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Reviewed, UniProtKB/Swiss-Prot O31632 (METC_BACSU)

Last modified November 3, 2009. Version 44. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Cystathionine beta-lyase metC
      Short name=CBL
    EC=4.4.1.8
Alternative name(s):
    Beta-cystathionase
    Cysteine lyase
Gene names
Name: metC
Synonyms: yjcJ
Ordered Locus Names: BSU11880
OrganismBacillus subtilis [Complete proteome] [HAMAP]
Taxonomic identifier1423 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

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Protein attributes

Sequence length390 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Catalyzes the transformation of cystathionine into homocysteine. Also exhibits cysteine desulfhydrase activity in vitro, producing sulfide from cysteine. Ref.2 Ref.3

Catalytic activity

L-cystathionine + H2O = L-homocysteine + NH3 + pyruvate. Ref.2

Cofactor

Pyridoxal phosphate By similarity.

Pathway

Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homocysteine from L-cystathionine: step 1/1.

Subunit structure

Homotetramer By similarity.

Subcellular location

Cytoplasm.

Induction

Repressed by methionine. Ref.2

Disruption phenotype

Grows poorly in the presence of cystathionine as sole sulfur source. Ref.2 Ref.3

Sequence similarities

Belongs to the trans-sulfuration enzymes family.

Biophysicochemical properties

Kinetic parameters:

KM=0.64 mM for cystathionine

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Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Methionine biosynthesis
   Cellular componentCytoplasm
   LigandPyridoxal phosphate
   Molecular functionLyase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processmethionine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functioncystathionine beta-lyase activity

Inferred from electronic annotation. Source: EC

pyridoxal phosphate binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 390390Cystathionine beta-lyase metC
PRO_0000360655

Amino acid modifications

Modified residue2001N6-(pyridoxal phosphate)lysine By similarity

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Sequences

Sequence LengthMass (Da)Tools
O31632-1 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 8E8C058802DFDD7F

FASTA39042,491
        10         20         30         40         50         60 
MSKHNWTLET QLVHNPFKTD GGTGAVSVPI QHASTFHQSS FEEFGAYDYS RSGTPTRTAL 

        70         80         90        100        110        120 
EETIAALEGG TRGFAFSSGM AAISTAFLLL SQGDHVLVTE DVYGGTFRMV TEVLTRFGIE 

       130        140        150        160        170        180 
HTFVDMTDRN EVARSIKPNT KVIYMETPSN PTLGITDIKA VVQLAKENGC LTFLDNTFMT 

       190        200        210        220        230        240 
PALQRPLDLG VDIVLHSATK FLSGHSDVLS GLAAVKDEEL GKQLYKLQNA FGAVLGVQDC 

       250        260        270        280        290        300 
WLVLRGLKTL QVRLEKASQT AQRLAEFFQK HPAVKRVYYP GLADHPGAET HKSQSTGAGA 

       310        320        330        340        350        360 
VLSFELESKE AVKKLVENVS LPVFAVSLGA VESILSYPAT MSHAAMPKEE REKRGITDGL 

       370        380        390 
LRLSVGVEHA DDLEHDFEQA LKEIAPVSVR

« Hide

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References

« Hide 'large scale' references
[1]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed: 9384377] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.
[2]"The metIC operon involved in methionine biosynthesis in Bacillus subtilis is controlled by transcription antitermination."
Auger S., Yuen W.H., Danchin A., Martin-Verstraete I.
Microbiology 148:507-518(2002) [PubMed: 11832514] [Abstract]
Cited for: CATALYTIC ACTIVITY, FUNCTION, DISRUPTION PHENOTYPE, INDUCTION.
Strain: 168.
[3]"The PatB protein of Bacillus subtilis is a C-S-lyase."
Auger S., Gomez M.P., Danchin A., Martin-Verstraete I.
Biochimie 87:231-238(2005) [PubMed: 15760717] [Abstract]
Cited for: BIOPHYSICOCHEMICAL PROPERTIES, FUNCTION, DISRUPTION PHENOTYPE.
Strain: 168.

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Cross-references

Sequence databases

AL009126 Genomic DNA. Translation: CAB13045.1.
PIRB69847.
RefSeqNP_389070.1.

3D structure databases

HSSPHSSP built from PDB template 1IBJ based on UniProtKB P53780.
ModBaseSearch...

Genome annotation databases

GeneID936424.
GenomeReviewsGene locus BSU11880 in contig AL009126_GR.
KEGGbsu:BSU11880.
NMPDRfig|224308.1.peg.1189.

Organism-specific databases

SubtiListBG13163. metC. [Micado]
CMRSearch...

Phylogenomic databases

HOGENOMO31632.
OMALSSTFHQ.

Enzyme and pathway databases

BioCycBSUB224308:BSU1189-MON.

Family and domain databases

InterProIPR000277. Cys/Met-Metab_PyrdxlP-dep_enz.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
Gene3DG3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.
G3DSA:3.90.1150.10. PyrdxlP-dep_Trfase_major_sub2. 1 hit.
PANTHERPTHR11808. Cys_Met_Meta_PP. 1 hit.
PfamPF01053. Cys_Met_Meta_PP. 1 hit.
[Graphical view]
PIRSFPIRSF001434. CGS. 1 hit.
PROSITEPS00868. CYS_MET_METAB_PP. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameMETC_BACSU
AccessionPrimary (citable) accession number: O31632
Entry history
Integrated into UniProtKB/Swiss-Prot: January 20, 2009
Last sequence update: January 1, 1998
Last modified: November 3, 2009
This is version 44 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents