ID L8X4E1_THACA Unreviewed; 637 AA.
AC L8X4E1;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=Cystathionine gamma-lyase {ECO:0000313|EMBL:ELU45171.1};
GN ORFNames=AG1IA_00805 {ECO:0000313|EMBL:ELU45171.1};
OS Thanatephorus cucumeris (strain AG1-IA) (Rice sheath blight fungus)
OS (Rhizoctonia solani).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Cantharellales; Ceratobasidiaceae; Rhizoctonia; Rhizoctonia solani AG-1.
OX NCBI_TaxID=983506 {ECO:0000313|EMBL:ELU45171.1, ECO:0000313|Proteomes:UP000011668};
RN [1] {ECO:0000313|EMBL:ELU45171.1, ECO:0000313|Proteomes:UP000011668}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AG-1 IA {ECO:0000313|Proteomes:UP000011668};
RX PubMed=23361014; DOI=10.1038/ncomms2427;
RA Zheng A., Lin R., Xu L., Qin P., Tang C., Ai P., Zhang D., Liu Y., Sun Z.,
RA Feng H., Wang Y., Chen Y., Liang X., Fu R., Li Q., Zhang J., Yu X., Xie Z.,
RA Ding L., Guan P., Tang J., Liang Y., Wang S., Deng Q., Li S., Zhu J.,
RA Wang L., Liu H., Li P.;
RT "The evolution and pathogenic mechanisms of the rice sheath blight
RT pathogen.";
RL Nat. Commun. 4:1424-1424(2013).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ELU45171.1}.
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DR EMBL; AFRT01000147; ELU45171.1; -; Genomic_DNA.
DR AlphaFoldDB; L8X4E1; -.
DR STRING; 983506.L8X4E1; -.
DR HOGENOM; CLU_018986_2_3_1; -.
DR OMA; HASTRYW; -.
DR Proteomes; UP000011668; 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 SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 4: Predicted;
KW Lyase {ECO:0000313|EMBL:ELU45171.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000011668};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..15
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 16..637
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012836303"
FT REGION 596..637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 637 AA; 68491 MW; 68F8A20C2FE4D061 CRC64;
MKALLAVLIT SRVFASIRFI DVKPSYTSDD HFRSPLKNVG CHTLTIMCSD DTPSKTSNRS
VLVTSDHLGM LRPVSSGYSS LYGMSLPCGQ LPYCESKFWW AKHASTRYWE SRYMSICRAG
ITRPLNGSAT TLTTLIGCTA VLLLPCITPR PLNIPPEMSH TTAGFGTRAI HVGSEANAET
GTALVNTRCA NSRQCQPSRF LLYQQGYEYS RSGNPNRDQL ERLLASIEAG GGDAVAFASG
SATTATVLQA LGPNAHVVSV NDVYGGTFRY MTRVAKENQG LETTFVDLEN SSDEQITASF
RDNTKLIWIE SPTNPTLRLI DIRRIVRLAH AHPSNPLVLV DNTFLSPFYS SPLLLGADAV
VHSLTKYING HSDVVMGALI VPSASTHPRA AAFAERTRFL QNATGAVPSP HDCWLAHRGA
KTLHLRMQAH GRNALKVAAY LQAIAGPESA VESVTYPGLA THPRHELAVR QLSPHAKKFI
DTLSSKETAT GVPFGGMISF RIRGGLDTAE SFLVNSQYFT LAESLGGVES LGEVPAIMTH
GSIPEAERAA LGISSNLIRL SVGVEDADDL IADIHQALKA AVPGLAVPEP LAIKTPEASR
SVNDTPEGSV PATPADALPA QPLSKPLKLE EMSQISY
//
