P00935 (METB_ECOLI) Reviewed, UniProtKB/Swiss-Prot

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) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	386 AA.
Sequence status	Complete.
Protein existence	Evidence 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

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 Reference proteome
Gene Ontology (GO)
Biological_process	methionine biosynthetic process Inferred from mutant phenotype PubMed 6086586. Source: EcoCyc
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	cystathionine gamma-synthase activity Inferred from direct assay Ref.6. Source: EcoCyc pyridoxal phosphate binding Inferred from direct assay Ref.6. Source: EcoCyc
Complete GO annotation...

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

1

N6-(pyridoxal phosphate)lysine Ref.5

Secondary structure

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386

Helix Strand Turn

Details...

Helix

5 – 11

7

Turn

12 – 15

4

Turn

18 – 20

3

Beta strand

22 – 24

3

Beta strand

31 – 33

3

Turn

47 – 49

3

Helix

52 – 65

14

Beta strand

68 – 75

8

Helix

76 – 87

12

Beta strand

93 – 97

5

Helix

102 – 112

11

Turn

113 – 115

3

Beta strand

118 – 122

5

Helix

127 – 135

9

Beta strand

139 – 144

6

Turn

148 – 150

3

Helix

156 – 165

10

Beta strand

169 – 173

5

Turn

175 – 177

3

Turn

179 – 181

3

Helix

184 – 187

4

Beta strand

190 – 195

6

Turn

196 – 201

6

Beta strand

209 – 215

7

Helix

216 – 228

13

Helix

235 – 245

11

Helix

248 – 266

19

Beta strand

272 – 276

5

Helix

286 – 292

7

Beta strand

298 – 306

9

Helix

308 – 316

9

Beta strand

319 – 325

7

Beta strand

329 – 331

3

Beta strand

333 – 336

4

Helix

337 – 339

3

Turn

340 – 344

5

Helix

347 – 352

6

Beta strand

359 – 363

5

Helix

369 – 383

15

Sequences

	Sequence		Length	Mass (Da)
	P00935 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: 423B825219A42E9E	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

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] [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 277:1453-1474(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.

PIR

SYECCG. A01158.

RefSeq

NP_418374.1. NC_000913.2.
YP_491512.1. NC_007779.1.

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	[»]

ProteinModelPortal

P00935.

SMR

P00935. Positions 3-386.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-10192N.

IntAct

P00935. 1 interaction.

STRING

511145.b3939.

Proteomic databases

PaxDb

P00935.

PRIDE

P00935.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC76921; AAC76921; b3939.
BAE77371; BAE77371; BAE77371.

GeneID

12932108.
948434.

KEGG

ecj:Y75_p3248.
eco:b3939.

PATRIC

32123397. VBIEscCol129921_4059.

Organism-specific databases

EchoBASE

EB0577.

EcoGene

EG10582. metB.

Phylogenomic databases

eggNOG

COG0626.

HOGENOM

HOG000246415.

KO

K01739.

OMA

SPIDCYL.

ProtClustDB

PRK08045.

Enzyme and pathway databases

BioCyc

EcoCyc:O-SUCCHOMOSERLYASE-MONOMER.
ECOL316407:JW3910-MONOMER.
MetaCyc:O-SUCCHOMOSERLYASE-MONOMER.

SABIO-RK

P00935.

UniPathway

UPA00051; UER00077.

Gene expression databases

Genevestigator

P00935.

Family and domain databases

Gene3D

3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.

InterPro

IPR000277. 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]

PANTHER

PTHR11808. PTHR11808. 1 hit.

Pfam

PF01053. Cys_Met_Meta_PP. 1 hit.
[Graphical view]

PIRSF

PIRSF001434. CGS. 1 hit.

SUPFAM

SSF53383. PyrdxlP-dep_Trfase_major. 1 hit.

TIGRFAMs

TIGR02080. O_succ_thio_ly. 1 hit.

PROSITE

PS00868. CYS_MET_METAB_PP. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P00935.

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:	May 1, 2013
This is version 133 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program