ID W2SH07_9EURO Unreviewed; 463 AA.
AC W2SH07;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 13-SEP-2023, entry version 39.
DE SubName: Full=Cystathionine beta-lyase {ECO:0000313|EMBL:ETN47159.1};
GN ORFNames=HMPREF1541_01350 {ECO:0000313|EMBL:ETN47159.1};
OS Cyphellophora europaea CBS 101466.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Cyphellophoraceae; Cyphellophora.
OX NCBI_TaxID=1220924 {ECO:0000313|EMBL:ETN47159.1, ECO:0000313|Proteomes:UP000030752};
RN [1] {ECO:0000313|EMBL:ETN47159.1, ECO:0000313|Proteomes:UP000030752}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101466 {ECO:0000313|EMBL:ETN47159.1,
RC ECO:0000313|Proteomes:UP000030752};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Phialophora europaea CBS 101466.";
RL Submitted (MAR-2013) 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}.
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DR EMBL; KB822711; ETN47159.1; -; Genomic_DNA.
DR RefSeq; XP_008711871.1; XM_008713649.1.
DR AlphaFoldDB; W2SH07; -.
DR STRING; 1220924.W2SH07; -.
DR GeneID; 19968689; -.
DR VEuPathDB; FungiDB:HMPREF1541_01350; -.
DR eggNOG; KOG0053; Eukaryota.
DR HOGENOM; CLU_018986_2_1_1; -.
DR InParanoid; W2SH07; -.
DR OrthoDB; 6018at2759; -.
DR Proteomes; UP000030752; Unassembled WGS sequence.
DR GO; GO:0004121; F:cystathionine beta-lyase activity; IEA:InterPro.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0071266; P:'de novo' L-methionine biosynthetic process; 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; IPR006238; Cys_b_lyase_euk.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR NCBIfam; TIGR01329; cysta_beta_ly_E; 1.
DR PANTHER; PTHR11808:SF50; CYSTATHIONINE BETA-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 Lyase {ECO:0000313|EMBL:ETN47159.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000030752}.
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 243
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 463 AA; 49981 MW; AB907985E3767FFC CRC64;
MSNSSSSTPP LPNPKVGAMA KAFSEVDLDG HDLPPSPAPS SPRNGRQYSI ATQLVYSEGN
DQYNASSMPI YQSATFKQTS ATGGASDYDY TRSGNPTRTH LEKHLAKIMR AKRALVVSSG
MGALDVITRT LKPGDEVVTG DDLYGGSHRL LKYLSTHGGI VVHHVDTTTP EKLKEVLSAK
TAMVLLETPT NPLIKIVDIP TIADLAHAAN PNCVVSVDNT MLSPLLQNPL ELGADIVYES
GTKYLSGHHD LMAGVLAVKS EELAERYYFV INSTGCGLAP FDCWLLMRGI KTLKVRMDAQ
QANAMRIATF LESVGFKVRY PGLKSHPQYD LHNSMARGAG AVLSFETGDI HLSERIVESA
KLWAISVSFG CVNSLISMPC RMSHASIDAK TRQERGVPED LIRLCVGIED GEDLLDDLRS
AMVQAGAMDL SLEGLYAKNP TILQKDPKEG EKIAAEAAAE NEP
//