ID J4GDN0_9APHY Unreviewed; 259 AA.
AC J4GDN0;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE RecName: Full=Cystathionine beta-lyase {ECO:0008006|Google:ProtNLM};
GN ORFNames=FIBRA_07166 {ECO:0000313|EMBL:CCM04968.1};
OS Fibroporia radiculosa.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Fibroporiaceae; Fibroporia.
OX NCBI_TaxID=599839 {ECO:0000313|EMBL:CCM04968.1, ECO:0000313|Proteomes:UP000006352};
RN [1] {ECO:0000313|EMBL:CCM04968.1, ECO:0000313|Proteomes:UP000006352}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TFFH 294 {ECO:0000313|EMBL:CCM04968.1,
RC ECO:0000313|Proteomes:UP000006352};
RX PubMed=22247176; DOI=10.1128/AEM.06745-11;
RA Tang J.D., Perkins A.D., Sonstegard T.S., Schroeder S.G., Burgess S.C.,
RA Diehl S.V.;
RT "Short-read sequencing for genomic analysis of the brown rot fungus
RT Fibroporia radiculosa.";
RL Appl. Environ. Microbiol. 78:2272-2281(2012).
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; HE797175; CCM04968.1; -; Genomic_DNA.
DR RefSeq; XP_012184251.1; XM_012328861.1.
DR AlphaFoldDB; J4GDN0; -.
DR STRING; 599839.J4GDN0; -.
DR GeneID; 24099879; -.
DR HOGENOM; CLU_018986_5_0_1; -.
DR InParanoid; J4GDN0; -.
DR OrthoDB; 6018at2759; -.
DR Proteomes; UP000006352; Unassembled WGS sequence.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0019346; P:transsulfuration; IEA:InterPro.
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 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 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|RuleBase:RU362118};
KW Reference proteome {ECO:0000313|Proteomes:UP000006352}.
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 259 AA; 28293 MW; 6C2D511D53D3F227 CRC64;
MSDDSDKKIP VYDLPTPESE SPSLPRSRQP YRFSTLIATV ETPNAGHQDQ HGSSSVPIYQ
TATFKGVGGQ YDYSRSGNPT RTHLEHHIAK ISSAEHAFVV SSGMAALDII TRILKPGCEV
IAGDDLYGGT NRLLTFLRTN MGVTVHHVDT TQATTVVPYL SPGKTSMVLL ETPTNPLLKV
VDIARISALV KERCPDAIIV VDNTMMSPYL QRPLEHGADI VYDSATKYLS GHHDLMAGVI
TCNRDDLAKV SQDLLHKKN
//