ID Q6FRS2_CANGA Unreviewed; 391 AA.
AC Q6FRS2;
DT 19-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 19-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 104.
DE SubName: Full=Candida glabrata strain CBS138 chromosome H complete sequence {ECO:0000313|EMBL:CAG60005.1};
GN Name=CYS3 {ECO:0000313|CGD:CAL0131600};
GN OrderedLocusNames=CAGL0H06369g {ECO:0000313|CGD:CAL0131600,
GN ECO:0000313|EMBL:CAG60005.1};
OS Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 /
OS NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces.
OX NCBI_TaxID=284593 {ECO:0000313|EMBL:CAG60005.1, ECO:0000313|Proteomes:UP000002428};
RN [1] {ECO:0000313|EMBL:CAG60005.1, ECO:0000313|Proteomes:UP000002428}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65
RC {ECO:0000313|Proteomes:UP000002428};
RX PubMed=15229592; DOI=10.1038/nature02579;
RG Genolevures;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.F., Straub M.L.,
RA Suleau A., Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E.,
RA Wirth B., Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA Wincker P., Souciet J.L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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; CR380954; CAG60005.1; -; Genomic_DNA.
DR RefSeq; XP_447072.1; XM_447072.1.
DR AlphaFoldDB; Q6FRS2; -.
DR STRING; 284593.Q6FRS2; -.
DR EnsemblFungi; CAGL0H06369g-T; CAGL0H06369g-T-p1; CAGL0H06369g.
DR GeneID; 2888813; -.
DR KEGG; cgr:CAGL0H06369g; -.
DR CGD; CAL0131600; CYS3.
DR VEuPathDB; FungiDB:CAGL0H06369g; -.
DR eggNOG; KOG0053; Eukaryota.
DR HOGENOM; CLU_018986_2_3_1; -.
DR InParanoid; Q6FRS2; -.
DR OMA; YKQDGVG; -.
DR Proteomes; UP000002428; Chromosome H.
DR GO; GO:0004123; F:cystathionine gamma-lyase activity; IEA:EnsemblFungi.
DR GO; GO:0047804; F:cysteine-S-conjugate beta-lyase activity; IEA:EnsemblFungi.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0019343; P:cysteine biosynthetic process via cystathionine; IEA:EnsemblFungi.
DR GO; GO:1904828; P:positive regulation of hydrogen sulfide biosynthetic process; IEA:EnsemblFungi.
DR GO; GO:0019346; P:transsulfuration; IEA:EnsemblFungi.
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.
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:UP000002428}.
FT MOD_RES 202
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 391 AA; 42172 MW; C3E719C380F403C9 CRC64;
MGLLESDKFA TKAIHAGAHE DIHGSVIEPI SLSTTFKQSE PAKPIGTYEY SRSQNPNREN
LEAAIASLEG GKYGLAFSSG SATTAVILQS LPQGSHAVSI GDVYGGTHRY FTKVANAHGV
DTSFTNNLIE DLPKLVKDNT KLVWIESPTN PTLKVTDIQL VAENVKKINK DILLVVDNTF
LSPYLSNPLK FGADIVVHSA TKYINGHSDV VLGVLATNSK DIYERLQFLQ NAIGCIPSPF
DAWLTHRGLK TLHLRVRQAS LNATKIATFL ESNENVVAVN YPGLQSHPNY DVVKKQHREA
LGGGMISFRI KGGAEAAAKF SSSTRLFTLA ESLGGIESLL EVPAVMTHGG IPKEAREASG
VFDDLVRLSV GIEDGEDLLE DIKQALQKAT A
//
