ID A0A0V8HBC8_9BACI Unreviewed; 378 AA.
AC A0A0V8HBC8;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Cystathionine beta-lyase/cystathionine gamma-synthase {ECO:0000313|EMBL:SCC28093.1};
GN ORFNames=GA0061094_3658 {ECO:0000313|EMBL:SCC28093.1};
OS [Bacillus] enclensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Rossellomorea.
OX NCBI_TaxID=1402860 {ECO:0000313|EMBL:SCC28093.1, ECO:0000313|Proteomes:UP000181997};
RN [1] {ECO:0000313|EMBL:SCC28093.1, ECO:0000313|Proteomes:UP000181997}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SGD-1123 {ECO:0000313|EMBL:SCC28093.1,
RC ECO:0000313|Proteomes:UP000181997};
RA Seilhamer J.J.;
RL Submitted (AUG-2016) 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; FMAU01000005; SCC28093.1; -; Genomic_DNA.
DR RefSeq; WP_058299583.1; NZ_KQ758486.1.
DR AlphaFoldDB; A0A0V8HBC8; -.
DR OrthoDB; 9803887at2; -.
DR Proteomes; UP000181997; Unassembled WGS sequence.
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:SF90; 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:SCC28093.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2}.
FT MOD_RES 203
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 378 AA; 41220 MW; B6B8E9E3D34BAD85 CRC64;
MKFTTKVVHS QLKGTEEIRS KTTPIYQTSA FSFKSLEELE GFYEGKSPYL YTRTGNPNTD
ELGGMVAALE GAPAGVATSS GLSAILAAVL AVVQSGDHII AAEDLYGGTF HMLKEELKGF
GIETTFVDFT SREEIEQAIT PRTKLLYSET VTNPFMRVED IQQLVELAEK HNLKTIIDNT
FATPYLRQPY LEGVDLVAHS ATKYIGGHSD ITAGVVTGKE ELVKKAREKV VNMGSNLSPF
EAWLTARGAK TLGLRMEAQA RNSGILADNL RSNQHIKHVY YPDNLSEKGH GAIVTIELDA
SCNISAFFKS LGWIKIVPTL AGVETTVSYP LGTSHRALPK EAQQKLGINT HVVRISLGIE
DAEDIVAQFN EAIEKSVG
//
