Cystathionine gamma-synthase - Escherichia coli (strain K12)

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Reviewed, UniProtKB/Swiss-Prot P00935 (METB_ECOLI)

Last modified February 9, 2010. Version 107. History...

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

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Names and origin

Protein names

Recommended 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

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

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Protein attributes

Sequence length	386 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Catalytic activity	O(4)-succinyl-L-homoserine + L-cysteine = L-cystathionine + succinate.
Cofactor	Pyridoxal phosphate.
Pathway	Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway.
Subunit structure	Homotetramer. Ref.6
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the trans-sulfuration enzymes family.

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Ontologies

Keywords
Biological process	Amino-acid biosynthesis Methionine biosynthesis
Cellular component	Cytoplasm
Ligand	Pyridoxal phosphate
Molecular function	Transferase
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	methionine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	cystathionine gamma-synthase activity Inferred from electronic annotation. Source: EC protein binding Inferred from physical interaction. Source: IntAct pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct	Notes
nadE	P18843	1	EBI-1134244,EBI-548960

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 386

386

Cystathionine gamma-synthase

PRO_0000114756

Amino acid modifications

Modified residue

198

N6-(pyridoxal phosphate)lysine

Secondary structure

386

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P00935-1 [UniParc].

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

386

41,550

        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

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References

	« Hide 'large scale' referencesShow '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: 6361020] [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: 8346018] [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 277:1453-1474(1997) [PubMed: 9278503] [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: 16738553] [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: 3307782] [Abstract] Cited for: PROTEIN SEQUENCE OF 182-209.
[6]	"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: 9843488] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS), SUBUNIT, PYRIDOXAL PHOSPHATE AT LYS-198.

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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.

PIR

SYECCG. A01158.

RefSeq

AP_003870.1.
NP_418374.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1CS1	X-ray	1.50	A/B/C/D	1-386	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-10192N.

IntAct

P00935. 1 interaction.

STRING

P00935.

2-D gel databases

ECO2DBASE

G040.1. 6TH EDITION.

Genome annotation databases

GeneID

948434.

GenomeReviews

Gene locus JW3910 in contig AP009048_GR.
Gene locus b3939 in contig U00096_GR.

KEGG

ecj:JW3910.
eco:b3939.

Organism-specific databases

EchoBASE

EB0577.

EcoGene

EG10582. metB.

CMR

Search...

Phylogenomic databases

eggNOG

COG0626.

HOGENOM

HBG754729.

OMA

REFDYSR.

Enzyme and pathway databases

BioCyc

EcoCyc:O-SUCCHOMOSERLYASE-MONOMER.
ECOL168927:B3939-MONOMER.
MetaCyc:O-SUCCHOMOSERLYASE-MONOMER.

Gene expression databases

Genevestigator

P00935.

Family and domain databases

InterPro

IPR000277. Cys/Met-Metab_PyrdxlP-dep_enz.
IPR011821. O_succ_thio_ly.
IPR015424. PyrdxlP-dep_Trfase_major_dom.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]

Gene3D

G3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.
G3DSA:3.90.1150.10. PyrdxlP-dep_Trfase_major_sub2. 1 hit.

PANTHER

PTHR11808. Cys_Met_Meta_PP. 1 hit.

Pfam

PF01053. Cys_Met_Meta_PP. 1 hit.
[Graphical view]

PIRSF

PIRSF001434. CGS. 1 hit.

TIGRFAMs

TIGR02080. O_succ_thio_ly. 1 hit.

PROSITE

PS00868. CYS_MET_METAB_PP. 1 hit.
[Graphical view]

ProtoNet

Search...

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Entry information

Entry name

METB_ECOLI

Accession

Primary (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:	February 9, 2010
This is version 107 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

Escherichia coli

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Amino acid modifications

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

2-D gel databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents