ID A0A0S1Y026_9BORD Unreviewed; 401 AA.
AC A0A0S1Y026;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE SubName: Full=Cystathionine beta-lyase {ECO:0000313|EMBL:ALM83421.1};
GN ORFNames=ASB57_10990 {ECO:0000313|EMBL:ALM83421.1};
OS Bordetella sp. N.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=1746199 {ECO:0000313|EMBL:ALM83421.1, ECO:0000313|Proteomes:UP000064621};
RN [1] {ECO:0000313|EMBL:ALM83421.1, ECO:0000313|Proteomes:UP000064621}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=N {ECO:0000313|EMBL:ALM83421.1,
RC ECO:0000313|Proteomes:UP000064621};
RA Hou L.;
RT "Draft genome of Bordetella sp. N.";
RL Submitted (NOV-2015) 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; CP013111; ALM83421.1; -; Genomic_DNA.
DR RefSeq; WP_057652267.1; NZ_CP013111.1.
DR AlphaFoldDB; A0A0S1Y026; -.
DR STRING; 1746199.ASB57_10990; -.
DR OrthoDB; 9805807at2; -.
DR Proteomes; UP000064621; 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 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:ALM83421.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000064621}.
FT MOD_RES 214
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 401 AA; 42833 MW; 7975A23E802C611C CRC64;
MSHADGLRIQ TRLAHAGAPT PVDGRAGPVN VPVVRTSTVR FPNTATHAAL AASRAAGEAV
ATYGRHGLDT HRALEEAVAT LEGGHRAVLA PSGLAAITLV LLATLTAGDH ALVSDSVYSP
VRKVDHTLLQ RYGIEVEYFS PARGDLEARI RPTTRLLYLE SPSSLLYEVL DLPALAAIAR
RHDVVVAVDN TWSGGLYYQP LALGANISVQ AATKYLGGHS DAMLGVVTVD SPALARSIGA
IHDALGFSVS ADEAYLVLRG LRTLDVRLAR HQVNATEVAR YLARHADVGR VYYPALPQDP
GHALWQRDFS GASGLVSFAF RGDDARAAAV FIDHLRHFAI GASWGGYESL ALEAAPARLS
EHSYWDGRGP VVRLHIGLEH PQDLIDDLSR AFQATADALR C
//
