ID A0A0P1E2C4_9RHOB Unreviewed; 366 AA.
AC A0A0P1E2C4;
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:CUH42554.1};
DE EC=4.4.1.8 {ECO:0000313|EMBL:CUH42554.1};
GN Name=metC {ECO:0000313|EMBL:CUH42554.1};
GN ORFNames=RUM4293_01442 {ECO:0000313|EMBL:CUH42554.1};
OS Ruegeria atlantica.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Ruegeria.
OX NCBI_TaxID=81569 {ECO:0000313|EMBL:CUH42554.1, ECO:0000313|Proteomes:UP000050786};
RN [1] {ECO:0000313|EMBL:CUH42554.1, ECO:0000313|Proteomes:UP000050786}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 4293 {ECO:0000313|EMBL:CUH42554.1,
RC ECO:0000313|Proteomes:UP000050786};
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}.
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DR EMBL; CYPS01000022; CUH42554.1; -; Genomic_DNA.
DR RefSeq; WP_058272612.1; NZ_CYPS01000022.1.
DR AlphaFoldDB; A0A0P1E2C4; -.
DR Proteomes; UP000050786; 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:CUH42554.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2}.
FT MOD_RES 193
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 366 AA; 39556 MW; 6597F9294021BFFE CRC64;
MKPPKTGEML HLRGNALNKG DPVALPLTQS SMYHLPGAPD GHPTYGRVEN PTWVHLEHVL
AHLEDAPCLT FPSGMGAISA ALFATVKAGS HILIPSDGYY VTRLLADRFL SNLGVSVTER
PTTAFAEGGF GGFDVVFLES PSNPGLDMMD LPAIATAVRT AGGLTIADNT TMTPLGQRPL
DLGIDVVVAS DTKAMGGHSD LLMGHVASRN AQIMERVEEW RRVSGAIPGP HEAWLLHRGL
ETLDVRFDRM CASAQVLAER LAEHEAVKQI RYPGLSDDPS YALAKAQTSR FGFLLSITLE
TEEKAETFIN TCPMLRPATS FGGVHSSAER RARWGDDVDP AFIRLSVGCE PIEELWQAIE
ISLNAL
//