ID A0A193GCX3_9BORD Unreviewed; 396 AA.
AC A0A193GCX3;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE SubName: Full=Cystathionine beta-lyase {ECO:0000313|EMBL:ANN77872.1};
GN ORFNames=BAU07_12900 {ECO:0000313|EMBL:ANN77872.1};
OS Bordetella flabilis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=463014 {ECO:0000313|EMBL:ANN77872.1, ECO:0000313|Proteomes:UP000091926};
RN [1] {ECO:0000313|EMBL:ANN77872.1, ECO:0000313|Proteomes:UP000091926}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AU10664 {ECO:0000313|EMBL:ANN77872.1,
RC ECO:0000313|Proteomes:UP000091926};
RA LiPuma J.J., Spilker T.;
RT "Complete genome sequences of Bordetella bronchialis and Bordetella
RT flabilis.";
RL Submitted (JUN-2016) 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}.
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DR EMBL; CP016172; ANN77872.1; -; Genomic_DNA.
DR RefSeq; WP_066658241.1; NZ_CP016172.1.
DR AlphaFoldDB; A0A193GCX3; -.
DR STRING; 463014.BAU07_12900; -.
DR KEGG; bfz:BAU07_12900; -.
DR OrthoDB; 9805807at2; -.
DR Proteomes; UP000091926; Chromosome.
DR GO; GO:0004121; F:cystathionine beta-lyase activity; IEA:InterPro.
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 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.
DR PROSITE; PS00868; CYS_MET_METAB_PP; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000313|EMBL:ANN77872.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2}.
FT MOD_RES 205
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 396 AA; 43102 MW; E06E166B7D23DD83 CRC64;
MNSDWTQCAI TPAVSHEGYA SLGVAVYRAS TIPFENAHAY ATRRERGSEG YSYGLYGTPT
TRTLERKITV LEQGARTLLA PSGQGAITTV MLALLKTGDQ LMLPDTVYPP VRDFADRDLA
RLGIQVSYYD PLDTADLVER MGDRVRLVWV ESPGSTTMEV QDLPRIATLA HARGALVGCD
NTWATPLNFK PLAHGADIVV EGLTKYFCGH SDVMMGSITV RDLALGDSLR AFLGRQGLGV
SADDAALVLR GVETMALRLA YNARVATTLI DDIRRQPEVA RVLYPALPDS PGHALWRRDF
QGASGVFSVV FTPQAAPHVA AAMDALRIFV IGASWGGTRS LVAPMPVRAH RTVRPWEGDD
MVLRISIGIE GEADLAHDLK TFFEALRREM VRHGTA
//
