ID C4R0F4_KOMPG Unreviewed; 390 AA.
AC C4R0F4;
DT 07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 07-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE SubName: Full=Cystathionine beta-lyase, converts cystathionine into homocysteine {ECO:0000313|EMBL:CAY68978.1};
GN OrderedLocusNames=PAS_chr2-1_0358 {ECO:0000313|EMBL:CAY68978.1};
OS Komagataella phaffii (strain GS115 / ATCC 20864) (Yeast) (Pichia pastoris).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Phaffomycetaceae; Komagataella.
OX NCBI_TaxID=644223 {ECO:0000313|EMBL:CAY68978.1, ECO:0000313|Proteomes:UP000000314};
RN [1] {ECO:0000313|EMBL:CAY68978.1, ECO:0000313|Proteomes:UP000000314}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GS115 / ATCC 20864 {ECO:0000313|Proteomes:UP000000314};
RX PubMed=19465926; DOI=10.1038/nbt.1544;
RA De Schutter K., Lin Y.C., Tiels P., Van Hecke A., Glinka S.,
RA Weber-Lehmann J., Rouze P., Van de Peer Y., Callewaert N.;
RT "Genome sequence of the recombinant protein production host Pichia
RT pastoris.";
RL Nat. Biotechnol. 27:561-566(2009).
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; FN392320; CAY68978.1; -; Genomic_DNA.
DR RefSeq; XP_002491258.1; XM_002491213.1.
DR AlphaFoldDB; C4R0F4; -.
DR SMR; C4R0F4; -.
DR STRING; 644223.C4R0F4; -.
DR EnsemblFungi; CAY68978; CAY68978; PAS_chr2-1_0358.
DR GeneID; 8199046; -.
DR KEGG; ppa:PAS_chr2-1_0358; -.
DR eggNOG; KOG0053; Eukaryota.
DR HOGENOM; CLU_018986_2_1_1; -.
DR InParanoid; C4R0F4; -.
DR OMA; IANGVCN; -.
DR OrthoDB; 6018at2759; -.
DR Proteomes; UP000000314; Chromosome 2.
DR GO; GO:0005777; C:peroxisome; IEA:EnsemblFungi.
DR GO; GO:0004121; F:cystathionine beta-lyase activity; IEA:EnsemblFungi.
DR GO; GO:0047804; F:cysteine-S-conjugate beta-lyase activity; IEA:EnsemblFungi.
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:EnsemblFungi.
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 Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000000314}.
FT MOD_RES 200
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 390 AA; 43072 MW; C89257B7B4F58ED4 CRC64;
MEEKFDIETE LVRLGFEDQY NSCNPPLYQT ATFRQDSLSN MGAYDYTRSG NPTRTTLQNY
LSRIMGAKAT FAVSSGMSAL DVIVRLLDPG DEVIAGDDLY GGTHRLLTFL KNKKQLIVNH
YDTTDTELMK QKITKNTRMI FLESPTNPLI KVVDVRSITA HAHEINPNCI VVFDNTMMSP
VLMSPLTDLG VDIQYESATK YLNGHHDIMS GVLATNSEKL AQDLYFVINS TGCGLAPFDC
WLLLRGLKTL ALRIERQQEN AIKIAQFLIT VPGLKVRSVA LPDHPQYELH KSMAKGPGAV
LSFETGSVET SSKIIEACKI WSITVSFGCV NSLISLPCQM SHASIDPDTR AERDLPEDLV
RLCVGIENVN DLIKDLAAAL RVGGISVPAQ
//
