ID   A0A158EAQ7_9BURK        Unreviewed;       399 AA.
AC   A0A158EAQ7;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   SubName: Full=Cystathionine beta-lyase {ECO:0000313|EMBL:SAL03863.1};
GN   ORFNames=AWB78_06705 {ECO:0000313|EMBL:SAL03863.1};
OS   Caballeronia calidae.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Caballeronia.
OX   NCBI_TaxID=1777139 {ECO:0000313|EMBL:SAL03863.1, ECO:0000313|Proteomes:UP000071859};
RN   [1] {ECO:0000313|EMBL:SAL03863.1, ECO:0000313|Proteomes:UP000071859}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 29321 {ECO:0000313|EMBL:SAL03863.1};
RA   Oliw E.H.;
RL   Submitted (JAN-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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FCOX02000056; SAL03863.1; -; Genomic_DNA.
DR   RefSeq; WP_062610795.1; NZ_FCOX02000056.1.
DR   AlphaFoldDB; A0A158EAQ7; -.
DR   OrthoDB; 9805807at2; -.
DR   Proteomes; UP000071859; Unassembled WGS sequence.
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:SAL03863.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR001434-2}.
FT   MOD_RES         214
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   399 AA;  43267 MW;  C5D910DF24038F6C CRC64;
     MTDSNNNAPD RDLQTRIVQP KDRITPGFES FSVPVARAST VVFPDLATMR ALVWSDDSKW
     RYGLHGTPTT IALAQRLAAI EGGEHALLQP SGLAAISNVY FALVKAGDHV LVPDNAYSPN
     REHADWLAAD FGLEVSYYDP MTGAGIADSI RPNTKLIWLE APGSVTMEVQ DVPAIVAVAR
     AKGIVTAIDN TYSAGLAFKP FEHGVDISVQ ALTKYQSGGS DILMGATITR DVELHKKMKR
     ARMRMGIGVS ADDASLVLRS LPTMKTRYEA HDRTAFALAT WLKTRPEVAA VLHPALEDCP
     GHAFYERDFK GGAGGLFSIV FDGRYSAAQV DAFVEALDLF AIGWSWGGAH SLAMPYNIGS
     MRTASQWPHE GVLVRFYIGL EAETDLRADL EAALVKAFA
//