Malate synthase G - Escherichia coli (strain K12)

Names and originHide

Protein names

Recommended name:
Malate synthase G
Short name=MSG
EC=2.3.3.9

Gene names

Name:	glcB
Synonyms:	glc
Ordered Locus Names:	b2976, JW2943

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 attributesHide

Sequence length	723 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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General annotation (Comments)Hide

Function	Accounts for almost the entire malate-synthesizing activity in cells metabolizing glyoxylate. HAMAP MF_00641
Catalytic activity	Acetyl-CoA + H₂O + glyoxylate = (S)-malate + CoA. HAMAP MF_00641
Cofactor	Magnesium. HAMAP MF_00641
Pathway	Carbohydrate metabolism; glyoxylate cycle; (S)-malate from isocitrate: step 2/2. HAMAP MF_00641
Subunit structure	Monomer. HAMAP MF_00641
Subcellular location	Cytoplasm HAMAP MF_00641.
Sequence similarities	Belongs to the malate synthase family. GlcB subfamily.

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OntologiesHide

Keywords
Biological process	Glyoxylate bypass Tricarboxylic acid cycle
Cellular component	Cytoplasm
Ligand	Magnesium
Molecular function	Transferase
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	glyoxylate catabolic process Inferred from expression pattern. Source: UniProtKB glyoxylate cycle Inferred from electronic annotation. Source: HAMAP tricarboxylic acid cycle Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	malate synthase activity Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

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Sequence annotation (Features)Hide

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

Removed Ref.1

Chain

2 – 723

722

Malate synthase G HAMAP MF_00641

PRO_0000166886

Sites

Active site

338

1

Proton acceptor HAMAP MF_00641

Active site

631

1

Proton donor HAMAP MF_00641

Secondary structure

1

.

723

Helix Strand Turn

Details...

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SequencesHide

Sequence

Length

Mass (Da)

Tools

P37330-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 820F177D3FE02632
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FASTA

723

80,489

        10         20         30         40         50         60 
MSQTITQSRL RIDANFKRFV DEEVLPGTGL DAAAFWRNFD EIVHDLAPEN RQLLAERDRI 

        70         80         90        100        110        120 
QAALDEWHRS NPGPVKDKAA YKSFLRELGY LVPQPERVTV ETTGIDSEIT SQAGPQLVVP 

       130        140        150        160        170        180 
AMNARYALNA ANARWGSLYD ALYGSDIIPQ EGAMVSGYDP QRGEQVIAWV RRFLDESLPL 

       190        200        210        220        230        240 
ENGSYQDVVA FKVVDKQLRI QLKNGKETTL RTPAQFVGYR GDAAAPTCIL LKNNGLHIEL 

       250        260        270        280        290        300 
QIDANGRIGK DDPAHINDVI VEAAISTILD CEDSVAAVDA EDKILLYRNL LGLMQGTLQE 

       310        320        330        340        350        360 
KMEKNGRQIV RKLNDDRHYT AADGSEISLH GRSLLFIRNV GHLMTIPVIW DSEGNEIPEG 

       370        380        390        400        410        420 
ILDGVMTGAI ALYDLKVQKN SRTGSVYIVK PKMHGPQEVA FANKLFTRIE TMLGMAPNTL 

       430        440        450        460        470        480 
KMGIMDEERR TSLNLRSCIA QARNRVAFIN TGFLDRTGDE MHSVMEAGPM LRKNQMKSTP 

       490        500        510        520        530        540 
WIKAYERNNV LSGLFCGLRG KAQIGKGMWA MPDLMADMYS QKGDQLRAGA NTAWVPSPTA 

       550        560        570        580        590        600 
ATLHALHYHQ TNVQSVQANI AQTEFNAEFE PLLDDLLTIP VAENANWSAQ EIQQELDNNV 

       610        620        630        640        650        660 
QGILGYVVRW VEQGIGCSKV PDIHNVALME DRATLRISSQ HIANWLRHGI LTKEQVQASL 

       670        680        690        700        710        720 
ENMAKVVDQQ NAGDPAYRPM AGNFANSCAF KAASDLIFLG VKQPNGYTEP LLHAWRLREK 


ESH

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ReferencesHide

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular characterization of Escherichia coli malate synthase G. Differentiation with the malate synthase A isoenzyme." Molina I., Badia J., Aguilar J.T., Pellicer M.T., Baldoma L. Eur. J. Biochem. 224:541-548(1994) [PubMed: 7925370] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-13. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[2]	"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.
[3]	"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.
[4]	"Crystal structure of Escherichia coli malate synthase G complexed with magnesium and glyoxylate at 2.0-A resolution: mechanistic implications." Howard B.R., Endrizzi J.A., Remington S.J. Biochemistry 39:3156-3168(2000) [PubMed: 10715138] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
+	Additional computationally mapped references.

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Cross-referencesHide

Sequence databases

EMBL
GenBank
DDBJ

X74547 Genomic DNA. Translation: CAA52639.1.
U28377 Genomic DNA. Translation: AAA69143.1.
U00096 Genomic DNA. Translation: AAC76012.1.
AP009048 Genomic DNA. Translation: BAE77036.1.

PIR

S51788.

RefSeq

AP_003530.1.
NP_417450.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1D8C	X-ray	2.00	A	3-723	[»]
1P7T	X-ray	1.95	A/B	3-722	[»]
1Y8B	NMR	-	A	3-722	[»]
2JQX	NMR	-	A	3-723	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-9761N.

IntAct

P37330. 6 interactions.

MINT

MINT-1248166.

STRING

P37330.

Genome annotation databases

EnsemblBacteria

EBESCT00000003943; EBESCP00000003943; EBESCG00000003228.
EBESCT00000016414; EBESCP00000015705; EBESCG00000015474.

GeneID

948857.

GenomeReviews

Gene locus JW2943 in contig AP009048_GR.
Gene locus b2976 in contig U00096_GR.

KEGG

ecj:JW2943.
eco:b2976.

Organism-specific databases

EchoBASE

EB4141.

EcoGene

EG20080. glcB.

CMR

Search...

Phylogenomic databases

eggNOG

COG2225.

HOGENOM

HBG350005.

OMA

SQFIENE.

ProtClustDB

PRK02999.

Enzyme and pathway databases

BioCyc

EcoCyc:MALSYNG-MONOMER.
ECOL168927:B2976-MONOMER.
MetaCyc:MALSYNG-MONOMER.

Gene expression databases

Genevestigator

P37330.

Family and domain databases

HAMAP

MF_00641. Malate_synth_G.
[Tree]

InterPro

IPR011076. Malate_synth-like.
IPR001465. Malate_synthase.
IPR006253. Malate_synthG.
[Graphical view]

PANTHER

PTHR21631:SF1. Malate_synthase. 1 hit.

Pfam

PF01274. Malate_synthase. 1 hit.
[Graphical view]

SUPFAM

SSF51645. Malat_synth_like. 1 hit.

TIGRFAMs

TIGR01345. malate_syn_G. 1 hit.

ProtoNet

Search...

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Entry informationHide

Entry name

MASZ_ECOLI

Accession

Primary (citable) accession number: P37330
Secondary accession number(s): Q2M9M0

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	January 23, 2007
Last modified:	July 13, 2010
This is version 95 of the entry and version 3 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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