ID A0A1Y1YB93_9FUNG Unreviewed; 390 AA.
AC A0A1Y1YB93;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Cystathionine gamma-lyase {ECO:0008006|Google:ProtNLM};
GN ORFNames=K493DRAFT_315094 {ECO:0000313|EMBL:ORX95222.1};
OS Basidiobolus meristosporus CBS 931.73.
OC Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota;
OC Entomophthoromycotina; Basidiobolomycetes; Basidiobolales; Basidiobolaceae;
OC Basidiobolus.
OX NCBI_TaxID=1314790 {ECO:0000313|EMBL:ORX95222.1, ECO:0000313|Proteomes:UP000193498};
RN [1] {ECO:0000313|EMBL:ORX95222.1, ECO:0000313|Proteomes:UP000193498}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 931.73 {ECO:0000313|EMBL:ORX95222.1,
RC ECO:0000313|Proteomes:UP000193498};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ORX95222.1}.
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DR EMBL; MCFE01000182; ORX95222.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y1YB93; -.
DR STRING; 1314790.A0A1Y1YB93; -.
DR InParanoid; A0A1Y1YB93; -.
DR OrthoDB; 6018at2759; -.
DR Proteomes; UP000193498; 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.
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:UP000193498}.
FT MOD_RES 201
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 390 AA; 41780 MW; 50AD527112EAF3FB CRC64;
MTLSEFTGFG TLAIHTGQEP DGVTGAVIPP ISLSTTFAQS AAGVHSGYEY SRAGNPTRHS
FEQAVAALEK GNFGLAFSSG SATTATIAHL LPAGSHVVLV NDVYGGTYRY FTKVATVTGI
EHTFVDLVNP DNIKSALREN TKLVWIETPT NPTLRLVDIE AIAKYAHEAG AILVVDNTFM
SPYFQNPLTL GADIVVHSGT KYLNGHSDVV IGVAVLKDEE LYTKLKFLQN AIGATPSPFD
CFLANRGLKT LHVRMKQHAE NAMTVAKALE ASDKVEEVIY PGLKSHKQHE LAKKQTAGFG
GMVSFRIKGN LDNSNKFLQT LKVFTLAESL GGVESLAELP SVMTHGAVSA EDRAKLGITD
TLIRLSVGIE DTEDLVNDVK RALEAAVPSQ
//
