ID   A0A2T3ZP84_9HYPO        Unreviewed;       404 AA.
AC   A0A2T3ZP84;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=Cystathionine beta-lyase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=M441DRAFT_53308 {ECO:0000313|EMBL:PTB46584.1};
OS   Trichoderma asperellum CBS 433.97.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX   NCBI_TaxID=1042311 {ECO:0000313|EMBL:PTB46584.1, ECO:0000313|Proteomes:UP000240493};
RN   [1] {ECO:0000313|EMBL:PTB46584.1, ECO:0000313|Proteomes:UP000240493}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 433.97 {ECO:0000313|EMBL:PTB46584.1,
RC   ECO:0000313|Proteomes:UP000240493};
RG   DOE Joint Genome Institute;
RA   Aerts A., Atanasova L., Chenthamara K., Zhang J., Grujic M., Henrissat B.,
RA   Kuo A., Salamov A., Lipzen A., Labutti K., Barry K., Miao Y., Rahimi M.J.,
RA   Shen Q., Grigoriev I.V., Kubicek C.P., Druzhinina I.S.;
RT   "Multiple horizontal gene transfer events from other fungi enriched the
RT   ability of initially mycotrophic Trichoderma (Ascomycota) to feed on dead
RT   plant biomass.";
RL   Submitted (JUL-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; KZ679256; PTB46584.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T3ZP84; -.
DR   STRING; 1042311.A0A2T3ZP84; -.
DR   OrthoDB; 5482552at2759; -.
DR   Proteomes; UP000240493; Unassembled WGS sequence.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
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:SF35; CYSTATHIONINE GAMMA-SYNTHASE (AFU_ORTHOLOGUE AFUA_7G01590); 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   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR001434-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000240493};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   MOD_RES         212
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   404 AA;  43727 MW;  FBC5CAC85335BCB5 CRC64;
     MGNASDEYVP DIAALSLASR AVHADARIDG HPAIAPGLHT STTFRYPNDP ERLKPISEVD
     TTKPLDFHVY SRHTSPNMAR FEALLTSIIG QQAIVYGSGL AAFHAMITHL NPKKVAIGDG
     YHGCHGILKI FERLTGLKKL PLDCDLSELG PGDIIHVETP LNPTGEARDL KYYADRAHSV
     GAYLTVDATF APPPLLDPFA WGADLVMHSG TKYFGGHSDL LCGVLAANPK HKTWVSDLLA
     DRLVLGSVIG SLEGWLGMRS LRTLELRVNR QSTTAAALVA WLAEQAKDPA TAAGKTIARI
     QHASLQPEAA QEGSWLRQQM PNGYGPVFAI TLKNKEMARR FPGKLGLFQH ATSLGGVESL
     IEWRAMTDAT VDQSLLRLSV GVESLEDLKA DLQHGFEALV KEGL
//