ID A0A0D2FF09_9EURO Unreviewed; 465 AA.
AC A0A0D2FF09;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Cystathionine beta-lyase {ECO:0000313|EMBL:KIW66618.1};
GN ORFNames=PV04_05935 {ECO:0000313|EMBL:KIW66618.1};
OS Phialophora macrospora.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Phialophora.
OX NCBI_TaxID=1851006 {ECO:0000313|EMBL:KIW66618.1, ECO:0000313|Proteomes:UP000054266};
RN [1] {ECO:0000313|EMBL:KIW66618.1, ECO:0000313|Proteomes:UP000054266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 27337 {ECO:0000313|EMBL:KIW66618.1,
RC ECO:0000313|Proteomes:UP000054266};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Capronia semiimmersa CBS27337.";
RL Submitted (JAN-2015) 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; KN846959; KIW66618.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D2FF09; -.
DR STRING; 5601.A0A0D2FF09; -.
DR HOGENOM; CLU_018986_2_1_1; -.
DR OrthoDB; 6018at2759; -.
DR Proteomes; UP000054266; 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:KIW66618.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2}.
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 245
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 465 AA; 49941 MW; 1E1FE463F7A05134 CRC64;
MSESGSSSTP PLKNPKLSAM SKAFAQVDLD GHDLPPSPVP SSPRSGRQYA LATQLVYSEG
NDQYNASSVP IYQSATFKQT SATGGVSNDY DYTRSGNPTR THLEKHLAKV MRAKRALVVS
SGMGALDVIS RQLRPGDEVV TGDDLYGGTN RLLKYLSTHG GIIVHHVDTT TPEKVQEVLS
EKTAMVLLET PTNPLIKIVD IPTIASMAHA ANPLCLVSVD NTMLSPLLQN PLELGADIVY
ESGTKYLSGH HDLMAGVIAV NDEALGDRFY FTINASGCGL APFDCWLLMR GIKTLKVRMD
AQQANAMRIA QFLESAGFKV RYPGLKSHPQ YDLFHSMARG AGAVLSFETG DVQLSERIVE
SAKLWAISVS FGCVNSLISM PCRMSHASID AKTRAERGVP EDLIRLCVGI EDGDDLLDDL
QSALVQSGAM NVTLDGIYAK KATVGDEHPA EGEHLAAKAA AINEP
//
