ID A0A0N1HFL5_9EURO Unreviewed; 441 AA.
AC A0A0N1HFL5;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 13-SEP-2023, entry version 33.
DE SubName: Full=Cystathionine beta-lyase {ECO:0000313|EMBL:KPI44137.1};
GN ORFNames=AB675_6130 {ECO:0000313|EMBL:KPI44137.1};
OS Phialophora attinorum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Phialophora.
OX NCBI_TaxID=1664694 {ECO:0000313|EMBL:KPI44137.1, ECO:0000313|Proteomes:UP000038010};
RN [1] {ECO:0000313|EMBL:KPI44137.1, ECO:0000313|Proteomes:UP000038010}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 131958 {ECO:0000313|EMBL:KPI44137.1,
RC ECO:0000313|Proteomes:UP000038010};
RA Moreno L.F., Stielow B.J., de Hoog S., Vicente V.A., Weiss V.A.,
RA de Vries M., Cruz L.M., Souza E.M.;
RT "Draft genome of the ant-associated black yeast Phialophora attae CBS
RT 131958.";
RL Submitted (JUN-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}.
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:KPI44137.1}.
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DR EMBL; LFJN01000004; KPI44137.1; -; Genomic_DNA.
DR RefSeq; XP_018004100.1; XM_018146397.1.
DR AlphaFoldDB; A0A0N1HFL5; -.
DR STRING; 1664694.A0A0N1HFL5; -.
DR GeneID; 28738277; -.
DR OrthoDB; 6018at2759; -.
DR Proteomes; UP000038010; 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:KPI44137.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000038010}.
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Polar residues"
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 441 AA; 47481 MW; 45E53BC55A288B1F CRC64;
MSEPSSSTPP VSNPKVSAMS KAFSQVDLDG HDLPPSPAPS SPRNGRQYSI ATQLVYSEGN
DQYNASSVPI YQSATFKQTS ATGGASDYDY TRSGNPTRTH LEKHLAKIMR AKRALVVSSG
MGALDVITRS LKPGDEVVTG DDLYGGSHRL LKYLSTHGEI IVHHVDTTTP EKVKEVLTSK
TALVLLETPT NPLIKVVDIA TIAAMAHEAN PSCVVSVDNT MLSPLLLNPL ELGADVVYES
GTKYLSGHHD LMAGVLAVKD EALADKYYFV INSTGCGLAP FDCWLLMRGI KTLKVRMDAQ
QANAQRLAEF LESVGFKVRY PGLKSHPQYD LFNTMARGAG AVLSFETGDI HLSERIVESA
KLFAISVSFG CVNSLISMPC RMSHASIDAK TRQERGVPED LIRLCVGIED GDDLLDDLSS
ALHDPLDGEV LAAHAAAKNE P
//
