ID K6U562_9CLOT Unreviewed; 397 AA.
AC K6U562;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=cysteine-S-conjugate beta-lyase {ECO:0000256|ARBA:ARBA00012224};
DE EC=4.4.1.13 {ECO:0000256|ARBA:ARBA00012224};
GN ORFNames=A370_01771 {ECO:0000313|EMBL:EKQ56696.1};
OS Clostridium sp. Maddingley MBC34-26.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1196322 {ECO:0000313|EMBL:EKQ56696.1, ECO:0000313|Proteomes:UP000001325};
RN [1] {ECO:0000313|EMBL:EKQ56696.1, ECO:0000313|Proteomes:UP000001325}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Maddingley MBC34-26 {ECO:0000313|Proteomes:UP000001325};
RX PubMed=23405323;
RA Rosewarne C.P., Greenfield P., Li D., Tran-Dinh N., Bradbury M.I.,
RA Midgley D.J., Hendry P.;
RT "Draft Genome Sequence of Clostridium sp. Maddingley, Isolated from Coal-
RT Seam Gas Formation Water.";
RL Genome Announc. 1:E00081-12(2013).
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:EKQ56696.1}.
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DR EMBL; ALXI01000064; EKQ56696.1; -; Genomic_DNA.
DR AlphaFoldDB; K6U562; -.
DR STRING; 1196322.A370_01771; -.
DR PATRIC; fig|1196322.3.peg.1715; -.
DR eggNOG; COG1168; Bacteria.
DR Proteomes; UP000001325; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:UniProt.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
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 Reference proteome {ECO:0000313|Proteomes:UP000001325}.
FT DOMAIN 32..387
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 397 AA; 46052 MW; B54485D5943ED3F0 CRC64;
MKYDFETLVS RKNIGSSKWN LMNKYNMDID ENIIPLSVAD MEFKNPPEIT EGLKKYIDSS
IFGYTIATEA YYKSICNWME RRHDWKIAKE SIIEFAGVVP ALYMIIRALT NQEDNVLVLS
PVYYPFYKAI TLNKRNLIKS ELVHCGDHYE IDFEDFEENA KLENTKLFIL CNPHNPVGRV
WTKDELIKIG RICIENNILI VSDEIHSDLI MPGFKHTVFA NISEEFANHS VICTAPSKTF
NLAGLQVSNI IVSNKKIRDK IVTERRLSTG NMGLNIFAYK ACEIAYNECE EWLEELLEVI
NKNKNLVEEF VKTNLPLIKV INMEGTYLQW LDFRNLEKDH KALEKFMTTE AMLFLDEGYI
FGDEGRGFER INLACPTSVL QKALERLLEA VKRCYKE
//
