ID A0A1W1WLZ9_SULTA Unreviewed; 384 AA.
AC A0A1W1WLZ9;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Cystathionine beta-lyase {ECO:0000313|EMBL:SMC07334.1};
GN ORFNames=SAMN00768000_3333 {ECO:0000313|EMBL:SMC07334.1};
OS Sulfobacillus thermosulfidooxidans (strain DSM 9293 / VKM B-1269 / AT-1).
OC Bacteria; Bacillota; Clostridia; Eubacteriales;
OC Clostridiales Family XVII. Incertae Sedis; Sulfobacillus.
OX NCBI_TaxID=929705 {ECO:0000313|EMBL:SMC07334.1, ECO:0000313|Proteomes:UP000192660};
RN [1] {ECO:0000313|Proteomes:UP000192660}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 9293 {ECO:0000313|Proteomes:UP000192660};
RA Varghese N., Submissions S.;
RL Submitted (APR-2017) 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; FWWY01000001; SMC07334.1; -; Genomic_DNA.
DR RefSeq; WP_020374740.1; NZ_FWWY01000001.1.
DR AlphaFoldDB; A0A1W1WLZ9; -.
DR STRING; 28034.BFX07_07000; -.
DR OrthoDB; 9780685at2; -.
DR Proteomes; UP000192660; 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 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; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR11808:SF15; CYSTATHIONINE GAMMA-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:SMC07334.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000192660}.
FT MOD_RES 202
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 384 AA; 42868 MW; 8798033A06E97A26 CRC64;
MPAHESRNWH LESLAAHSGV GQDRLYGAVS TPIYQTVTYQ HPGTELGPYD YSRTENPTRH
AAQEAINRLD NGAGALLYSS GMAALTALVH TLQQGDHVLI TEDAYGGTYR IMVDIFSKFG
IASSMVNTRD IDQVKQHITS KTRLFIVETP SNPLLRISPL EELAELAHAH HAELAVDNTF
MTAVRQRPLE LGADYVVYSA TKYLAGHNDV LAGAIVCKTP EQYDKLNELT NATGSVLGPW
DAWLLLRGLK TLAIRMDRQE SNARRIAEFL SHHQNIRHVY YPELADHDMR ERHLRQASGY
GAMLSFVLTH PEEYAAVMDR LQVILPAVSL GGVESLITHP YNETHRELPE SMRRQLGIVP
GLMRLSVGIE HIDDLLTDLD NALR
//
