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Protein

Cystathionine gamma-synthase

Gene

metB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

O(4)-succinyl-L-homoserine + L-cysteine = L-cystathionine + succinate.1 Publication

Cofactori

pyridoxal 5'-phosphate1 PublicationNote: Binds 1 pyridoxal phosphate per subunit.1 Publication

Kineticsi

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

  1. KM=0.33 mM for O-succinyl-L-homoserine (at pH 8.2 and 25 degrees Celsius, when assaying the gamma-elimination reaction)1 Publication
  2. KM=1.0 mM for O-succinyl-L-homoserine (at pH 8.2 and 25 degrees Celsius, when assaying the gamma-replacement reaction)1 Publication
  3. KM=0.05 mM for L-cysteine (at pH 8.2 and 25 degrees Celsius, when assaying the gamma-replacement reaction)1 Publication

pH dependencei

Optimum pH is 7.8 for the gamma-replacement reaction.1 Publication

Pathwayi

GO - Molecular functioni

  1. cystathionine gamma-synthase activity Source: EcoCyc
  2. pyridoxal phosphate binding Source: EcoCyc

GO - Biological processi

  1. methionine biosynthetic process Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Amino-acid biosynthesis, Methionine biosynthesis

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciEcoCyc:O-SUCCHOMOSERLYASE-MONOMER.
ECOL316407:JW3910-MONOMER.
MetaCyc:O-SUCCHOMOSERLYASE-MONOMER.
BRENDAi2.5.1.48. 2026.
SABIO-RKP00935.
UniPathwayiUPA00051; UER00077.

Names & Taxonomyi

Protein namesi
Recommended name:
Cystathionine gamma-synthase (EC:2.5.1.48)
Short name:
CGS
Alternative name(s):
O-succinylhomoserine (thiol)-lyase
Gene namesi
Name:metB
Ordered Locus Names:b3939, JW3910
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10582. metB.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 386386Cystathionine gamma-synthasePRO_0000114756Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei198 – 1981N6-(pyridoxal phosphate)lysine1 Publication

Proteomic databases

PaxDbiP00935.
PRIDEiP00935.

Expressioni

Gene expression databases

GenevestigatoriP00935.

Interactioni

Subunit structurei

Homotetramer.2 Publications

Protein-protein interaction databases

DIPiDIP-10192N.
IntActiP00935. 1 interaction.
STRINGi511145.b3939.

Structurei

Secondary structure

1
386
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 117Combined sources
Turni12 – 154Combined sources
Turni18 – 203Combined sources
Beta strandi22 – 243Combined sources
Beta strandi31 – 333Combined sources
Turni47 – 493Combined sources
Helixi52 – 6514Combined sources
Beta strandi68 – 758Combined sources
Helixi76 – 8712Combined sources
Beta strandi93 – 975Combined sources
Helixi102 – 11211Combined sources
Turni113 – 1153Combined sources
Beta strandi118 – 1225Combined sources
Helixi127 – 1359Combined sources
Beta strandi139 – 1446Combined sources
Turni148 – 1503Combined sources
Helixi156 – 16510Combined sources
Beta strandi169 – 1735Combined sources
Turni175 – 1773Combined sources
Turni179 – 1813Combined sources
Helixi184 – 1874Combined sources
Beta strandi190 – 1956Combined sources
Turni196 – 2016Combined sources
Beta strandi209 – 2157Combined sources
Helixi216 – 22813Combined sources
Helixi235 – 24511Combined sources
Helixi248 – 26619Combined sources
Beta strandi272 – 2765Combined sources
Helixi286 – 2927Combined sources
Beta strandi298 – 3069Combined sources
Helixi308 – 3169Combined sources
Beta strandi319 – 3257Combined sources
Beta strandi329 – 3313Combined sources
Beta strandi333 – 3364Combined sources
Helixi337 – 3393Combined sources
Turni340 – 3445Combined sources
Helixi347 – 3526Combined sources
Beta strandi359 – 3635Combined sources
Helixi369 – 38315Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CS1X-ray1.50A/B/C/D1-386[»]
ProteinModelPortaliP00935.
SMRiP00935. Positions 3-386.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00935.

Family & Domainsi

Sequence similaritiesi

Belongs to the trans-sulfuration enzymes family.Curated

Phylogenomic databases

eggNOGiCOG0626.
HOGENOMiHOG000246415.
InParanoidiP00935.
KOiK01739.
OMAiMQTKLIH.
OrthoDBiEOG67DPN3.
PhylomeDBiP00935.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProiIPR000277. 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]
PANTHERiPTHR11808. PTHR11808. 1 hit.
PfamiPF01053. Cys_Met_Meta_PP. 1 hit.
[Graphical view]
PIRSFiPIRSF001434. CGS. 1 hit.
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR02080. O_succ_thio_ly. 1 hit.
PROSITEiPS00868. CYS_MET_METAB_PP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P00935-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTRKQATIAV RSGLNDDEQY GCVVPPIHLS STYNFTGFNE PRAHDYSRRG
60 70 80 90 100
NPTRDVVQRA LAELEGGAGA VLTNTGMSAI HLVTTVFLKP GDLLVAPHDC
110 120 130 140 150
YGGSYRLFDS LAKRGCYRVL FVDQGDEQAL RAALAEKPKL VLVESPSNPL
160 170 180 190 200
LRVVDIAKIC HLAREVGAVS VVDNTFLSPA LQNPLALGAD LVLHSCTKYL
210 220 230 240 250
NGHSDVVAGV VIAKDPDVVT ELAWWANNIG VTGGAFDSYL LLRGLRTLVP
260 270 280 290 300
RMELAQRNAQ AIVKYLQTQP LVKKLYHPSL PENQGHEIAA RQQKGFGAML
310 320 330 340 350
SFELDGDEQT LRRFLGGLSL FTLAESLGGV ESLISHAATM THAGMAPEAR
360 370 380
AAAGISETLL RISTGIEDGE DLIADLENGF RAANKG
Length:386
Mass (Da):41,550
Last modified:July 21, 1986 - v1
Checksum:i423B825219A42E9E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K01546 Genomic DNA. Translation: AAA24167.1.
L19201 Genomic DNA. Translation: AAB03071.1.
U00096 Genomic DNA. Translation: AAC76921.1.
AP009048 Genomic DNA. Translation: BAE77371.1.
PIRiA01158. SYECCG.
RefSeqiNP_418374.1. NC_000913.3.
YP_491512.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC76921; AAC76921; b3939.
BAE77371; BAE77371; BAE77371.
GeneIDi12932108.
948434.
KEGGiecj:Y75_p3248.
eco:b3939.
PATRICi32123397. VBIEscCol129921_4059.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K01546 Genomic DNA. Translation: AAA24167.1.
L19201 Genomic DNA. Translation: AAB03071.1.
U00096 Genomic DNA. Translation: AAC76921.1.
AP009048 Genomic DNA. Translation: BAE77371.1.
PIRiA01158. SYECCG.
RefSeqiNP_418374.1. NC_000913.3.
YP_491512.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CS1X-ray1.50A/B/C/D1-386[»]
ProteinModelPortaliP00935.
SMRiP00935. Positions 3-386.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-10192N.
IntActiP00935. 1 interaction.
STRINGi511145.b3939.

Proteomic databases

PaxDbiP00935.
PRIDEiP00935.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76921; AAC76921; b3939.
BAE77371; BAE77371; BAE77371.
GeneIDi12932108.
948434.
KEGGiecj:Y75_p3248.
eco:b3939.
PATRICi32123397. VBIEscCol129921_4059.

Organism-specific databases

EchoBASEiEB0577.
EcoGeneiEG10582. metB.

Phylogenomic databases

eggNOGiCOG0626.
HOGENOMiHOG000246415.
InParanoidiP00935.
KOiK01739.
OMAiMQTKLIH.
OrthoDBiEOG67DPN3.
PhylomeDBiP00935.

Enzyme and pathway databases

UniPathwayiUPA00051; UER00077.
BioCyciEcoCyc:O-SUCCHOMOSERLYASE-MONOMER.
ECOL316407:JW3910-MONOMER.
MetaCyc:O-SUCCHOMOSERLYASE-MONOMER.
BRENDAi2.5.1.48. 2026.
SABIO-RKP00935.

Miscellaneous databases

EvolutionaryTraceiP00935.
PROiP00935.

Gene expression databases

GenevestigatoriP00935.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProiIPR000277. 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]
PANTHERiPTHR11808. PTHR11808. 1 hit.
PfamiPF01053. Cys_Met_Meta_PP. 1 hit.
[Graphical view]
PIRSFiPIRSF001434. CGS. 1 hit.
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR02080. O_succ_thio_ly. 1 hit.
PROSITEiPS00868. CYS_MET_METAB_PP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1982) [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(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. 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(2005) [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(1986) [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(1989) [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(1996) [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(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS), SUBUNIT, PYRIDOXAL PHOSPHATE AT LYS-198.

Entry informationi

Entry nameiMETB_ECOLI
AccessioniPrimary (citable) accession number: P00935
Secondary accession number(s): Q2M8N5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: April 1, 2015
This is version 144 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.