ID W1SH03_9BACI Unreviewed; 404 AA.
AC W1SH03;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=cysteine-S-conjugate beta-lyase {ECO:0000256|ARBA:ARBA00012224};
DE EC=4.4.1.13 {ECO:0000256|ARBA:ARBA00012224};
GN ORFNames=BAVI_12769 {ECO:0000313|EMBL:ETI68345.1};
OS Neobacillus vireti LMG 21834.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Neobacillus.
OX NCBI_TaxID=1131730 {ECO:0000313|EMBL:ETI68345.1, ECO:0000313|Proteomes:UP000018877};
RN [1] {ECO:0000313|EMBL:ETI68345.1, ECO:0000313|Proteomes:UP000018877}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 21834 {ECO:0000313|EMBL:ETI68345.1,
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 -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC aminotransferase family. MalY/PatB cystathionine beta-lyase subfamily.
CC {ECO:0000256|ARBA:ARBA00037974}.
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:ETI68345.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ALAN01000071; ETI68345.1; -; Genomic_DNA.
DR RefSeq; WP_024028739.1; NZ_ALAN01000071.1.
DR AlphaFoldDB; W1SH03; -.
DR STRING; 220686.AA980_17525; -.
DR PATRIC; fig|1131730.3.peg.2670; -.
DR eggNOG; COG1168; Bacteria.
DR OrthoDB; 9802872at2; -.
DR Proteomes; UP000018877; Unassembled WGS sequence.
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:ETI68345.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000018877};
KW Transferase {ECO:0000313|EMBL:ETI68345.1}.
FT DOMAIN 61..378
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 404 AA; 46439 MW; 5D7F1A1A7401744C CRC64;
MKYNFDEVIN RRGTYSLKWD GGELIKEIGI TERYDEDSIP LFTADMDLPV PQPLIDALHK
TVDHKIFGYS IFPEEYYEAI QHWFSRRHNW NIKKEEIIYS PGTVNALNIA VRAFTEPGDG
IIIQRPVYPP FTAAIENNRR QVINNALKCD EEGYYSIDFE DFEAKAKDKK TKMFILCNPH
NPTGRVLNSE ELQKLAEICA ENDVLIIADE IHGDLIRRNL TFTPIAKSTD KGDHIITCTA
INKTFNVAGL HCTNVIIPNP ELRKTFIDTM GFQLASPFTI SALIAVYNEG EDWLNQLKEY
IDGTMEWVVN FLAERMPHVK VRIPEGTYVM WMDFSAYGLS PEEVHDRIYN KANVLLEDGS
MFGEEGLQYQ RICIPSPRPI IKEAFERIAR EFEDLHVGVR PPLS
//
