ID G3B2H4_CANTC Unreviewed; 397 AA.
AC G3B2H4;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=Cystathionine gamma-lyase {ECO:0008006|Google:ProtNLM};
GN ORFNames=CANTEDRAFT_113467 {ECO:0000313|EMBL:EGV65093.1};
OS Candida tenuis (strain ATCC 10573 / BCRC 21748 / CBS 615 / JCM 9827 / NBRC
OS 10315 / NRRL Y-1498 / VKM Y-70) (Yeast) (Yamadazyma tenuis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Yamadazyma.
OX NCBI_TaxID=590646 {ECO:0000313|Proteomes:UP000000707};
RN [1] {ECO:0000313|EMBL:EGV65093.1, ECO:0000313|Proteomes:UP000000707}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10573 {ECO:0000313|EMBL:EGV65093.1}, and ATCC 10573 / BCRC
RC 21748 / CBS 615 / JCM 9827 / NBRC 10315 / NRRL Y-1498 / VKM Y-70
RC {ECO:0000313|Proteomes:UP000000707};
RX PubMed=21788494; DOI=10.1073/pnas.1103039108;
RA Wohlbach D.J., Kuo A., Sato T.K., Potts K.M., Salamov A.A., LaButti K.M.,
RA Sun H., Clum A., Pangilinan J.L., Lindquist E.A., Lucas S., Lapidus A.,
RA Jin M., Gunawan C., Balan V., Dale B.E., Jeffries T.W., Zinkel R.,
RA Barry K.W., Grigoriev I.V., Gasch A.P.;
RT "Comparative genomics of xylose-fermenting fungi for enhanced biofuel
RT production.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:13212-13217(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}.
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DR EMBL; GL996515; EGV65093.1; -; Genomic_DNA.
DR EMBL; GL996515; EGV65094.1; -; Genomic_DNA.
DR RefSeq; XP_006685899.1; XM_006685836.1.
DR RefSeq; XP_006685900.1; XM_006685837.1.
DR STRING; 590646.G3B2H4; -.
DR GeneID; 18246972; -.
DR KEGG; cten:CANTEDRAFT_113467; -.
DR eggNOG; KOG0053; Eukaryota.
DR HOGENOM; CLU_018986_2_3_1; -.
DR OrthoDB; 6018at2759; -.
DR Proteomes; UP000000707; Unassembled WGS sequence.
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.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000000707}.
FT MOD_RES 209
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 397 AA; 42335 MW; EA61D22E033EA410 CRC64;
MTKDDTTQYG FGTNAIHAGA PIDPHTGAVI EAISLSTTFG QSQPSKPIGV YEYSRSANPN
RDNFEQAVAA LEGAQYALAI SSGSATTALL VQSLPVDSHI ISGGDVYGGT HRYFTKVAST
HGVTASFVPD LVDDLEAALR PNTRMVWLET PSNPTLKVTD IAAVKQVLQR HQDATGSRVV
LVVDNTFLSP YISNPLAHGA DVVIHSVTKY INGHSDVVMG VLATNDDSLA ETYRFLQNAI
GSVPSAFDSW LAHRGLKTLH LRVRHAATSA LSIAQHLEAH PKVKAVNYPG LKTHANHGVV
LKQHRDGLGG GMISFRIHGG ADAASVFTSS TKLFTLAESL GGIESLIEVP AIMTHGGIPR
EEREANGVFD DLVRVSVGIE DTVDLLRDID QALDKVQ
//
