ID A0A2R6P8U7_9APHY Unreviewed; 450 AA.
AC A0A2R6P8U7;
DT 20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Cystathionine gamma-lyase {ECO:0008006|Google:ProtNLM};
GN ORFNames=PHLCEN_2v5169 {ECO:0000313|EMBL:PSR87352.1};
OS Hermanssonia centrifuga.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Meruliaceae; Hermanssonia.
OX NCBI_TaxID=98765 {ECO:0000313|EMBL:PSR87352.1, ECO:0000313|Proteomes:UP000186601};
RN [1] {ECO:0000313|EMBL:PSR87352.1, ECO:0000313|Proteomes:UP000186601}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FBCC195 {ECO:0000313|EMBL:PSR87352.1,
RC ECO:0000313|Proteomes:UP000186601};
RA Granchi Z., Peng M., de Vries R.P., Hilden K., Makela M.R., Grigoriev I.,
RA Riley R.;
RT "Genome sequence of the basidiomycete white-rot fungus Phlebia
RT centrifuga.";
RL Submitted (FEB-2018) 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:PSR87352.1}.
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DR EMBL; MLYV02000514; PSR87352.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2R6P8U7; -.
DR STRING; 98765.A0A2R6P8U7; -.
DR Proteomes; UP000186601; 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; 2.
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:UP000186601}.
FT MOD_RES 224
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 450 AA; 48114 MW; AF04494F01F3E751 CRC64;
MSPAIYNGES SATNGHVVKK AHLDGFGTRA IHVGSEANQE TGAVIPSISL STTYKQNGIG
NHKGFEYSRS GNPNRNALEE TLASIETGGA HALAFSSGSA TTSTVLQSLG PDAHIVSVND
VYGGTFRYMT KVAKINQGLE TTFVDLEHAD DDTILAAIRP NTKLIWIESP TNPTLRLIDI
PRVVSLARSH PSSPLVLVDN TFLSPFYSSP LLLGADIVLH SLTKYVNGHS DVVMGALILP
AHHTELVEKL RFLQNAIGAI PSPYDCWLAQ RGVKTLHLRM KAHGTNALAV AQVLKRSPHV
EEVIYPGLAS HPRNDLAYRS LSPHARKFVD NFLATGTKNI DEDGVEADVG GFPYGGMISF
RIRGGAEEAE KFLTSTRLFT LAESLGGVES LAEHPAKMTH GSIPPAERAI LGIGDNLVRL
SVGVEEVEDL VADVEQALEA AASLRSNGSL
//