ID W4EM93_9BACL Unreviewed; 395 AA.
AC W4EM93;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Cystathionine beta-lyase {ECO:0000313|EMBL:ETT80906.1};
GN ORFNames=C176_19364 {ECO:0000313|EMBL:ETT80906.1};
OS Viridibacillus arenosi FSL R5-213.
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Viridibacillus.
OX NCBI_TaxID=1227360 {ECO:0000313|EMBL:ETT80906.1, ECO:0000313|Proteomes:UP000019062};
RN [1] {ECO:0000313|EMBL:ETT80906.1, ECO:0000313|Proteomes:UP000019062}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSL R5-213 {ECO:0000313|EMBL:ETT80906.1,
RC ECO:0000313|Proteomes:UP000019062};
RX PubMed=24422886; DOI=10.1186/1471-2164-15-26;
RA Moreno Switt A.I., Andrus A.D., Ranieri M.L., Orsi R.H., Ivy R.,
RA den Bakker H.C., Martin N.H., Wiedmann M., Boor K.J.;
RT "Genomic comparison of sporeforming bacilli isolated from milk.";
RL BMC Genomics 15:26-26(2014).
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:ETT80906.1}.
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DR EMBL; ASQA01000042; ETT80906.1; -; Genomic_DNA.
DR AlphaFoldDB; W4EM93; -.
DR PATRIC; fig|1227360.4.peg.3933; -.
DR eggNOG; COG0626; Bacteria.
DR Proteomes; UP000019062; 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: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:ETT80906.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000019062}.
FT MOD_RES 202
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 395 AA; 42635 MW; 58C89A57701E5FCA CRC64;
MSSINENIET SLITASTRGD YEQKTGAVNV PIYLSSTFDQ EHFDSFGPYD YSRSGNPTRD
ALEKTIAELE GGARGFAFSS GIAAIASAFM ILEAGDHIVV TSEVYGGTYR FVTQVLTKFG
VEHTFADFSD LTSVEAAIRP NTKVLYIETP ANPLLGITDI EGVVAIAKAN GALTFLDNTF
MTPLYQRPLD LGVDVVLHSA TKFLGGHSDI IAGLAVTKDV ELGNRIYFMQ NSFGAILGAQ
DSFSLIQGIK TLNARLTQST ASASKLANYL EAHELVEEVH FPGLKSHPGH DIHAKQAKSA
GAVLSFKLPN REITKAFVEH VQIPIFAVSL GGVESILSYP ATMSHAAIPK EEREKRGITD
GLLRFSVGLE NIDDLIADFE QAFVKAKELT VVGNK
//
