ID C5CWI8_VARPS Unreviewed; 400 AA.
AC C5CWI8;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=cysteine-S-conjugate beta-lyase {ECO:0000256|ARBA:ARBA00012224};
DE EC=4.4.1.13 {ECO:0000256|ARBA:ARBA00012224};
GN OrderedLocusNames=Vapar_2106 {ECO:0000313|EMBL:ACS18743.1};
OS Variovorax paradoxus (strain S110).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Variovorax.
OX NCBI_TaxID=543728 {ECO:0000313|EMBL:ACS18743.1};
RN [1] {ECO:0000313|EMBL:ACS18743.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=S110 {ECO:0000313|EMBL:ACS18743.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G., Orwin P.,
RA Leadbetter J.R., Spain J.C., Han J.I.;
RT "Complete sequence of chromosome 1 of Variovorax paradoxus S110.";
RL Submitted (JUN-2009) 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 ---------------------------------------------------------------------------
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; CP001635; ACS18743.1; -; Genomic_DNA.
DR AlphaFoldDB; C5CWI8; -.
DR STRING; 543728.Vapar_2106; -.
DR KEGG; vap:Vapar_2106; -.
DR eggNOG; COG1168; Bacteria.
DR HOGENOM; CLU_017584_15_0_4; -.
DR OrthoDB; 9803354at2; -.
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:ACS18743.1};
KW Transferase {ECO:0000313|EMBL:ACS18743.1}.
FT DOMAIN 50..393
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 400 AA; 45317 MW; 017C4D00FD41D562 CRC64;
MTSNFDQLIS RQGTNALAED GYEKYLFGAE PLVPPLQVPS TELVSMWVAD MQFAAPEAAI
GAMRERLAHP IFGYTMNFDD QLYDAFSAWC DRRYGWRFDR EQMQISLGVI PALFGLVEYV
CAPGDKVLSL TPSYGYFKHA VVQRDRVFET SPLRKTDDGD YEIDFEDFER KVRDPAVKLF
FLCHPHNPTG RVWTEDELRR MAELCLSNGV KIVSDEIHCD LTRTGVTHVP LAKLFPSSKD
IITCMAVSKT FNLAGLMVAT VVIPDPELRA TWKRRHYPFV NPLSLAAAVG AYRDGEAWLD
ALRKYLDDNF AFMHRYLALW LPKARFQIPQ ATYLAWVDLS AYFDDSVNLT RFFLEKAGLI
LEGGEMFVAN GAQCIRLNLA CPRIQAEEAL KKLVAAIASH
//
