ID   U7PKA2_SPOS1            Unreviewed;       423 AA.
AC   U7PKA2;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   08-NOV-2023, entry version 33.
DE   RecName: Full=Cystathionine beta-lyase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=HMPREF1624_07609 {ECO:0000313|EMBL:ERS96073.1};
OS   Sporothrix schenckii (strain ATCC 58251 / de Perez 2211183) (Rose-picker's
OS   disease fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Sporothrix.
OX   NCBI_TaxID=1391915 {ECO:0000313|EMBL:ERS96073.1, ECO:0000313|Proteomes:UP000018087};
RN   [1] {ECO:0000313|Proteomes:UP000018087}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 58251 / de Perez 2211183
RC   {ECO:0000313|Proteomes:UP000018087};
RX   PubMed=24855299; DOI=10.1128/genomea.00446-14;
RA   Cuomo C.A., Rodriguez-Del Valle N., Perez-Sanchez L., Abouelleil A.,
RA   Goldberg J., Young S., Zeng Q., Birren B.W.;
RT   "Genome sequence of the pathogenic fungus Sporothrix schenckii (ATCC
RT   58251).";
RL   Genome Announc. 2:E0044614-E0044614(2014).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; KI440851; ERS96073.1; -; Genomic_DNA.
DR   AlphaFoldDB; U7PKA2; -.
DR   STRING; 1391915.U7PKA2; -.
DR   eggNOG; KOG0053; Eukaryota.
DR   HOGENOM; CLU_018986_3_0_1; -.
DR   OrthoDB; 5482552at2759; -.
DR   Proteomes; UP000018087; 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.
PE   3: Inferred from homology;
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR001434-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018087}.
FT   MOD_RES         219
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   423 AA;  46004 MW;  5261A1411FCE490C CRC64;
     MVAARKGPDG LAAAFEPLTL SSATRAVHAD DYVNSHRAVA PPMHVSTTFR YSDDPDALHM
     WDNTDPAAPY DSHIYSRESA PNTTRLEAIL SDLIGHPTLT YASGMAAFHA LVVFLNPRRV
     AIGAGYHGCH GVLDIMKKLN GLEKLDLLND DDLAKLQPGD VVHVETPLNP TGEARDLAHY
     AQLARAKKCY LTVDATFAPP PLLDPFRWGA DIVMHSGSKY FGGHSDMLCG VLAVHKKYVK
     DPAARAADQN WLAALQDERL VIGGVMGSLE GWLGVRSLRT LALRVERQAS NAAALVAWLA
     AEHKTAGSVV VQVVERIHHA SLQPEAADPG SWLNQQMPHG FGPVFSLVLR EEALARRLPS
     KLALFHHATS LGGVESLIEW RAMSDPHIDK RLLRLSIGVE GWEDIKADLA RAFTELVAEA
     KQA
//