METC_STAHJ
ID METC_STAHJ Reviewed; 391 AA.
AC Q4L332;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 25-MAY-2022, entry version 109.
DE RecName: Full=Cystathionine beta-lyase MetC {ECO:0000303|PubMed:19035565};
DE Short=CBL {ECO:0000303|PubMed:19035565};
DE EC=4.4.1.13 {ECO:0000269|PubMed:19035565};
DE AltName: Full=Beta-cystathionase {ECO:0000303|PubMed:19035565};
DE AltName: Full=Cysteine lyase {ECO:0000303|PubMed:19035565};
DE AltName: Full=Cysteine-S-conjugate beta-lyase;
GN Name=metC {ECO:0000303|PubMed:19035565};
GN OrderedLocusNames=SH2636 {ECO:0000312|EMBL:BAE05945.1};
OS Staphylococcus haemolyticus (strain JCSC1435).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=279808;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCSC1435;
RX PubMed=16237012; DOI=10.1128/jb.187.21.7292-7308.2005;
RA Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y.,
RA Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C.,
RA Hiramatsu K.;
RT "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the
RT extreme plasticity of its genome and the evolution of human-colonizing
RT staphylococcal species.";
RL J. Bacteriol. 187:7292-7308(2005).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, AND SUBUNIT.
RC STRAIN=AX3;
RX PubMed=19035565; DOI=10.1002/cbdv.200890202;
RA Troccaz M., Benattia F., Borchard G., Clark A.J.;
RT "Properties of recombinant Staphylococcus haemolyticus cystathionine beta-
RT lyase (metC) and its potential role in the generation of volatile thiols in
RT axillary malodor.";
RL Chem. Biodivers. 5:2372-2385(2008).
CC -!- FUNCTION: Catalyzes the transformation of cystathionine into
CC homocysteine (PubMed:19035565). Can also catalyze, at low levels, the
CC conversion of cystathionine into methionine and the conversion of
CC methionine into methanethiol (PubMed:19035565).
CC {ECO:0000269|PubMed:19035565}.
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:19035565};
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:19035565};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:19035565};
CC -!- ACTIVITY REGULATION: Cystathionine beta-lyase activity is inhibited by
CC sweat components such as glycine, serine and ammonium sulfate.
CC Inhibited by cystathionine at a concentration higher than 6 mM.
CC {ECO:0000269|PubMed:19035565}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.2 mM for L-cystathionine {ECO:0000269|PubMed:19035565};
CC Vmax=32 umol/min/mg enzyme with L-cystathionine as substrate
CC {ECO:0000269|PubMed:19035565};
CC Vmax=3.6 umol/min/mg enzyme with methionine as substrate;
CC pH dependence:
CC Optimum pH is 8.5. {ECO:0000269|PubMed:19035565};
CC Temperature dependence:
CC Optimum temperature is 37 degrees Celsius.
CC {ECO:0000269|PubMed:19035565};
CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo
CC pathway; L-homocysteine from L-cystathionine: step 1/1.
CC {ECO:0000305|PubMed:19035565}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000305|PubMed:19035565}.
CC -!- SIMILARITY: Belongs to the trans-sulfuration enzymes family.
CC {ECO:0000305}.
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DR EMBL; AP006716; BAE05945.1; -; Genomic_DNA.
DR RefSeq; WP_011276875.1; NC_007168.1.
DR AlphaFoldDB; Q4L332; -.
DR SMR; Q4L332; -.
DR STRING; 279808.SH2636; -.
DR EnsemblBacteria; BAE05945; BAE05945; SH2636.
DR KEGG; sha:SH2636; -.
DR eggNOG; COG0626; Bacteria.
DR HOGENOM; CLU_018986_2_0_9; -.
DR OMA; THGGIIV; -.
DR OrthoDB; 637281at2; -.
DR UniPathway; UPA00051; UER00078.
DR Proteomes; UP000000543; 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:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0019346; P:transsulfuration; IEA:InterPro.
DR CDD; cd00614; CGS_like; 1.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR000277; Cys/Met-Metab_PyrdxlP-dep_enz.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR11808; PTHR11808; 1.
DR Pfam; PF01053; Cys_Met_Meta_PP; 1.
DR PIRSF; PIRSF001434; CGS; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR PROSITE; PS00868; CYS_MET_METAB_PP; 1.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; Lyase; Methionine biosynthesis;
KW Pyridoxal phosphate.
FT CHAIN 1..391
FT /note="Cystathionine beta-lyase MetC"
FT /id="PRO_0000445392"
FT MOD_RES 196
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P06721"
SQ SEQUENCE 391 AA; 42697 MW; 90E1D48A7257B73E CRC64;
MSLSKETEVI FDEHRGVDYD SANPPLYDSS TFHQKVLGGN AKFDYARSGN PNRQLLEEKL
AKLEGGQYAF AYASGIAAIS AVLLTLKAND HVILPDDVYG GTFRLTEQIL NRFDIQFTTV
NATQPKEIER AIQPNTKLIY VETPSNPCFK ITDIRAVAAI AKRHHLLLAV DNTFMTPLGQ
SPLALGADIV VHSATKFLGG HSDIIAGAAI TNRKDVADAL YLLQNGTGTA LSAHDSWTLA
KHLKTLPVRF KQSTSNAEKL VAFLKEREEI AEVYYPGNSS LHLSQANSGG AVIGFRLKDE
TKTQDFVDAL TLPLVSVSLG GVETILSHPA TMSHAAVPED VRNERGITFG LFRLSVGLEQ
PQELIADLNY ALKEAFNESI IESITEQRFS S
