ID   A0A2J6QKI6_9HELO        Unreviewed;       422 AA.
AC   A0A2J6QKI6;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Cystathionine gamma-lyase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=NA56DRAFT_641440 {ECO:0000313|EMBL:PMD26790.1};
OS   Hyaloscypha hepaticicola.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Hyaloscyphaceae; Hyaloscypha.
OX   NCBI_TaxID=2082293 {ECO:0000313|EMBL:PMD26790.1, ECO:0000313|Proteomes:UP000235672};
RN   [1] {ECO:0000313|EMBL:PMD26790.1, ECO:0000313|Proteomes:UP000235672}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH 7357 {ECO:0000313|EMBL:PMD26790.1,
RC   ECO:0000313|Proteomes:UP000235672};
RG   DOE Joint Genome Institute;
RA   Martino E., Morin E., Grelet G., Kuo A., Kohler A., Daghino S., Barry K.,
RA   Choi C., Cichocki N., Clum A., Copeland A., Hainaut M., Haridas S.,
RA   Labutti K., Lindquist E., Lipzen A., Khouja H.-R., Murat C., Ohm R.,
RA   Olson A., Spatafora J., Veneault-Fourrey C., Henrissat B., Grigoriev I.,
RA   Martin F., Perotto S.;
RT   "A degradative enzymes factory behind the ericoid mycorrhizal symbiosis.";
RL   Submitted (MAY-2016) 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   -!- SIMILARITY: Belongs to the trans-sulfuration enzymes family.
CC       {ECO:0000256|RuleBase:RU362118}.
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DR   EMBL; KZ613467; PMD26790.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2J6QKI6; -.
DR   STRING; 1745343.A0A2J6QKI6; -.
DR   OrthoDB; 6018at2759; -.
DR   Proteomes; UP000235672; Unassembled WGS sequence.
DR   GO; GO:0016846; F:carbon-sulfur lyase activity; IEA:UniProt.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0019344; P:cysteine biosynthetic process; IEA:UniProtKB-KW.
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   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR001434-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000235672}.
FT   MOD_RES         214
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   422 AA;  45074 MW;  E8DBF1449DC2C66C CRC64;
     MSPLTDHPID TPPRAPSPVQ RFATLAVHAG SPYDPSTGAV IEPISLSTTF AQTSVGKPVG
     IYEYSRSSNP NRDNFEIAVA AVEHAKYALA FSSGSATTAI ILQSLAAGSH VVSVSDVYGG
     THRYFTQVAK AHGVKVTFTP EIEVDIREHI TSDTKLVWIE TPSNPTLRLV DIRAVATQAH
     EHGIMVVVDN TFMSPYIQNP LDHGADIVVH SVTKYINGHS DVVMGVAAFN SDAMKERLGF
     LQNAIGAIPS PFDCWLAHRG LKTLHLRVRE ASTNATAVAK ALEASPHVIA VNYPGLDSHP
     HRAIAKKQHR NGMGGGMLSF RIKGGHAAAE RFCQTTTIFT LAESLGGVES LVEVPSSMTH
     AGIPKDQREA VGVFDDLVRI SCGVEDAEDL KADVLQALER AVVWPKISHG LNGMANGNGH
     AA
//