ID W1SCP5_9BACI Unreviewed; 377 AA.
AC W1SCP5;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Cystathionine beta-lyase {ECO:0000313|EMBL:ETI67181.1};
DE EC=4.4.1.8 {ECO:0000313|EMBL:ETI67181.1};
GN ORFNames=BAVI_18919 {ECO:0000313|EMBL:ETI67181.1};
OS Neobacillus vireti LMG 21834.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Neobacillus.
OX NCBI_TaxID=1131730 {ECO:0000313|EMBL:ETI67181.1, ECO:0000313|Proteomes:UP000018877};
RN [1] {ECO:0000313|EMBL:ETI67181.1, ECO:0000313|Proteomes:UP000018877}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 21834 {ECO:0000313|EMBL:ETI67181.1,
RC ECO:0000313|Proteomes:UP000018877};
RX PubMed=24708037; DOI=10.1111/1462-2920.12478;
RA Mania D., Heylen K., van Spanning R.J., Frostegard A.;
RT "The nitrate-ammonifying and nosZ-carrying bacterium Bacillus vireti is a
RT potent source and sink for nitric and nitrous oxide under high nitrate
RT conditions.";
RL Environ. Microbiol. 16:3196-3210(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|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:ETI67181.1}.
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DR EMBL; ALAN01000103; ETI67181.1; -; Genomic_DNA.
DR RefSeq; WP_024029953.1; NZ_ALAN01000103.1.
DR AlphaFoldDB; W1SCP5; -.
DR STRING; 220686.AA980_13440; -.
DR PATRIC; fig|1131730.3.peg.3971; -.
DR eggNOG; COG0626; Bacteria.
DR OrthoDB; 9803887at2; -.
DR Proteomes; UP000018877; Unassembled WGS sequence.
DR GO; GO:0004121; F:cystathionine beta-lyase activity; 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.
DR PROSITE; PS00868; CYS_MET_METAB_PP; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000313|EMBL:ETI67181.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000018877}.
FT MOD_RES 195
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 377 AA; 40946 MW; 6B7C6A011A91838F CRC64;
MRRKTKLIHG GISEDPATGA VSFPIYQVST YKQEGVGGHK GFEYSRTGNP TRNALEELIK
DLEGGEAGFA FGSGMAAMTA VMMLFNSGDH VILTDDVYGG SFRVMTKVLN RLGIDSTFVD
TTDLENIKRE IRANTKAIHL ETPTNPLLKI TDIKAVAKLA KEHNLLTIVD NTFSTPYWQN
PIELGADIVL HSATKYLGGH SDVVAGLAVV NSKELAEELH FIQNSTGGIL GPQDSWLLIR
GMRTLGIRLE EMESNTAAIV AFLQGHSAVK KVFYPGLETH PNHELAKRQT RGFGGMVSFD
VGSAENADRL LSKVKYFTLA ESLGAVESLI SVPARMTHAS IPAERRAELG ITDGLVRISV
GLEDIEDLLE DLAQALE
//
