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Database: UniProt
Entry: T5ACZ3_OPHSC
LinkDB: T5ACZ3_OPHSC
Original site: T5ACZ3_OPHSC 
ID   T5ACZ3_OPHSC            Unreviewed;       477 AA.
AC   T5ACZ3;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   SubName: Full=Cystathionine beta-lyase {ECO:0000313|EMBL:EQL00464.1};
GN   ORFNames=OCS_03823 {ECO:0000313|EMBL:EQL00464.1};
OS   Ophiocordyceps sinensis (strain Co18 / CGMCC 3.14243) (Yarsagumba
OS   caterpillar fungus) (Hirsutella sinensis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Ophiocordyceps.
OX   NCBI_TaxID=911162 {ECO:0000313|EMBL:EQL00464.1, ECO:0000313|Proteomes:UP000019374};
RN   [1] {ECO:0000313|EMBL:EQL00464.1, ECO:0000313|Proteomes:UP000019374}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Co18 / CGMCC 3.14243 {ECO:0000313|Proteomes:UP000019374};
RC   TISSUE=Fruit-body {ECO:0000313|EMBL:EQL00464.1};
RX   DOI=10.1007/s11434-013-5929-5;
RA   Hu X., Zhang Y., Xiao G., Zheng P., Xia Y., Zhang X., St Leger R.J.,
RA   Liu X., Wang C.;
RT   "Genome survey uncovers the secrets of sex and lifestyle in caterpillar
RT   fungus.";
RL   Chin. Sci. Bull. 58:2846-2854(2013).
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; KE652805; EQL00464.1; -; Genomic_DNA.
DR   AlphaFoldDB; T5ACZ3; -.
DR   eggNOG; KOG0053; Eukaryota.
DR   HOGENOM; CLU_018986_2_1_1; -.
DR   Proteomes; UP000019374; Unassembled WGS sequence.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
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:SF50; CYSTATHIONINE BETA-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.
DR   PROSITE; PS00868; CYS_MET_METAB_PP; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000313|EMBL:EQL00464.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR001434-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019374};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   REGION          1..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..18
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         243
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   477 AA;  51402 MW;  A83A927ED058BACD CRC64;
     MAASFSSNGA TSASSGGANP LKRRVDPDGH QLPPSPAPSS PRNGRRRYAL ATELVYTEAT
     DQYGASSIPI YQSATFKQTT ASGGQQEYDY TRSGNPTRTH LERHIAKIMN ANRALAVSSG
     MGALDVISRL LRPGDEVVTG DDLYGGTHRL LTYMATNQGI TVHHVDTTST NAVSQCLSSK
     TAMVLLETPT NPLIKIVDLL SIARMAHEVN PRALVVVDNT MLSPWLCNPL DLGADIAYES
     GTKYLSGHHD IMAGVIACND AAIGNKLFFT INSTGWGVSP NDSFLLMRGV KTLSIRMEKQ
     QANAQAIADF LEGVKTLGIR MEKQQANAQA IADFLESRGF RVRYPGLKSH PQYDLHWSMA
     RGAGAVLSFE TGDPTVSERI VEAARLWSIS VSFGCVNSLI SMPCQMSHAS IDAKTRRERQ
     MPEDIIRLCV GIEDANDLIE DLSRALVQAG AVTMTLDGFH AKGVAKGLGG TTLDVQH
//
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