ID A0A0A8X3D6_9BACI Unreviewed; 393 AA.
AC A0A0A8X3D6;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Cystathionine beta-lyase {ECO:0000313|EMBL:GAM14480.1};
DE EC=4.4.1.8 {ECO:0000313|EMBL:GAM14480.1};
GN ORFNames=SAMD00020551_2631 {ECO:0000313|EMBL:GAM14480.1};
OS Mesobacillus selenatarsenatis SF-1.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Mesobacillus.
OX NCBI_TaxID=1321606 {ECO:0000313|EMBL:GAM14480.1, ECO:0000313|Proteomes:UP000031014};
RN [1] {ECO:0000313|EMBL:GAM14480.1, ECO:0000313|Proteomes:UP000031014}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SF-1 {ECO:0000313|EMBL:GAM14480.1,
RC ECO:0000313|Proteomes:UP000031014};
RA Kuroda M., Sei K., Yamashita M., Ike M.;
RT "Whole genome shotgun sequence of Bacillus selenatarsenatis SF-1.";
RL Submitted (JUN-2013) 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:GAM14480.1}.
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DR EMBL; BASE01000058; GAM14480.1; -; Genomic_DNA.
DR RefSeq; WP_041966228.1; NZ_BASE01000058.1.
DR AlphaFoldDB; A0A0A8X3D6; -.
DR STRING; 1321606.SAMD00020551_2631; -.
DR OrthoDB; 9803887at2; -.
DR Proteomes; UP000031014; Unassembled WGS sequence.
DR GO; GO:0004121; F:cystathionine beta-lyase activity; IEA:UniProtKB-EC.
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:GAM14480.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000031014}.
FT MOD_RES 199
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 393 AA; 43221 MW; 0BCF4EBA79091008 CRC64;
MSHQYTFETQ LLHNKHKFDP ATGGVSVPIQ HASTFHQSTA DKFGKYDYSR SLNPTREALE
EIIAELEGGV RGFAFSSGMA AISTAFLLLS QGDHVVVTVD VYGGTYRMVT QVLNRFGIEH
TFVDMTDLDA VEQAIRPNTT LLYAETPSNP LLKVTDIQAV SEIAKKHGAY TFVDNTFMTP
YLQRPLELGA DIVLHSATKF LSGHSDTVAG LAVVKDEELA KRLYSLQNSF GAVLGVQDAW
LVMRGIKTLS VRMNQSQESA VKIAGFLKEH PLIKKVYYPG LAGHPQSKLQ LQQAYGPGAV
LSFELKNAEF LARFIEKVRL PVFAVSLGAV ESILSYPAKM SHAAMPQDER KKRGISDGLL
RLSVGLESAD DLITDFEQAL DSILTLEAQK EEV
//
