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P00935 (METB_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 138. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cystathionine gamma-synthase

Short name=CGS
EC=2.5.1.48
Alternative name(s):
O-succinylhomoserine (thiol)-lyase
Gene names
Name:metB
Ordered Locus Names:b3939, JW3910
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length386 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the formation of L-cystathionine from O-succinyl-L-homoserine (OSHS) and L-cysteine, via a gamma-replacement reaction. In the absence of thiol, catalyzes gamma-elimination to form 2-oxobutanoate, succinate and ammonia. Ref.6

Catalytic activity

O(4)-succinyl-L-homoserine + L-cysteine = L-cystathionine + succinate. Ref.6

Cofactor

Binds 1 pyridoxal phosphate per subunit. Ref.6

Pathway

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

Subunit structure

Homotetramer. Ref.6 Ref.8

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the trans-sulfuration enzymes family.

Biophysicochemical properties

Kinetic parameters:

kcat are 700 min(-1) and 460 min (-1) for the gamma-replacement and gamma-elimination reaction, respectively.

KM=0.33 mM for O-succinyl-L-homoserine (at pH 8.2 and 25 degrees Celsius, when assaying the gamma-elimination reaction) Ref.6

KM=1.0 mM for O-succinyl-L-homoserine (at pH 8.2 and 25 degrees Celsius, when assaying the gamma-replacement reaction)

KM=0.05 mM for L-cysteine (at pH 8.2 and 25 degrees Celsius, when assaying the gamma-replacement reaction)

pH dependence:

Optimum pH is 7.8 for the gamma-replacement reaction.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 386386Cystathionine gamma-synthase
PRO_0000114756

Amino acid modifications

Modified residue1981N6-(pyridoxal phosphate)lysine Ref.5

Secondary structure

........................................................................ 386
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00935 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 423B825219A42E9E

FASTA38641,550
        10         20         30         40         50         60 
MTRKQATIAV RSGLNDDEQY GCVVPPIHLS STYNFTGFNE PRAHDYSRRG NPTRDVVQRA 

        70         80         90        100        110        120 
LAELEGGAGA VLTNTGMSAI HLVTTVFLKP GDLLVAPHDC YGGSYRLFDS LAKRGCYRVL 

       130        140        150        160        170        180 
FVDQGDEQAL RAALAEKPKL VLVESPSNPL LRVVDIAKIC HLAREVGAVS VVDNTFLSPA 

       190        200        210        220        230        240 
LQNPLALGAD LVLHSCTKYL NGHSDVVAGV VIAKDPDVVT ELAWWANNIG VTGGAFDSYL 

       250        260        270        280        290        300 
LLRGLRTLVP RMELAQRNAQ AIVKYLQTQP LVKKLYHPSL PENQGHEIAA RQQKGFGAML 

       310        320        330        340        350        360 
SFELDGDEQT LRRFLGGLSL FTLAESLGGV ESLISHAATM THAGMAPEAR AAAGISETLL 

       370        380 
RISTGIEDGE DLIADLENGF RAANKG 

« Hide

References

« Hide 'large scale' references
[1]"Structure of the metJBLF cluster in Escherichia coli K12. Sequence of the metB structural gene and of the 5'- and 3'-flanking regions of the metBL operon."
Duchange N., Zakin M.M., Ferrara P., Saint-Girons I., Park I., Tran S.V., Py M.-C., Cohen G.N.
J. Biol. Chem. 258:14868-14871(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12.
[2]"Analysis of the Escherichia coli genome. III. DNA sequence of the region from 87.2 to 89.2 minutes."
Plunkett G. III, Burland V., Daniels D.L., Blattner F.R.
Nucleic Acids Res. 21:3391-3398(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[3]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"Pyridoxal 5'phosphate binding site of Escherichia coli beta cystathionase and cystathionine gamma synthase comparison of their sequences."
Martel A., Bouthier de la Tour C., Le Goffic F.
Biochem. Biophys. Res. Commun. 147:565-571(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 182-209.
[6]"Purification and properties of cystathionine gamma-synthase from overproducing strains of Escherichia coli."
Holbrook E.L., Greene R.C., Krueger J.H.
Biochemistry 29:435-442(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
[7]"Escherichia coli proteome analysis using the gene-protein database."
VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY 2D-GEL.
[8]"Crystal structure of Escherichia coli cystathionine gamma-synthase at 1.5-A resolution."
Clausen T., Huber R., Prade L., Wahl M.C., Messerschmidt A.
EMBO J. 17:6827-6838(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS), SUBUNIT, PYRIDOXAL PHOSPHATE AT LYS-198.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
K01546 Genomic DNA. Translation: AAA24167.1.
L19201 Genomic DNA. Translation: AAB03071.1.
U00096 Genomic DNA. Translation: AAC76921.1.
AP009048 Genomic DNA. Translation: BAE77371.1.
PIRSYECCG. A01158.
RefSeqNP_418374.1. NC_000913.3.
YP_491512.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1CS1X-ray1.50A/B/C/D1-386[»]
ProteinModelPortalP00935.
SMRP00935. Positions 3-386.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-10192N.
IntActP00935. 1 interaction.
STRING511145.b3939.

Proteomic databases

PaxDbP00935.
PRIDEP00935.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC76921; AAC76921; b3939.
BAE77371; BAE77371; BAE77371.
GeneID12932108.
948434.
KEGGecj:Y75_p3248.
eco:b3939.
PATRIC32123397. VBIEscCol129921_4059.

Organism-specific databases

EchoBASEEB0577.
EcoGeneEG10582. metB.

Phylogenomic databases

eggNOGCOG0626.
HOGENOMHOG000246415.
KOK01739.
OMAMQTKLIH.
OrthoDBEOG67DPN3.
PhylomeDBP00935.
ProtClustDBPRK08045.

Enzyme and pathway databases

BioCycEcoCyc:O-SUCCHOMOSERLYASE-MONOMER.
ECOL316407:JW3910-MONOMER.
MetaCyc:O-SUCCHOMOSERLYASE-MONOMER.
SABIO-RKP00935.
UniPathwayUPA00051; UER00077.

Gene expression databases

GenevestigatorP00935.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProIPR000277. Cys/Met-Metab_PyrdxlP-dep_enz.
IPR011821. O_succ_thio_ly.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PANTHERPTHR11808. PTHR11808. 1 hit.
PfamPF01053. Cys_Met_Meta_PP. 1 hit.
[Graphical view]
PIRSFPIRSF001434. CGS. 1 hit.
SUPFAMSSF53383. SSF53383. 1 hit.
TIGRFAMsTIGR02080. O_succ_thio_ly. 1 hit.
PROSITEPS00868. CYS_MET_METAB_PP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP00935.
PROP00935.

Entry information

Entry nameMETB_ECOLI
AccessionPrimary (citable) accession number: P00935
Secondary accession number(s): Q2M8N5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: April 16, 2014
This is version 138 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene