ID B9WMM0_CANDC Unreviewed; 399 AA.
AC B9WMM0;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE SubName: Full=Cystathionine gamma-lyase, putative {ECO:0000313|EMBL:CAX40335.1};
DE EC=4.4.1.1 {ECO:0000313|EMBL:CAX40335.1};
GN OrderedLocusNames=Cd36_33930 {ECO:0000313|CGD:CAL0000168149};
GN ORFNames=CD36_33930 {ECO:0000313|EMBL:CAX40335.1};
OS Candida dubliniensis (strain CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 /
OS NRRL Y-17841) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=573826 {ECO:0000313|EMBL:CAX40335.1, ECO:0000313|Proteomes:UP000002605};
RN [1] {ECO:0000313|EMBL:CAX40335.1, ECO:0000313|Proteomes:UP000002605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 / NRRL Y-17841
RC {ECO:0000313|Proteomes:UP000002605};
RX PubMed=19745113; DOI=10.1101/gr.097501.109;
RA Jackson A.P., Gamble J.A., Yeomans T., Moran G.P., Saunders D., Harris D.,
RA Aslett M., Barrell J.F., Butler G., Citiulo F., Coleman D.C.,
RA de Groot P.W.J., Goodwin T.J., Quail M.A., McQuillan J., Munro C.A.,
RA Pain A., Poulter R.T., Rajandream M.A., Renauld H., Spiering M.J.,
RA Tivey A., Gow N.A.R., Barrell B., Sullivan D.J., Berriman M.;
RT "Comparative genomics of the fungal pathogens Candida dubliniensis and
RT Candida albicans.";
RL Genome Res. 19:2231-2244(2009).
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; FM992695; CAX40335.1; -; Genomic_DNA.
DR RefSeq; XP_002422329.1; XM_002422284.1.
DR AlphaFoldDB; B9WMM0; -.
DR GeneID; 8050290; -.
DR KEGG; cdu:CD36_33930; -.
DR CGD; CAL0000168149; Cd36_33930.
DR VEuPathDB; FungiDB:CD36_33930; -.
DR eggNOG; KOG0053; Eukaryota.
DR HOGENOM; CLU_018986_2_3_1; -.
DR OrthoDB; 6018at2759; -.
DR Proteomes; UP000002605; Chromosome R.
DR GO; GO:0004123; F:cystathionine gamma-lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0080146; F:L-cysteine desulfhydrase activity; IEA:UniProtKB-EC.
DR GO; GO:0044540; F:L-cystine L-cysteine-lyase (deaminating); IEA:UniProtKB-EC.
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 PIRSF; PIRSF001434; CGS; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000313|EMBL:CAX40335.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2}.
FT MOD_RES 209
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 399 AA; 42919 MW; F50404564E7C0C09 CRC64;
MTIESSTNYS FGTKAIHAGA PLDPSTGAVI EPISLSTTFA QSEPSKPLGI YEYSRSSNPN
RDNFENAVAA LENAKYAIAL SSGSATTALV IQSLPINSHI VSSGDVYGGT HRYFTQVANT
HGVEAQFVGN LVEDLQGALR ENTRLVWLET PSNPTLQVTD IAKVKSILAD HEAKTGNKVL
LVVDNTFLSP YLSNPLTHGA DVVVHSVTKY INGHSDVVMG VLATNNSQLH ERFRFLQNAI
GSIPSPFDSW LAHRGLKTLH LRVRQASNSA QRIAEYLSQH SAVLKVNYPG LKSHKNHDVV
LRQQRDGLGG GMISFRIAGG AKGAAVFTSS TKLFTLAESL GGIESLIEVP AIMTHGGIPK
EEREANGVYD DLVRVSVGIE DTEDLLKDIE QALQKVASV
//
