ID G8BZT5_TETPH Unreviewed; 391 AA.
AC G8BZT5;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=Cystathionine gamma-lyase {ECO:0008006|Google:ProtNLM};
GN Name=TPHA0L00570 {ECO:0000313|EMBL:CCE65413.1};
GN OrderedLocusNames=TPHA_0L00570 {ECO:0000313|EMBL:CCE65413.1};
OS Tetrapisispora phaffii (strain ATCC 24235 / CBS 4417 / NBRC 1672 / NRRL
OS Y-8282 / UCD 70-5) (Yeast) (Fabospora phaffii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Tetrapisispora.
OX NCBI_TaxID=1071381 {ECO:0000313|EMBL:CCE65413.1, ECO:0000313|Proteomes:UP000005666};
RN [1] {ECO:0000313|EMBL:CCE65413.1, ECO:0000313|Proteomes:UP000005666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24235 / CBS 4417 / NBRC 1672 / NRRL Y-8282 / UCD 70-5
RC {ECO:0000313|Proteomes:UP000005666};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
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; HE612867; CCE65413.1; -; Genomic_DNA.
DR RefSeq; XP_003687847.1; XM_003687799.1.
DR AlphaFoldDB; G8BZT5; -.
DR STRING; 1071381.G8BZT5; -.
DR GeneID; 11531793; -.
DR KEGG; tpf:TPHA_0L00570; -.
DR eggNOG; KOG0053; Eukaryota.
DR HOGENOM; CLU_018986_2_3_1; -.
DR OMA; YKQDGVG; -.
DR OrthoDB; 6018at2759; -.
DR Proteomes; UP000005666; Chromosome 12.
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 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:UP000005666}.
FT MOD_RES 202
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 391 AA; 42042 MW; B992B0E61694D131 CRC64;
MGVQATDKFA TKAIHAGSHV DVHGSVIEPI SLSTTFKQSA PAEPIGEYEY SRSQNPNRKN
LEDAIAALEN GKYGLAFSSG SATTAIILQS LPQNSHAISI GDVYGGTHRY FSKVANTHGV
DTDFTNDLVA DLPKLVKENT RLVWIESPTN PTLKVTDIEL VAKTIKSLNK DILLVVDNTF
LSPYLSNPLN FGADIVVHSA TKYINGHSDV VLGVLATNSR DIYERLQFLQ NAVGAIPSPF
DAWLTHRGLK TLHLRVRQAA LNATKIAEFL AQSDNVVAVN YPGLPTNPDY AIVKKQHRDA
LGGGMISFRV KGGAEAASKF ASSTRLFTLA ESLGGIESLL EVPAVMTHGG IPKEQREASG
VFDDLVRLSV GIEDGDDLLE DVKAALQKAS N
//
