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Database: UniProt
Entry: B5F5X4_SALA4
LinkDB: B5F5X4_SALA4
Original site: B5F5X4_SALA4 
ID   B5F5X4_SALA4            Unreviewed;       400 AA.
AC   B5F5X4;
DT   14-OCT-2008, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2008, sequence version 1.
DT   27-MAR-2024, entry version 61.
DE   RecName: Full=cysteine-S-conjugate beta-lyase {ECO:0000256|ARBA:ARBA00012224};
DE            EC=4.4.1.13 {ECO:0000256|ARBA:ARBA00012224};
GN   OrderedLocusNames=SeAg_B1608 {ECO:0000313|EMBL:ACH52209.1};
OS   Salmonella agona (strain SL483).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=454166 {ECO:0000313|EMBL:ACH52209.1, ECO:0000313|Proteomes:UP000008819};
RN   [1] {ECO:0000313|EMBL:ACH52209.1, ECO:0000313|Proteomes:UP000008819}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SL483 {ECO:0000313|EMBL:ACH52209.1,
RC   ECO:0000313|Proteomes:UP000008819};
RX   PubMed=21602358; DOI=10.1128/JB.00297-11;
RA   Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G.,
RA   Leclerc J.E., Ravel J., Cebula T.A.;
RT   "Comparative genomics of 28 Salmonella enterica isolates: evidence for
RT   CRISPR-mediated adaptive sublineage evolution.";
RL   J. Bacteriol. 193:3556-3568(2011).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC       aminotransferase family. MalY/PatB cystathionine beta-lyase subfamily.
CC       {ECO:0000256|ARBA:ARBA00037974}.
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DR   EMBL; CP001138; ACH52209.1; -; Genomic_DNA.
DR   RefSeq; WP_000347153.1; NC_011149.1.
DR   AlphaFoldDB; B5F5X4; -.
DR   KEGG; sea:SeAg_B1608; -.
DR   HOGENOM; CLU_017584_15_0_6; -.
DR   Proteomes; UP000008819; Chromosome.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   CDD; cd00609; AAT_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; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR027619; C-S_lyase_PatB-like.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   NCBIfam; TIGR04350; C_S_lyase_PatB; 1.
DR   PANTHER; PTHR43525; PROTEIN MALY; 1.
DR   PANTHER; PTHR43525:SF1; PROTEIN MALY; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000313|EMBL:ACH52209.1};
KW   Transferase {ECO:0000313|EMBL:ACH52209.1}.
FT   DOMAIN          36..384
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   400 AA;  45110 MW;  117C5901D5F6353C CRC64;
     MDFNQIINRN NTGSVKWDFI ERHFGDGAGK LLPMWVSDFD FACPPEVQAA LHQRIEHGVF
     GYSERDEAYF NALLHWFSSR HQLTLKQEWV CSVEGVVPGL ALLVQMLTHP GDGVVVQGPY
     YGSFAKIITL NGRKLLENPL SESPDDGYQM DFCQLERLFR HERPPLMILC NPHNPTGRCW
     SANELEQLLL LCEAYDVTLI SDEIWADLLL PGETFTSVLH LGERWHKRVI SATAASKTFG
     LSSLRISNFL IPDPTLRQRF LSRLDAHGLD VFNALSVQAA TIAWNESRQW LDSLLDYLAE
     NRRWFVEQAT EYLPWARIVP AQGTYLLWMD CKKLGLDDEQ LKWVMADVAG IAPSMGSGFG
     PAGSGFIRLN LGCPRTYLEM AIDGLKRISV KTIKGIPIGG
//
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