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
//