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Database: UniProt
Entry: A0A0S8K376_9BACE
LinkDB: A0A0S8K376_9BACE
Original site: A0A0S8K376_9BACE 
ID   A0A0S8K376_9BACE        Unreviewed;       401 AA.
AC   A0A0S8K376;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Cystathionine beta-lyase {ECO:0000313|EMBL:KPL16369.1};
GN   ORFNames=AMS26_04880 {ECO:0000313|EMBL:KPL16369.1};
OS   Bacteroides sp. SM23_62.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=1703352 {ECO:0000313|EMBL:KPL16369.1, ECO:0000313|Proteomes:UP000050819};
RN   [1] {ECO:0000313|EMBL:KPL16369.1, ECO:0000313|Proteomes:UP000050819}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SM23_62 {ECO:0000313|EMBL:KPL16369.1};
RX   PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA   Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT   "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT   among widespread estuary sediment bacteria.";
RL   Microbiome 3:14-14(2015).
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}.
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:KPL16369.1}.
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DR   EMBL; LJUP01000029; KPL16369.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0S8K376; -.
DR   PATRIC; fig|1703352.3.peg.1881; -.
DR   Proteomes; UP000050819; 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   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.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000313|EMBL:KPL16369.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR001434-2}.
FT   MOD_RES         205
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   401 AA;  44393 MW;  D4B755ACB1D00186 CRC64;
     MKKNDPASSI QDLRQFGEFG GVNPSITDSS TYTFLAADTM EDTFHGETQG CFLYSRHWNP
     SNKYLADALA ALEETESGWI TASGMAAITC TILELCNSGD HIVTSVTTYG GTFAFLKNYL
     PKFNIEVSFV NIADIESVER AIQPNTRLIY TESLTNPLLQ ISDIPALSDI CRRNGIQLIV
     DNTFSPMIIS PARLGADIIV YSMTKFINGK NDCVAGAICS STDFIKRLSD VNSGTAMLLG
     PVLDPLRSSS ILKNLHTLHI RMKQHGHNAM FLARRFSELG LKVIYPGLES HPQHDLMKEL
     MNEEFGFGGM LAIDFGDHQT SNKIMQLMQE NDIGYLAVSL GYFKTLFSCS GHSTSSELPP
     EIQKEIGLSE GLTRFSVGLD NDIERTYDKI LYCMKELKIL S
//
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