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
//