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Database: UniProt
Entry: A0A0N1LZ73_9ENTE
LinkDB: A0A0N1LZ73_9ENTE
Original site: A0A0N1LZ73_9ENTE 
ID   A0A0N1LZ73_9ENTE        Unreviewed;       405 AA.
AC   A0A0N1LZ73;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=cysteine-S-conjugate beta-lyase {ECO:0000256|ARBA:ARBA00012224};
DE            EC=4.4.1.13 {ECO:0000256|ARBA:ARBA00012224};
GN   ORFNames=AEQ18_09620 {ECO:0000313|EMBL:KPG70150.1};
OS   Enterococcus sp. RIT-PI-f.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=1690244 {ECO:0000313|EMBL:KPG70150.1, ECO:0000313|Proteomes:UP000037898};
RN   [1] {ECO:0000313|EMBL:KPG70150.1, ECO:0000313|Proteomes:UP000037898}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RIT-PI-f {ECO:0000313|EMBL:KPG70150.1,
RC   ECO:0000313|Proteomes:UP000037898};
RA   Tan N.E.H., Lee Y.P., Gan H.M., Savka M.A.;
RT   "Whole genome sequencing of endophytes isolated from poison ivy
RT   (Toxicodendron radicans).";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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:KPG70150.1}.
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DR   EMBL; LHOX01000016; KPG70150.1; -; Genomic_DNA.
DR   RefSeq; WP_054116123.1; NZ_LHOX01000016.1.
DR   AlphaFoldDB; A0A0N1LZ73; -.
DR   STRING; 1690244.AEQ18_09620; -.
DR   PATRIC; fig|1690244.3.peg.2513; -.
DR   OrthoDB; 9802872at2; -.
DR   Proteomes; UP000037898; 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:KPG70150.1};
KW   Transferase {ECO:0000313|EMBL:KPG70150.1}.
FT   DOMAIN          39..382
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   405 AA;  45924 MW;  9647A27A2D4983F3 CRC64;
     MTTDSFISDY ARQRTQTDSL KWDLVDQRFD GKDLLPLWVA DMDFAVPAAV TEALHRRVAQ
     GVFGYSIVPK DYVAAYQGWQ ERHWQTSFQE DWLRFSTGVV QSLYDLLHCF TKAGDAILIQ
     PPVYYPFFDS IKDTKRRIIE APLLAQGDTY QIDFDAFERK IKEESVKLFI FCSPHNPAGR
     VWYADEIKQL LAICQKYQVL VIADEIHGDL ILPGHRFVSA VTVAASLDFE GVIVVNSPSK
     TFNLAGLLLS HIWLPSETLQ QRYDAWAKQY KQTEVNIFGL TAAKAAYQHG DEWLEHILAV
     VAQNAETVAH GLRQAVPEVR TAPLEGTYLL WIDMRGLGID NLKQLVQDEA GLAVDYGAWF
     SQAYAGFIRL NLATTPTIIA AALDQLIRSI NTYKQQTFEE DIHDN
//
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