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Database: UniProt
Entry: A7TP41_VANPO
LinkDB: A7TP41_VANPO
Original site: A7TP41_VANPO 
ID   A7TP41_VANPO            Unreviewed;       391 AA.
AC   A7TP41;
DT   02-OCT-2007, integrated into UniProtKB/TrEMBL.
DT   02-OCT-2007, sequence version 1.
DT   24-JAN-2024, entry version 75.
DE   RecName: Full=cystathionine gamma-lyase {ECO:0000256|ARBA:ARBA00012085};
DE            EC=4.4.1.1 {ECO:0000256|ARBA:ARBA00012085};
DE   AltName: Full=Gamma-cystathionase {ECO:0000256|ARBA:ARBA00029853};
GN   ORFNames=Kpol_1044p10 {ECO:0000313|EMBL:EDO15951.1};
OS   Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS
OS   2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Vanderwaltozyma.
OX   NCBI_TaxID=436907 {ECO:0000313|Proteomes:UP000000267};
RN   [1] {ECO:0000313|EMBL:EDO15951.1, ECO:0000313|Proteomes:UP000000267}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 /
RC   NRRL Y-8283 / UCD 57-17 {ECO:0000313|Proteomes:UP000000267};
RX   PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA   Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.;
RT   "Independent sorting-out of thousands of duplicated gene pairs in two yeast
RT   species descended from a whole-genome duplication.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(2007).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|RuleBase:RU362118};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine
CC       from L-homocysteine and L-serine: step 2/2.
CC       {ECO:0000256|ARBA:ARBA00005038}.
CC   -!- SIMILARITY: Belongs to the trans-sulfuration enzymes family.
CC       {ECO:0000256|ARBA:ARBA00009077, ECO:0000256|RuleBase:RU362118}.
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DR   EMBL; DS480438; EDO15951.1; -; Genomic_DNA.
DR   RefSeq; XP_001643809.1; XM_001643759.1.
DR   AlphaFoldDB; A7TP41; -.
DR   STRING; 436907.A7TP41; -.
DR   GeneID; 5544062; -.
DR   KEGG; vpo:Kpol_1044p10; -.
DR   eggNOG; KOG0053; Eukaryota.
DR   HOGENOM; CLU_018986_2_3_1; -.
DR   InParanoid; A7TP41; -.
DR   OMA; YKQDGVG; -.
DR   OrthoDB; 6018at2759; -.
DR   PhylomeDB; A7TP41; -.
DR   Proteomes; UP000000267; Unassembled WGS sequence.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
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   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00023192};
KW   Cysteine biosynthesis {ECO:0000256|ARBA:ARBA00023192};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR001434-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000267}.
FT   MOD_RES         202
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   391 AA;  42177 MW;  F12738FCF9DF9977 CRC64;
     MGLKATDKFA TKAIHAGSHV DVHGSVIEPI SLSTTFKQSA PAQPIGEYEY SRSQNPNRKN
     LEDAIAALEN GKYGLAFSSG SATTSVILQS LPQGSHAVSI GDVYGGTHRY FTKVANTHGV
     ETTFTNNLVE ELPQLIKENT RLVWIESPTN PTLKVTDIGL VSQTIKSLKK DIILVVDNTF
     LSPYLSNPLN FGADIVVHSA TKYINGHSDV VLGVLATNDK DIYERLQFLQ NAIGAIPSPF
     DSWLVHRGLK TLHLRVRQAA LNATKIAEFL ASNENVIAVN YPGLPSSENF EVVKKQHRDA
     LGGGMISFRI KGGAEAASKF SSSTRLFTLA ESLGGIESLL EVPAVMTHGG IPKEQREASG
     VFDDLIRLSV GIEDSDDLLD DIKQALQGAT N
//
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