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Database: UniProt
Entry: A0A085MYV6_9BILA
LinkDB: A0A085MYV6_9BILA
Original site: A0A085MYV6_9BILA 
ID   A0A085MYV6_9BILA        Unreviewed;       325 AA.
AC   A0A085MYV6;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 26.
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=M514_00895 {ECO:0000313|EMBL:KFD62402.1};
OS   Trichuris suis (pig whipworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichuridae; Trichuris.
OX   NCBI_TaxID=68888 {ECO:0000313|EMBL:KFD62402.1};
RN   [1] {ECO:0000313|EMBL:KFD62402.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DCEP-RM93F {ECO:0000313|EMBL:KFD62402.1};
RX   PubMed=24929829; DOI=10.1038/ng.3012;
RA   Jex A.R., Nejsum P., Schwarz E.M., Hu L., Young N.D., Hall R.S.,
RA   Korhonen P.K., Liao S., Thamsborg S., Xia J., Xu P., Wang S.,
RA   Scheerlinck J.P., Hofmann A., Sternberg P.W., Wang J., Gasser R.B.;
RT   "Genome and transcriptome of the porcine whipworm Trichuris suis.";
RL   Nat. Genet. 46:701-706(2014).
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}.
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DR   EMBL; KL367596; KFD62402.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A085MYV6; -.
DR   UniPathway; UPA00136; UER00202.
DR   Proteomes; UP000030758; 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); 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.
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}.
FT   MOD_RES         133
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   325 AA;  35804 MW;  B338ABF9447CB892 CRC64;
     MNYLSGKTFA SGLAAISAIT AILRPGEAIL ALTDMYGGTM RFFNQVLGKV GIKCIMVDLI
     GKNIEEYLTP DVKMIWIESP TNPLLRIVDI EEVCTTARKT EGLLTVVDNT FMSPYFQRPL
     ALGATMTVHS VTKYINGHSD VIMGCVCTNS KEIFDHLNFQ QLAVGAVPSP FDCYLVNRGI
     KTLHLRMRAH EENGFEVARF LEKHPLVESV IFPGLPSHPQ HELHVKQTTG TSGMVSFYIR
     GGQTEAVTFL KSLKIFALAE SLGGYESLAE HPALMTHASV PEKIRKQLGI TDNLIRLSVG
     LEDPEDLKAD LDNALKATQR FPNGI
//
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