位置:首页 > 蛋白库 > CBL_MYCLE
CBL_MYCLE
ID   CBL_MYCLE               Reviewed;         402 AA.
AC   Q9CBM9;
DT   14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Putative cystathionine beta-lyase;
DE            Short=CBL;
DE            EC=4.4.1.13;
DE   AltName: Full=Beta-cystathionase;
DE   AltName: Full=Cysteine lyase;
DE   AltName: Full=Cysteine-S-conjugate beta-lyase;
GN   OrderedLocusNames=ML1794;
OS   Mycobacterium leprae (strain TN).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=272631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TN;
RX   PubMed=11234002; DOI=10.1038/35059006;
RA   Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA   Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA   Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA   Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA   Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA   Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA   Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA   Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA   Barrell B.G.;
RT   "Massive gene decay in the leprosy bacillus.";
RL   Nature 409:1007-1011(2001).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L,L-cystathionine = L-homocysteine + NH4(+) + pyruvate;
CC         Xref=Rhea:RHEA:13965, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:28938, ChEBI:CHEBI:58161, ChEBI:CHEBI:58199;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an S-substituted L-cysteine + H2O = a thiol + NH4(+) +
CC         pyruvate; Xref=Rhea:RHEA:18121, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:28938, ChEBI:CHEBI:29256, ChEBI:CHEBI:58717; EC=4.4.1.13;
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo
CC       pathway; L-homocysteine from L-cystathionine: step 1/1.
CC   -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC       aminotransferase family. MalY/PatB cystathionine beta-lyase subfamily.
CC       {ECO:0000305}.
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; AL583923; CAC30747.1; -; Genomic_DNA.
DR   PIR; C87133; C87133.
DR   RefSeq; NP_302217.1; NC_002677.1.
DR   RefSeq; WP_010908538.1; NC_002677.1.
DR   AlphaFoldDB; Q9CBM9; -.
DR   SMR; Q9CBM9; -.
DR   STRING; 272631.ML1794; -.
DR   EnsemblBacteria; CAC30747; CAC30747; CAC30747.
DR   KEGG; mle:ML1794; -.
DR   PATRIC; fig|272631.5.peg.3415; -.
DR   Leproma; ML1794; -.
DR   eggNOG; COG1168; Bacteria.
DR   HOGENOM; CLU_017584_15_2_11; -.
DR   OMA; RINIGCP; -.
DR   UniPathway; UPA00051; UER00078.
DR   Proteomes; UP000000806; Chromosome.
DR   GO; GO:0004121; F:cystathionine beta-lyase activity; IEA:RHEA.
DR   GO; GO:0047804; F:cysteine-S-conjugate beta-lyase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProt.
DR   GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Lyase; Methionine biosynthesis;
KW   Pyridoxal phosphate; Reference proteome.
FT   CHAIN           1..402
FT                   /note="Putative cystathionine beta-lyase"
FT                   /id="PRO_0000163849"
FT   MOD_RES         236
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   402 AA;  43861 MW;  7696E8684CB220D6 CRC64;
     MTSNPLEQLT IEQLQCRTSM KWRAHPEDVL PLWVAEMDVL LAPTVAEAVH RAVDNGDTGY
     PYGTTFAEAI SEFASQRWQW HDLDVSRTAI VPDVMLGVVE MLRLITDRGD GVIVSPPVYP
     PFYAFVTHDG RRVLEAPLGR DGRLDLAALQ DAFSRARRSS GPNGKVAYLL CNPHNPTGSV
     HTVAELHGVA ELARRFGVRV ISDEIHAPLV LSGARFTPYL SIPGAENAFA LMSATKGWNL
     CGLKAAIAIA GREAAADLRR IPKEVSHGPS HLGIIAHTAA FRTGSSWLDA LLQGLEANRA
     LLRDLVTKHL PGVRYQRPQG TYLTWLDCRH LGFDEQINEG LAAISDLSGP ARWFLDHSRV
     ALTSGHAFGT GGVGHVRVNF ATSQAILIEA LSRMGRALVN FR
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024