UniProt: A0A0U0WRI3

Database: UniProt
Entry: A0A0U0WRI3_SALET

LinkDB:  A0A0U0WRI3_SALET 
Original site:  A0A0U0WRI3_SALET

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Ontology (3)   
   GO (3)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (15)   
   EMBL (15)   
Protein domain (7)   
   InterPro (5)   
   Pfam (1)   
   PROSITE (1)   
Literature (1)   
   PubMed (1)   
All databases (28)   

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ID   A0A0U0WRI3_SALET        Unreviewed;       395 AA.
AC   A0A0U0WRI3;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 53.
DE   SubName: Full=Cystathionine beta-lyase {ECO:0000313|EMBL:SUE45998.1};
DE            EC=4.4.1.8 {ECO:0000313|EMBL:SUE45998.1};
GN   Name=metC {ECO:0000313|EMBL:SUE45998.1};
GN   ORFNames=B7N00_06950 {ECO:0000313|EMBL:EDG5016697.1}, B7N01_17345
GN   {ECO:0000313|EMBL:EDG4996187.1}, B7N35_08045
GN   {ECO:0000313|EMBL:EDG5125981.1}, B7N72_18370
GN   {ECO:0000313|EMBL:EDG5372064.1}, B7N78_01180
GN   {ECO:0000313|EMBL:EDG5278406.1}, B7N80_13515
GN   {ECO:0000313|EMBL:EDG5289397.1}, B7N84_04795
GN   {ECO:0000313|EMBL:EDG5265666.1}, DRU31_00480
GN   {ECO:0000313|EMBL:EBS2450827.1}, E0916_03035
GN   {ECO:0000313|EMBL:ECF1444951.1}, EJV93_00965
GN   {ECO:0000313|EMBL:ECA2719818.1}, EWC73_15005
GN   {ECO:0000313|EMBL:ECE8537500.1}, G0B02_20825
GN   {ECO:0000313|EMBL:HAC6381512.1}, G0D18_01870
GN   {ECO:0000313|EMBL:HAC6679435.1}, G2206_04080
GN   {ECO:0000313|EMBL:HAE0433961.1}, NCTC5754_00803
GN   {ECO:0000313|EMBL:SUE45998.1};
OS   Salmonella enterica subsp. enterica serovar Bovismorbificans.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=58097 {ECO:0000313|EMBL:SUE45998.1, ECO:0000313|Proteomes:UP000254190};
RN   [1] {ECO:0000313|EMBL:HAC6381512.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BCW_3301 {ECO:0000313|EMBL:HAC6381512.1}, M123
RC   {ECO:0000313|EMBL:HAC6679435.1}, and MS140073
RC   {ECO:0000313|EMBL:HAE0433961.1};
RX   PubMed=30286803;
RA   Souvorov A., Agarwala R., Lipman D.J.;
RT   "SKESA: strategic k-mer extension for scrupulous assemblies.";
RL   Genome Biol. 19:153-153(2018).
RN   [2] {ECO:0000313|EMBL:SUE45998.1, ECO:0000313|Proteomes:UP000254190}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC5754 {ECO:0000313|EMBL:SUE45998.1,
RC   ECO:0000313|Proteomes:UP000254190};
RG   Pathogen Informatics;
RA   Doyle S.;
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:HAC6679435.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BCW_3301 {ECO:0000313|EMBL:HAC6381512.1}, M123
RC   {ECO:0000313|EMBL:HAC6679435.1}, and MS140073
RC   {ECO:0000313|EMBL:HAE0433961.1};
RG   NCBI Pathogen Detection Project;
RL   Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EMBL:EBS2450827.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=136768 {ECO:0000313|EMBL:EDG4996187.1}, 138330
RC   {ECO:0000313|EMBL:EDG5289397.1}, 143652
RC   {ECO:0000313|EMBL:EDG5372064.1}, 273631
RC   {ECO:0000313|EMBL:EDG5016697.1}, 330535
RC   {ECO:0000313|EMBL:EDG5265666.1}, 333944
RC   {ECO:0000313|EMBL:EDG5278406.1}, 337042
RC   {ECO:0000313|EMBL:EDG5125981.1}, 387147
RC   {ECO:0000313|EMBL:EBS2450827.1}, 470200
RC   {ECO:0000313|EMBL:ECE8537500.1}, 598023
RC   {ECO:0000313|EMBL:ECA2719818.1}, and 692616
RC   {ECO:0000313|EMBL:ECF1444951.1};
RA   Ashton P.M., Dallman T., Nair S., De Pinna E., Peters T., Grant K.;
RL   Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L,L-cystathionine = L-homocysteine + NH4(+) + pyruvate;
CC         Xref=Rhea:RHEA:13965, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:28938, ChEBI:CHEBI:58161, ChEBI:CHEBI:58199;
CC         Evidence={ECO:0000256|ARBA:ARBA00001535};
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; AAGUWJ010000001; EBS2450827.1; -; Genomic_DNA.
DR   EMBL; AAHTVM010000001; ECA2719818.1; -; Genomic_DNA.
DR   EMBL; AAIJHK010000013; ECE8537500.1; -; Genomic_DNA.
DR   EMBL; AAIKGE010000002; ECF1444951.1; -; Genomic_DNA.
DR   EMBL; AAMEJW010000019; EDG4996187.1; -; Genomic_DNA.
DR   EMBL; AAMEJY010000003; EDG5016697.1; -; Genomic_DNA.
DR   EMBL; AAMEKY010000005; EDG5125981.1; -; Genomic_DNA.
DR   EMBL; AAMEMC010000002; EDG5265666.1; -; Genomic_DNA.
DR   EMBL; AAMEMH010000001; EDG5278406.1; -; Genomic_DNA.
DR   EMBL; AAMEML010000013; EDG5289397.1; -; Genomic_DNA.
DR   EMBL; AAMEMP010000025; EDG5372064.1; -; Genomic_DNA.
DR   EMBL; DAAMEZ010000018; HAC6381512.1; -; Genomic_DNA.
DR   EMBL; DAAMHM010000001; HAC6679435.1; -; Genomic_DNA.
DR   EMBL; DAAQQK010000003; HAE0433961.1; -; Genomic_DNA.
DR   EMBL; UGVQ01000002; SUE45998.1; -; Genomic_DNA.
DR   RefSeq; WP_000130262.1; NZ_WFIN01000002.1.
DR   AlphaFoldDB; A0A0U0WRI3; -.
DR   SMR; A0A0U0WRI3; -.
DR   Proteomes; UP000254190; Unassembled WGS sequence.
DR   Proteomes; UP000839929; 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; IPR006233; Cys_b_lyase_bac.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   NCBIfam; TIGR01324; cysta_beta_ly_B; 1.
DR   PANTHER; PTHR43500; CYSTATHIONINE BETA-LYASE-RELATED; 1.
DR   PANTHER; PTHR43500:SF1; CYSTATHIONINE BETA-LYASE-RELATED; 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:SUE45998.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR001434-2}.
FT   MOD_RES         210
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   395 AA;  42872 MW;  38B0A41A1A063447 CRC64;
     MTDKQLDTKL VNAGRSKKYT LGSVNSVIQR ASSLVFDTVE AKKHATRNLA NGELFYGRRG
     TLTHFSLQEA MCELEGGAGC ALFPCGAAAV ANTILAFVEQ GDHILMTNTA YEPSQDFCSK
     ILGKLGVTTS WFDPLIGADI TQHIQPNTKV VFLESPGSIT MEVHDIPSIV SAVRRVAPEA
     VIMIDNTWAA GVLFKALEFD IDISIQAGTK YLIGHSDAMV GTAVANARCW EQLRENAYLM
     GQMLDADTAY MTSRGLRTLG VRLRQHQESS LKIAAWLANH PQVARVNHPA LPGSKGHAFW
     KRDFTGSSGL FSFVLNKKLT EAELSAYLDN FSLFSMAYSW GGYESLIIAN QPEQIAAIRP
     AGGVDFTGTL VRVHIGLESV DDLIADLAAG FARIV
//

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