CBL_THET8
ID CBL_THET8 Reviewed; 354 AA.
AC Q5SHW0;
DT 31-JAN-2018, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 84.
DE RecName: Full=Cystathionine beta-lyase {ECO:0000303|PubMed:15893507};
DE Short=CBL {ECO:0000250|UniProtKB:Q93QC6};
DE EC=4.4.1.13 {ECO:0000269|PubMed:15893507};
DE AltName: Full=Beta-cystathionase {ECO:0000303|PubMed:15893507};
DE AltName: Full=Cysteine lyase {ECO:0000250|UniProtKB:Q93QC6};
DE AltName: Full=Cysteine-S-conjugate beta-lyase;
GN OrderedLocusNames=TTHA1620 {ECO:0000312|EMBL:BAD71443.1};
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, IDENTIFICATION BY MASS
RP SPECTROMETRY, AND INTERACTION WITH GCBP.
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RX PubMed=15893507; DOI=10.1016/j.bbapap.2005.04.005;
RA Arai R., Nishimoto M., Toyama M., Terada T., Kuramitsu S., Shirouzu M.,
RA Yokoyama S.;
RT "Conserved protein TTHA1554 from Thermus thermophilus HB8 binds to
RT glutamine synthetase and cystathionine beta-lyase.";
RL Biochim. Biophys. Acta 1750:40-47(2005).
CC -!- FUNCTION: Catalyzes the transformation of cystathionine to
CC homocysteine. Can also use cystine or S-methylcysteine as substrate.
CC {ECO:0000269|PubMed:15893507}.
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 Evidence={ECO:0000269|PubMed:15893507};
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 Evidence={ECO:0000269|PubMed:15893507};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250|UniProtKB:P23256};
CC -!- ACTIVITY REGULATION: Activity increases by approximately two-fold in
CC the presence of GCBP. {ECO:0000269|PubMed:15893507}.
CC -!- SUBUNIT: Interacts with GCBP (TTHA1554). {ECO:0000269|PubMed:15893507}.
CC -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC aminotransferase family. MalY/PatB cystathionine beta-lyase subfamily.
CC {ECO:0000305}.
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DR EMBL; AP008226; BAD71443.1; -; Genomic_DNA.
DR RefSeq; WP_011228809.1; NC_006461.1.
DR RefSeq; YP_144886.1; NC_006461.1.
DR AlphaFoldDB; Q5SHW0; -.
DR SMR; Q5SHW0; -.
DR STRING; 300852.55773002; -.
DR EnsemblBacteria; BAD71443; BAD71443; BAD71443.
DR GeneID; 3168874; -.
DR KEGG; ttj:TTHA1620; -.
DR PATRIC; fig|300852.9.peg.1590; -.
DR eggNOG; COG1168; Bacteria.
DR HOGENOM; CLU_017584_15_0_0; -.
DR OMA; NEVCDVN; -.
DR PhylomeDB; Q5SHW0; -.
DR Proteomes; UP000000532; 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:0008652; P:cellular amino acid 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 1: Evidence at protein level;
KW Amino-acid biosynthesis; Lyase; Pyridoxal phosphate; Reference proteome.
FT CHAIN 1..354
FT /note="Cystathionine beta-lyase"
FT /id="PRO_0000442989"
FT MOD_RES 212
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P23256"
SQ SEQUENCE 354 AA; 39078 MW; BB1E52833A985684 CRC64;
MDLPPRTGSL KWGTYPEDVL PLWVADMDFP PAEAIQQALA ERARGFLGYP PREGDRELRE
LILEALGLEA ELAFMPGVVV GLYAAVAAFT APGQGVLTQV PIYPPFLAAI RDQRRTVLAN
PLRETPEGYR LDLAGLERLA FATRLLLFCH PHNPTGRVFG EEELAALAQI ARRHDLIVVS
DELHAPLTYE KPHVPLARFL PERTLTLVGP GKTYNLAGLP IGAVLGPKPL VEAVKRHLPH
VFPNVLAMAA WKAALKEGGP WLKATLEQLR ANRDRVAAWA KARGLGHHPP EGTYLAWIQT
PFPKAAAYFL ERARVALNPG ESFGRGYDTY VRLNFATYPE VLEEALRRLD GALK
