P0A731 (MGSA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Methylglyoxal synthase
Short name=MGS
EC=4.2.3.3

Gene names

Name:	mgsA
Synonyms:	yccG
Ordered Locus Names:	b0963, JW5129

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	152 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	Glycerone phosphate = methylglyoxal + phosphate. HAMAP-Rule MF_00549
Subunit structure	Homohexamer.
Subcellular location	Cytoplasm HAMAP-Rule MF_00549.
Sequence similarities	Belongs to the methylglyoxal synthase family.

Ontologies

Keywords
Cellular component	Cytoplasm
Molecular function	Lyase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	methylglyoxal biosynthetic process Inferred from mutant phenotype PubMed 15489434. Source: EcoCyc
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	methylglyoxal synthase activity Inferred from direct assay PubMed 4563643. Source: EcoCyc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 152

152

Methylglyoxal synthase HAMAP-Rule MF_00549

PRO_0000178625

Sites

Active site

71

1

Experimental info

Sequence conflict

1 – 2

2

ME → WK in J04726. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

152

Helix Strand Turn

Details...

Beta strand

3 – 8

6

Beta strand

13 – 18

6

Helix

20 – 22

3

Helix

23 – 32

10

Helix

34 – 37

4

Beta strand

40 – 45

6

Helix

48 – 56

9

Beta strand

61 – 63

3

Helix

66 – 68

3

Helix

70 – 79

10

Beta strand

85 – 89

5

Helix

99 – 111

13

Beta strand

116 – 119

4

Helix

120 – 127

8

Helix

130 – 133

4

Beta strand

136 – 141

6

Helix

143 – 147

5

Sequences

	Sequence		Length	Mass (Da)
	P0A731 [UniParc]. Last modified June 7, 2005. Version 1. Checksum: 85157193BD4CE72D	FASTA	152	16,919
	10 20 30 40 50 60 MELTTRTLPA RKHIALVAHD HCKQMLMSWV ERHQPLLEQH VLYATGTTGN LISRATGMNV 70 80 90 100 110 120 NAMLSGPMGG DQQVGALISE GKIDVLIFFW DPLNAVPHDP DVKALLRLAT VWNIPVATNV 130 140 150 ATADFIIQSP HFNDAVDILI PDYQRYLADR LK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The molecular cloning of the gene encoding the Escherichia coli 75-kDa helicase and the determination of its nucleotide sequence and gentic map position." Wood E.R., Matson S.W. J. Biol. Chem. 264:8297-8303(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"From famine to feast: the role of methylglyoxal production in Escherichia coli." Totemeyer S., Booth N.A., Nichols W.W., Dunbar B., Booth I.R. Mol. Microbiol. 27:553-562(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, FUNCTION.
[3]	"A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map." Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K. , Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M., Horiuchi T. DNA Res. 3:137-155(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]	"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.
[5]	"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.
[6]	"Intrinsic and extrinsic approaches for detecting genes in a bacterial genome." Borodovsky M., Rudd K.E., Koonin E.V. Nucleic Acids Res. 22:4756-4767(1994) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION.
[7]	"Identification of catalytic bases in the active site of Escherichia coli methylglyoxal synthase: cloning, expression, and functional characterization of conserved aspartic acid residues." Saadat D., Harrison D.H.T. Biochemistry 37:10074-10086(1998) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF ASPARTIC ACID RESIDUES.
[8]	"The crystal structure of methylglyoxal synthase from Escherichia coli." Saadat D., Harrison D.H.T. Structure 7:309-317(1999) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
[9]	"Mirroring perfection: the structure of methylglyoxal synthase complexed with the competitive inhibitor 2-phosphoglycolate." Saadat D., Harrison D.H.T. Biochemistry 39:2950-2960(2000) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

J04726 Genomic DNA. No translation available.
Y11249 Genomic DNA. Translation: CAA72119.1.
U00096 Genomic DNA. Translation: AAC74049.2.
AP009048 Genomic DNA. Translation: BAA35728.2.

PIR

B64837.

RefSeq

NP_415483.2. NC_000913.2.
YP_489235.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1B93	X-ray	1.90	A/B/C	1-152	[»]
1EGH	X-ray	2.00	A/B/C/D/E/F	1-152	[»]
1IK4	X-ray	2.00	A/B/C/D/E/F	1-152	[»]
1S89	X-ray	2.22	A/B/C/D/E/F	1-152	[»]
1S8A	X-ray	2.20	A/B/C/D/E/F	1-152	[»]

ProteinModelPortal

P0A731.

SMR

P0A731. Positions 1-151.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-48252N.

STRING

511145.b0963.

Proteomic databases

PaxDb

P0A731.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC74049; AAC74049; b0963.
BAA35728; BAA35728; BAA35728.

GeneID

12931944.
945574.

KEGG

ecj:Y75_p0935.
eco:b0963.

PATRIC

32117145. VBIEscCol129921_0997.

Organism-specific databases

EchoBASE

EB2213.

EcoGene

EG12307. mgsA.

Phylogenomic databases

eggNOG

COG1803.

HOGENOM

HOG000283729.

KO

K01734.

OMA

EPQPHDP.

ProtClustDB

PRK05234.

Enzyme and pathway databases

BioCyc

EcoCyc:METHGLYSYN-MONOMER.
ECOL316407:JW5129-MONOMER.
MetaCyc:METHGLYSYN-MONOMER.

BRENDA

4.2.3.3. 2026.

SABIO-RK

P0A731.

Gene expression databases

Genevestigator

P0A731.

Family and domain databases

Gene3D

3.40.50.1380. 1 hit.

HAMAP

MF_00549. Methylglyoxal_synth.

InterPro

IPR004363. Methylgl_synth.
IPR018148. Methylglyoxal_synth_AS.
IPR011607. MGS-like_dom.
[Graphical view]

Pfam

PF02142. MGS. 1 hit.
[Graphical view]

PIRSF

PIRSF006614. Methylglyox_syn. 1 hit.

SMART

SM00851. MGS. 1 hit.
[Graphical view]

SUPFAM

SSF52335. MGS-like_dom. 1 hit.

TIGRFAMs

TIGR00160. MGSA. 1 hit.

PROSITE

PS01335. METHYLGLYOXAL_SYNTH. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P0A731.

Entry information

Entry name

MGSA_ECOLI

Accession

Primary (citable) accession number: P0A731
Secondary accession number(s): P37066 , P75872, Q8XD91, Q9R7Q3

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 7, 2005
Last sequence update:	June 7, 2005
Last modified:	May 1, 2013
This is version 71 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program