ID M4RQH0_9BIFI Unreviewed; 405 AA.
AC M4RQH0;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=Cystathionine beta-lyase {ECO:0000313|EMBL:AGH40777.1};
GN ORFNames=D805_0510 {ECO:0000313|EMBL:AGH40777.1};
OS Bifidobacterium thermophilum RBL67.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1254439 {ECO:0000313|EMBL:AGH40777.1, ECO:0000313|Proteomes:UP000011835};
RN [1] {ECO:0000313|EMBL:AGH40777.1, ECO:0000313|Proteomes:UP000011835}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RBL67 {ECO:0000313|EMBL:AGH40777.1,
RC ECO:0000313|Proteomes:UP000011835};
RX PubMed=23640377;
RA Jans C., Lacroix C., Follador R., Stevens M.J.;
RT "Complete Genome Sequence of the Probiotic Bifidobacterium thermophilum
RT Strain RBL67.";
RL Genome Announc. 1:E00191-13(2013).
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; CP004346; AGH40777.1; -; Genomic_DNA.
DR RefSeq; WP_015450038.1; NC_020546.1.
DR AlphaFoldDB; M4RQH0; -.
DR KEGG; btp:D805_0510; -.
DR PATRIC; fig|1254439.12.peg.511; -.
DR eggNOG; COG0626; Bacteria.
DR HOGENOM; CLU_018986_2_0_11; -.
DR Proteomes; UP000011835; Chromosome.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0019346; P:transsulfuration; IEA:InterPro.
DR CDD; cd00614; CGS_like; 1.
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:SF15; CYSTATHIONINE GAMMA-LYASE; 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.
DR PROSITE; PS00868; CYS_MET_METAB_PP; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000313|EMBL:AGH40777.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2}.
FT MOD_RES 208
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 405 AA; 43842 MW; 80FBFF992E324B9F CRC64;
MTRFNTQLVH GLPVNDNTTG AVNPPIYNSS TYAFESVESM PRWDYARSGN PTRDFLERQI
AQLEHGTRGF AFASGLAAIH AVLSIFKPGD RIVVGSNVYG GTYSQFNEHF TRWGLVSQPV
DTNDYEALEA AISGVGVAGD EDGASEPAKA VYFETLTNPL LQVNDVAAIA RIAHKYGAIV
IVDNTFVTPY LQQPLDLGAD IVLHSATKYL AGHSDVIAGL AVVRDDKLGE RVYYAQNRLG
GILPPAESDS VRRGIQTLGL RIERQQSNAV AIANWLLDNP LVATVHYPGV EGGRQPGDTE
KGLKGFGGVL GFEVVKGIDP AEILDNLHLF RLAVSLGAVE SLAELPCRMT HFELPREERL
KVGITDELIR LSIGIEDVND LIEDLDQAFA VAAKAAQPQL AETVQ
//
