METC_COXBU
ID METC_COXBU Reviewed; 387 AA.
AC Q83A83;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Cystathionine beta-lyase;
DE Short=CBL;
DE EC=4.4.1.13 {ECO:0000250|UniProtKB:P06721};
DE AltName: Full=Beta-cystathionase;
DE AltName: Full=Cysteine lyase;
DE AltName: Full=Cysteine-S-conjugate beta-lyase;
GN Name=metC; OrderedLocusNames=CBU_2025;
OS Coxiella burnetii (strain RSA 493 / Nine Mile phase I).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC Coxiella.
OX NCBI_TaxID=227377;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RSA 493 / Nine Mile phase I;
RX PubMed=12704232; DOI=10.1073/pnas.0931379100;
RA Seshadri R., Paulsen I.T., Eisen J.A., Read T.D., Nelson K.E., Nelson W.C.,
RA Ward N.L., Tettelin H., Davidsen T.M., Beanan M.J., DeBoy R.T.,
RA Daugherty S.C., Brinkac L.M., Madupu R., Dodson R.J., Khouri H.M.,
RA Lee K.H., Carty H.A., Scanlan D., Heinzen R.A., Thompson H.A., Samuel J.E.,
RA Fraser C.M., Heidelberg J.F.;
RT "Complete genome sequence of the Q-fever pathogen, Coxiella burnetii.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:5455-5460(2003).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND DEVELOPMENTAL STAGE.
RC STRAIN=Nine Mile Crazy / RSA 514;
RX PubMed=17088354; DOI=10.1128/iai.00883-06;
RA Coleman S.A., Fischer E.R., Cockrell D.C., Voth D.E., Howe D., Mead D.J.,
RA Samuel J.E., Heinzen R.A.;
RT "Proteome and antigen profiling of Coxiella burnetii developmental forms.";
RL Infect. Immun. 75:290-298(2007).
CC -!- FUNCTION: Catalyzes the cleavage of cystathionine to homocysteine,
CC pyruvate and ammonia during methionine biosynthesis.
CC {ECO:0000250|UniProtKB:P06721}.
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:0000250|UniProtKB:P06721};
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:0000250|UniProtKB:P06721};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250|UniProtKB:P06721};
CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo
CC pathway; L-homocysteine from L-cystathionine: step 1/1.
CC {ECO:0000250|UniProtKB:P06721}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P06721}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P06721}.
CC -!- DEVELOPMENTAL STAGE: More than twofold more abundant in the small cell
CC variant (SCV) stage than in the large cell variant (LCV) stage (at
CC protein level). LCVs are more metabolically active than SCVs.
CC {ECO:0000269|PubMed:17088354}.
CC -!- SIMILARITY: Belongs to the trans-sulfuration enzymes family.
CC {ECO:0000305}.
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DR EMBL; AE016828; AAO91512.1; -; Genomic_DNA.
DR RefSeq; NP_820998.1; NC_002971.3.
DR RefSeq; WP_010958610.1; NZ_CCYB01000066.1.
DR AlphaFoldDB; Q83A83; -.
DR SMR; Q83A83; -.
DR STRING; 227377.CBU_2025; -.
DR PRIDE; Q83A83; -.
DR EnsemblBacteria; AAO91512; AAO91512; CBU_2025.
DR GeneID; 1209938; -.
DR KEGG; cbu:CBU_2025; -.
DR PATRIC; fig|227377.7.peg.2017; -.
DR eggNOG; COG0626; Bacteria.
DR HOGENOM; CLU_018986_2_0_6; -.
DR OMA; MQTKLIH; -.
DR UniPathway; UPA00051; UER00078.
DR Proteomes; UP000002671; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016846; F:carbon-sulfur lyase activity; IBA:GO_Central.
DR GO; GO:0004121; F:cystathionine beta-lyase activity; IEA:RHEA.
DR GO; GO:0004123; F:cystathionine gamma-lyase activity; IBA:GO_Central.
DR GO; GO:0003962; F:cystathionine gamma-synthase activity; IBA:GO_Central.
DR GO; GO:0047804; F:cysteine-S-conjugate beta-lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR GO; GO:0019343; P:cysteine biosynthetic process via cystathionine; IBA:GO_Central.
DR GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0019346; P:transsulfuration; IBA:GO_Central.
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; Cytoplasm; Lyase; Methionine biosynthesis;
KW Pyridoxal phosphate; Reference proteome.
FT CHAIN 1..387
FT /note="Cystathionine beta-lyase"
FT /id="PRO_0000320579"
FT MOD_RES 204
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P06721"
SQ SEQUENCE 387 AA; 42776 MW; 6DF7959AA345B6AB CRC64;
MTANNNKKSH IDTRVIHAGQ KPDPLTGAVM TPIYTASTYA QKSPGVHQGY EYSRSQNPTR
FAYERCVADL ESGQHGFAFA SGMAATATIL ELLQPGDHVV VMDDVYGGSY RLFENVRKRS
AGLSFSFVDF TDENKVREAV TAKTKMLWVE SPSNPRLKIV DLAKIAEIAK EKNIIAVADN
TFATPIIQRP LELGFDIVTH SATKYLNGHS DIIGGVAVVG DNKTLAEQLK YLQNAIGAIA
APFDSFMVLR GLKTLAIRME RHCENAMQLA QWLEKHPKVK RVYYPGLPSH PQHSIAKKQM
RYFGGMISVE LKCDLNETKK VLERCQLFTL AESLGGVESL IEHPAIMTHA SIPQAERQKL
GITDGFIRLS VGIEAITDLR HDLEAAL
