ID A0A087BN06_9BIFI Unreviewed; 428 AA.
AC A0A087BN06;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Cystathionine beta-lyase {ECO:0000313|EMBL:KFI72406.1};
DE EC=2.5.1.48 {ECO:0000313|EMBL:KFI72406.1};
GN ORFNames=BMIN_0301 {ECO:0000313|EMBL:KFI72406.1};
OS Bifidobacterium minimum.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1693 {ECO:0000313|EMBL:KFI72406.1, ECO:0000313|Proteomes:UP000029014};
RN [1] {ECO:0000313|EMBL:KFI72406.1, ECO:0000313|Proteomes:UP000029014}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 11592 {ECO:0000313|EMBL:KFI72406.1,
RC ECO:0000313|Proteomes:UP000029014};
RA Ventura M., Milani C., Lugli G.A.;
RT "Genomics of Bifidobacteria.";
RL Submitted (MAR-2014) 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|ARBA:ARBA00009077, ECO:0000256|RuleBase:RU362118}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KFI72406.1}.
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DR EMBL; JGZD01000009; KFI72406.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A087BN06; -.
DR STRING; 1693.BMIN_0301; -.
DR eggNOG; COG0626; Bacteria.
DR Proteomes; UP000029014; Unassembled WGS sequence.
DR GO; GO:0016846; F:carbon-sulfur lyase activity; IEA:UniProt.
DR GO; GO:0003962; F:cystathionine gamma-synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0102028; F:cystathionine gamma-synthase activity (acts on O-phosphohomoserine); IEA:UniProtKB-EC.
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:SF92; CYSTATHIONINE GAMMA-SYNTHASE; 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:KFI72406.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000029014};
KW Transferase {ECO:0000313|EMBL:KFI72406.1}.
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 243
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 428 AA; 44788 MW; 4A1DA66297ACD5EB CRC64;
MTATTNRPTN SAVSTNPASS TNSENSAGAA SPVSPVDLSS VDLSAMAVAT RAIHAGQEPD
AATGAVVPPI YMTSTFKQDG VGGLRGGYDY SRSVNPTRDS FDTQLAAIEG ARHALAFSSG
LAAIDVLLRS TVKPGDRILL GNDVYGGTYR LLSQVFVPWG VGLDVVDMTD LESVSHALES
AAYSYVWVET PSNPLLGITD IAATSEVAHR HGAKVVVDNT FASPILQRPL DEGADAVVYS
TTKYIGGHSD VVGGAVVLND DAIRDRVAFL QNAAGAVPSP FDSWLDIRGL KTLDLRVHRH
SENALAVATW LQSRPEVERV WYPGLESHPG HDIAARQMRG GFGGMVSIQL ASGEDAAKAF
AGATSIFTLA ESLGGVESLI EHPAAMTHAS VSGTTLEVPS NLVRLSVGVE DADDLIADLD
AAFARIAR
//
