ID   A0A0R3PZW0_ANGCS        Unreviewed;       408 AA.
AC   A0A0R3PZW0;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 31.
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=ACOC_LOCUS12149 {ECO:0000313|EMBL:VDM63734.1};
OS   Angiostrongylus costaricensis (Nematode worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Strongyloidea; Metastrongylidae;
OC   Angiostrongylus.
OX   NCBI_TaxID=334426 {ECO:0000313|Proteomes:UP000050601, ECO:0000313|WBParaSite:ACOC_0001214801-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:ACOC_0001214801-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDM63734.1, ECO:0000313|Proteomes:UP000267027}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Costa Rica {ECO:0000313|EMBL:VDM63734.1,
RC   ECO:0000313|Proteomes:UP000267027};
RG   Pathogen Informatics;
RL   Submitted (NOV-2018) 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|ARBA:ARBA00009077, ECO:0000256|RuleBase:RU362118}.
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DR   EMBL; UYYA01004913; VDM63734.1; -; Genomic_DNA.
DR   STRING; 334426.A0A0R3PZW0; -.
DR   WBParaSite; ACOC_0001214801-mRNA-1; ACOC_0001214801-mRNA-1; ACOC_0001214801.
DR   OMA; YKQDGVG; -.
DR   UniPathway; UPA00136; UER00202.
DR   Proteomes; UP000050601; Unplaced.
DR   Proteomes; UP000267027; 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.
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:UP000267027}.
FT   REGION          36..56
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         205
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   408 AA;  45281 MW;  194A894642D2F3F1 CRC64;
     MSRDSFPNFG TAAIHVGQEP EQWDMNQVVA PISLSTTYKQ DRPGEPKGHD YSRAGNPSRD
     VLQKCLASLE DGKYCHVFSS GLASSMAIIN LLRAGDHIIC SDDVYGGTQR FIRRVSVVNH
     GLQADFVDLT DIARLEEAFK PNTKMVWFET PSNPLLKVVD IAVVVHCVKR VNSNILVVVD
     NTFMSPYFQR PLSMGVDIVI HSITKYINGH SDVVMGAVIT DNDDIQQHLF FQQLAVGAVP
     SPFDCFLVNR GLKTLHVRMR AHYENALAVA QYLENNERVE RVLYPALPSH PQHKIHKSQT
     KGMSGMMSFY LKGDLEESRT FLSSLKIFTL AESLGGYESL AELPSIMTHA SVPPEERKKL
     RITDNLIRLS VGIEDLDDLI ADLDQALKAA VSFSGSKHST SLTILGNV
//