ID A0A0B9A4S9_9SPHN Unreviewed; 411 AA.
AC A0A0B9A4S9;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE SubName: Full=Cystathionine beta-lyase {ECO:0000313|EMBL:KHS45576.1};
DE EC=4.4.1.8 {ECO:0000313|EMBL:KHS45576.1};
GN ORFNames=NJ75_02595 {ECO:0000313|EMBL:KHS45576.1};
OS Novosphingobium subterraneum.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=48936 {ECO:0000313|EMBL:KHS45576.1, ECO:0000313|Proteomes:UP000031338};
RN [1] {ECO:0000313|EMBL:KHS45576.1, ECO:0000313|Proteomes:UP000031338}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12447 {ECO:0000313|EMBL:KHS45576.1,
RC ECO:0000313|Proteomes:UP000031338};
RA Gan H.M., Gan H.Y., Savka M.A.;
RT "Draft genome sequence of Novosphingobium subterraneum DSM 12447.";
RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L,L-cystathionine = L-homocysteine + NH4(+) + pyruvate;
CC Xref=Rhea:RHEA:13965, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:28938, ChEBI:CHEBI:58161, ChEBI:CHEBI:58199;
CC Evidence={ECO:0000256|ARBA:ARBA00001535};
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|ARBA:ARBA00009077, 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:KHS45576.1}.
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DR EMBL; JRVC01000012; KHS45576.1; -; Genomic_DNA.
DR RefSeq; WP_039335118.1; NZ_JRVC01000012.1.
DR AlphaFoldDB; A0A0B9A4S9; -.
DR STRING; 48936.NJ75_02595; -.
DR PATRIC; fig|48936.3.peg.2602; -.
DR Proteomes; UP000031338; 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 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; IPR006233; Cys_b_lyase_bac.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR NCBIfam; TIGR01324; cysta_beta_ly_B; 1.
DR PANTHER; PTHR43500; CYSTATHIONINE BETA-LYASE-RELATED; 1.
DR PANTHER; PTHR43500:SF1; CYSTATHIONINE BETA-LYASE-RELATED; 1.
DR Pfam; PF01053; Cys_Met_Meta_PP; 1.
DR PIRSF; PIRSF001434; CGS; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000313|EMBL:KHS45576.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2}.
FT MOD_RES 220
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 411 AA; 43926 MW; FDC3DD34527C0EBF CRC64;
MSSSDDFENY GAATRGVLAG RREEWTGTPG HPGAVVNPAV WRASTHLYPD MSALRAHPAN
EDGRFYYGRR GSPTQWGLSE ALTQLEGDSA GTVLYPSGVA AIAGALLTVL RPGDVLLMTD
NAYEPSRIMG RGLLKDFGIE TRWFDPTDLA SFEAACCERT RCVLLESPGS LTMEVQDVPA
IAAAAKARGI VSVLDNTWAS PLGFQGLRHG VDIVVMSLTK HVSGHSDCMM GSASAGPEWY
RKLRLRSQGM GTVVSPDDAA LMLRGLRTMK HRLEAETASA LGIAQWLEGR PEVARVLCPM
LPGSPGHELW RRDFTGGCGL FSFVLKGGTS AARDALIDAL TLFGIGYSWG GFESLATPVD
PAGIRTASQW PLKGMDAEDR FGVRLSIGLE DSTDLIADLE RGLAVWAGAT A
//
