ID A0A1G6A223_EUBOX Unreviewed; 386 AA.
AC A0A1G6A223;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Cystathionine beta-lyase {ECO:0000313|EMBL:SDB02484.1};
GN ORFNames=SAMN02910417_00172 {ECO:0000313|EMBL:SDB02484.1};
OS Eubacterium oxidoreducens.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC Eubacterium.
OX NCBI_TaxID=1732 {ECO:0000313|EMBL:SDB02484.1, ECO:0000313|Proteomes:UP000199228};
RN [1] {ECO:0000313|EMBL:SDB02484.1, ECO:0000313|Proteomes:UP000199228}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 3217 {ECO:0000313|EMBL:SDB02484.1,
RC ECO:0000313|Proteomes:UP000199228};
RA de Groot N.N.;
RL Submitted (OCT-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|ARBA:ARBA00009077, ECO:0000256|RuleBase:RU362118}.
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DR EMBL; FMXR01000004; SDB02484.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G6A223; -.
DR STRING; 1732.SAMN02910417_00172; -.
DR OrthoDB; 9780685at2; -.
DR Proteomes; UP000199228; Unassembled WGS sequence.
DR GO; GO:0016846; F:carbon-sulfur lyase activity; IEA:UniProt.
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.
DR PROSITE; PS00868; CYS_MET_METAB_PP; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000313|EMBL:SDB02484.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000199228}.
FT MOD_RES 199
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 386 AA; 41741 MW; D1AA5EAF1D07D3D7 CRC64;
MSKYKKIESA LIHGGIYGDK QTGAVNVPIY QTSTYEQRGL GENTGWEYSR TGNPTRAALE
ALIAELESGK AGFAFGSGMA AITAVLSLFK AGDKIIISSN VYGGTFRVLD KIFNNFNISY
SIEDTTNPEA LESKITSDVK AILIESPANP LLTVTDIAAI ADIAKKKGIL SIVDNTFMTP
YLQRPIELGV DIVIHSATKY LGGHSDVVSG LVVVNDDELA DRLAFIQNST GGVLGPFDSF
LLIRGIKTLG VRLDRHVENA EKVAAYLKNH KAVKNVYYPG LPDAQGYEIN KKQAKNGGAM
ISFELYENYD IAKFFSALNL IALAESLGGV ESLACHPASM THASIPYEVR QKVGITDGLI
RLSIGIENID DLIEDLEQAI GESEER
//