1611254 {ECO:0000313|EMBL:PIC53164.1, ECO:0000313|Proteomes:UP000230233};
RN [1] {ECO:0000313|Proteomes:UP000230233}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JU1422 {ECO:0000313|Proteomes:UP000230233};
RA Yin D., Schwarz E.M., Thomas C.G., Felde R.L., Korf I.F., Cutter A.D.,
RA Schartner C.M., Ralston E.J., Meyer B.J., Haag E.S.;
RT "Rapid genome shrinkage in a self-fertile nematode reveals novel sperm
RT competition proteins.";
RL Submitted (OCT-2017) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PIC53164.1}.
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DR EMBL; PDUG01000001; PIC53164.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G5VN26; -.
DR STRING; 1611254.A0A2G5VN26; -.
DR UniPathway; UPA00136; UER00202.
DR Proteomes; UP000230233; Chromosome i.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 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:SF90; CYSTATHIONINE GAMMA-LYASE; 1.
DR PANTHER; PTHR11808; TRANS-SULFURATION ENZYME FAMILY MEMBER; 1.
DR Pfam; PF01053; Cys_Met_Meta_PP; 2.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00023192};
KW Cysteine biosynthesis {ECO:0000256|ARBA:ARBA00023192};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU362118};
KW Reference proteome {ECO:0000313|Proteomes:UP000230233};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 72..95
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 197 AA; 21935 MW; 61FECFC8A6B9E137 CRC64;
MSPIYSGTSS FINETLKRFG VEVTFVDVEK EKNFAEAVET EYQDIYFETI ANPTMAVPDV
LGTLKVAEKH KILTSSLSAL TLILVFIVVV TVANYENWKR PKLQQLTTGS SLSPYDAALL
TRGLKTLALR MKQLSENALE IAKFLESHLK VTCVYYPGLE SHPQHKYAKE AMNKSSGMIV
FEVGSAENAI KLVEPLK
//
