ID   A0A0P1IKA0_9RHOB        Unreviewed;       365 AA.
AC   A0A0P1IKA0;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Cystathionine beta-lyase {ECO:0000313|EMBL:CUK19345.1};
DE            EC=4.4.1.8 {ECO:0000313|EMBL:CUK19345.1};
GN   Name=metC {ECO:0000313|EMBL:CUK19345.1};
GN   ORFNames=RUE5091_04377 {ECO:0000313|EMBL:CUK19345.1};
OS   Ruegeria denitrificans.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Ruegeria.
OX   NCBI_TaxID=1715692 {ECO:0000313|EMBL:CUK19345.1, ECO:0000313|Proteomes:UP000051260};
RN   [1] {ECO:0000313|EMBL:CUK19345.1, ECO:0000313|Proteomes:UP000051260}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 5091 {ECO:0000313|EMBL:CUK19345.1,
RC   ECO:0000313|Proteomes:UP000051260};
RG   Swine Surveillance;
RL   Submitted (SEP-2015) 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   ---------------------------------------------------------------------------
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; CYUD01000022; CUK19345.1; -; Genomic_DNA.
DR   RefSeq; WP_058283976.1; NZ_CYUD01000022.1.
DR   AlphaFoldDB; A0A0P1IKA0; -.
DR   STRING; 1715692.RUE5091_04377; -.
DR   OrthoDB; 9805807at2; -.
DR   Proteomes; UP000051260; 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; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR11808:SF93; CYSTATHIONINE GAMMA-LYASE-RELATED; 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.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000313|EMBL:CUK19345.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR001434-2}.
FT   MOD_RES         192
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   365 AA;  39204 MW;  20CDFBDB6D5015B1 CRC64;
     MAPKTGEMLH LRGNALNAGD PVALPLTQSS MYHLPGGTDG LPTYGRVDNP TWLHLEHVLA
     HLEEAPCLTF PSGMGAISAA LFATLKTGSR LLIPSDGYYV TRVLADRFLS GLGMSVTERP
     TTTFTEGGFD GFDVVFVESP SNPGLDMLDL PAIAAAVRAA GGITIADNTT LTPLGQRPLE
     LGIDVVVSSD TKAMAGHSDL LMGHVASRNA QIMERVEEWR RVSGAIPGPH EAWMLHRGLE
     TLDVRFERMC SSAQVLAERL ADHPAVKQIR YPGLTGDPSH ALAAAQTARF GFLLSITLET
     EEKAETFINA CPMLRPATSF GGVHSSAERR ARWGDDVDPA FIRLSVGCEP VEELWQAIET
     SLNAL
//