ID M9M3S9_PSEA3 Unreviewed; 737 AA.
AC M9M3S9;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 28-JUN-2023, entry version 33.
DE SubName: Full=Cystathionine beta-lyases {ECO:0000313|EMBL:GAC74990.1};
GN ORFNames=PANT_13c00101 {ECO:0000313|EMBL:GAC74990.1};
OS Pseudozyma antarctica (strain T-34) (Yeast) (Candida antarctica).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Moesziomyces.
OX NCBI_TaxID=1151754 {ECO:0000313|EMBL:GAC74990.1, ECO:0000313|Proteomes:UP000011976};
RN [1] {ECO:0000313|Proteomes:UP000011976}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T-34 {ECO:0000313|Proteomes:UP000011976};
RX PubMed=23558529; DOI=10.1128/genomea.00064-13;
RA Morita T., Koike H., Koyama Y., Hagiwara H., Ito E., Fukuoka T., Imura T.,
RA Machida M., Kitamoto D.;
RT "Genome sequence of the basidiomycetous yeast Pseudozyma antarctica T-34, a
RT producer of the glycolipid biosurfactants mannosylerythritol lipids.";
RL Genome Announc. 1:E0006413-E0006413(2013).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
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DR EMBL; DF196779; GAC74990.1; -; Genomic_DNA.
DR AlphaFoldDB; M9M3S9; -.
DR STRING; 1151754.M9M3S9; -.
DR OrthoDB; 35837at2759; -.
DR Proteomes; UP000011976; Unassembled WGS sequence.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0019346; P:transsulfuration; IEA:InterPro.
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; PTHR42699; -; 1.
DR PANTHER; PTHR42699:SF1; CYSTATHIONINE GAMMA-SYNTHASE-RELATED; 1.
DR Pfam; PF01053; Cys_Met_Meta_PP; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 4: Predicted;
KW Lyase {ECO:0000313|EMBL:GAC74990.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000011976}.
FT REGION 217..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 260..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 345..368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 260..289
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 737 AA; 79782 MW; 7AF20471785AFB07 CRC64;
MQLATPVPLP TAPPPSAGAA AACKKDLAVG TSIPANMPHA VSVSLPLWSD NIDYEEGRLS
NAMETGYPRF FIHRSIQRLA SLLSKKFARP DEACMLFPSA KIADRCRDYM RTLAPSPSPL
PIRIVRFSML EHAASNPASI PDANSSSSTA EHVADQLDAT HHHASSSSTT AHYIFIVFFP
AHLFPLAKSF WQHTGDGISS RQADRCLSLL EHSSRNAADQ HDVANKPAAA DAAPAPESAT
SISTDDVYKK SAGKRFYNRY TRTNSHTATP SPNSSAPQTP SSSGILQRPS TAGEDAAAAV
AASVEPVSSD LVTYVEERYG RNLPLTSAPS AKLALRRRIA GTLLSDRSEQ SATEAPGDQV
GESGRTGTGV TEDDVFLFPC GMSAIFHAHQ LAMRAAPRLV RADSPANVSP RAVGKSVCFG
FPYTDTLKIL QKFGPGCHFY GLGVDDDLDS LEQLLQTQQQ AGSEEAPVLA LFCEFPSNPL
LRSPNLPRIR ALADRYNVLV CVDETIGNFV NVEVLPYADV LVSSLTKVFS GDANVMGGSM
VLNPKGPHYG ALKDVMREHY EDTYFDEDAI FMERNSRDFI RRIVRIDANT RAVTEMLWRA
KEETHSDVVK QLFYPRYQTP ENYNVCRRRK AFTPLGAMEG DGGGGYGGLF SITFASEAAS
KAFYDTLQCA KGPSLGTNLT LASPYTILAH YGELEWAAQF GVERGLVRVS VGLEDESFLL
NMFGDSLDAA ARAHASA
//
