mdh:Gene Product(s)

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Nomenclature Function Interactions Localization Sequence Domains Structure Resources Accessions Links References Suggestions

Nomenclature

See Help:Product_nomenclature for help entering or editing information in this section of EcoliWiki.

Standard name

Mdh

Synonyms

malate dehydrogenase, NAD(P)-binding[1], B3236[2][1], Mdh[2][1] , ECK3225, JW3205, b3236

Product description

Mdh[2][3];

Component of malate dehydrogenase[2][3]

Malate dehydrogenase, NAD-dependent[4]

EC number (for enzymes)
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Notes

Function

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<protect> Gene Ontology
See Help:Gene_ontology for help entering or editing GO terms and GO annotations in EcoliWiki.

Qualifier GO ID GO term name Reference Evidence Code with/from Aspect Notes Status
GO:0005737

cytoplasm

C

Seeded from Riley et al 2006 [1].

Missing: evidence, reference

GO:0016615

malate dehydrogenase activity

PMID:4914076[5]

IMP: Inferred from Mutant Phenotype

F

complete

GO:0000300

peripheral to membrane of membrane fraction

PMID:15976458[6]

IDA: Inferred from Direct Assay

C

Seeded from EcoCyc (v14.0)

complete

GO:0005488

binding

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR016040

F

Seeded from EcoCyc (v14.0)

complete

GO:0005737

cytoplasm

PMID:4914076[5]

IDA: Inferred from Direct Assay

C

Seeded from EcoCyc (v14.0)

complete

GO:0005829

cytosol

PMID:16858726[7]

IDA: Inferred from Direct Assay

C

Seeded from EcoCyc (v14.0)

complete

GO:0005975

carbohydrate metabolic process

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR015955

P

Seeded from EcoCyc (v14.0)

complete

GO:0006096

glycolysis

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR001557

P

Seeded from EcoCyc (v14.0)

complete

GO:0016615

malate dehydrogenase activity

PMID:4960671[8]

IDA: Inferred from Direct Assay

F

complete

GO:0006099

tricarboxylic acid cycle

GOA:hamap
GO_REF:0000020

IEA: Inferred from Electronic Annotation

HAMAP:MF_01516

P

Seeded from EcoCyc (v14.0)

complete

GO:0016491

oxidoreductase activity

PMID:4960671[8]

IDA: Inferred from Direct Assay

F

complete

GO:0006099

tricarboxylic acid cycle

GOA:spkw
SP_KW:GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0816

P

Seeded from EcoCyc (v14.0)

complete

GO:0006108

malate metabolic process

PMID:4960671[8]

IDA: Inferred from Direct Assay

P

complete

GO:0006108

malate metabolic process

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR001252

P

Seeded from EcoCyc (v14.0)

complete

GO:0006108

malate metabolic process

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR010097

P

Seeded from EcoCyc (v14.0)

complete

GO:0009061

anaerobic respiration

PMID:2993232[9]

IDA: Inferred from Direct Assay

P

complete

GO:0016020

membrane

PMID:16858726[7]

IDA: Inferred from Direct Assay

C

Seeded from EcoCyc (v14.0)

complete

GO:0016615

malate dehydrogenase activity

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR001252

F

Seeded from EcoCyc (v14.0)

complete

GO:0006113

fermentation

PMID:2993232[9]

IDA: Inferred from Direct Assay

P

complete

GO:0016616

oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR001557

F

Seeded from EcoCyc (v14.0)

complete

GO:0006099

tricarboxylic acid cycle

PMID:2993232[9]

IDA: Inferred from Direct Assay

P

complete

GO:0016615

malate dehydrogenase activity

PMID:2993232[9]

IDA: Inferred from Direct Assay

F

complete

GO:0030060

L-malate dehydrogenase activity

GOA:hamap
GO_REF:0000020

IEA: Inferred from Electronic Annotation

HAMAP:MF_01516

F

Seeded from EcoCyc (v14.0)

complete

GO:0005737

cytoplasm

PMID:4914076[5]

IDA: Inferred from Direct Assay

C

The authors conclude that 96% of malate dehydrogenase (Mdh) activity was present in the soluble fraction of mechanically disrupted cells subjected to ultracentrifugation while 4% was in the membrane fraction (cells were grown in minimal malate medium) (pp 725).

complete

GO:0006096

glycolysis

PMID:2993232[9]

IDA: Inferred from Direct Assay

P

complete

GO:0030060

L-malate dehydrogenase activity

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR010097

F

Seeded from EcoCyc (v14.0)

complete

GO:0000300

peripheral to membrane of membrane fraction

PMID:15976458[6]

IDA: Inferred from Direct Assay

C

The authors demonstrate the presence of Mdh in the membrane fraction (Figure 3).

complete

GO:0030060

L-malate dehydrogenase activity

GOA:spec
GO_REF:0000003

IEA: Inferred from Electronic Annotation

EC:1.1.1.37

F

Seeded from EcoCyc (v14.0)

complete

GO:0055114

oxidation reduction

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR001236

P

Seeded from EcoCyc (v14.0)

complete

GO:0055114

oxidation reduction

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR001252

P

Seeded from EcoCyc (v14.0)

complete

GO:0055114

oxidation reduction

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR001557

P

Seeded from EcoCyc (v14.0)

complete

GO:0055114

oxidation reduction

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR010097

P

Seeded from EcoCyc (v14.0)

complete

GO:0055114

oxidation reduction

GOA:spkw
SP_KW:GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0560

P

Seeded from EcoCyc (v14.0)

complete

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Interactions See Help:Product_interactions for help entering or editing information about gene product interactions in this section of EcoliWiki.

Partner Type Partner Notes References Evidence

Protein

Subunits of malate dehydrogenase

could be indirect

Protein

rpsD

PMID:16606699[10]

Experiment(s):EBI-1145248

Protein

rplC

PMID:16606699[10]

Experiment(s):EBI-1145248
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Notes

Localization

See Help:Product_localization for how to add or edit information in this section of EcoliWiki.

Compartment Description Evidence Reference/Source Notes

Cytoplasm

PMID:7028159[11]

EchoLocation:mdh


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Notes

Structure and Physical Properties

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<protect> Physical Properties See Help:Product_physical_properties for help entering or editing information about the physical properties of this gene product.

Name
Sequence

at EcoCyc 

MKVAVLGAAG GIGQALALLL KTQLPSGSEL SLYDIAPVTP GVAVDLSHIP TAVKIKGFSG
EDATPALEGA DVVLISAGVA RKPGMDRSDL FNVNAGIVKN LVQQVAKTCP KACIGIITNP
VNTTVAIAAE VLKKAGVYDK NKLFGVTTLD IIRSNTFVAE LKGKQPGEVE VPVIGGHSGV
TILPLLSQVP GVSFTEQEVA DLTKRIQNAG TEVVEAKAGG GSATLSMGQA AARFGLSLVR
ALQGEQGVVE CAYVEGDGQY ARFFSQPLLL GKNGVEERKS IGTLSAFEQN ALEGMLDTLK
KDIALGEEFV NK
Length

312

Mol. Wt

32.336 kDa

pI

5.6 (calculated)

Extinction coefficient

5,960 - 6,335 (calc based on 4 Y, 0 W, and 3 C residues)

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Domains/Motifs/Modification Sites

See Help:Product_domains_motifs for help entering or editing information in this section of EcoliWiki.

Type Residues Description Notes References

Modification Site

26

phosphorylation site at S26

probability less than 75%

PMID:17938405[12]

Modification Site

28

phosphorylation site at S28

probability less than 75%

PMID:17938405[12]

Modification Site

193

phosphorylation site at S193

probability greater than 75%

PMID:17938405[12]

Modification Site

280

phosphorylation site at S280

probability greater than 75%

PMID:17938405[12]

Domain

1..145

PF00056 lactate/malate dehydrogenase, NAD binding domain

PMID:19920124[13]

Domain

147..310

PF02866 lactate/malate dehydrogenase, alpha/beta C-terminal domain

PMID:19920124[13]

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Structure
See Help:Product_structure for help entering or editing information in this section of EcoliWiki.

Structures

<beststructure> gene=mdh taxon=562,83333 </beststructure>

Models

View models at:

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Structure figures

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Notes

Gene Product Resources

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See Help:Product_resources for help with entering or editing information in this section of EcoliWiki.

Resource type Source Notes/Reference
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Notes

Accessions in Other Databases

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See Help:Gene_accessions for help with entering information into the Gene Accessions table.

Database Accession Notes

NCBI (Protein) (EcoliWiki Page)

GI:16131126

Escherichia coli str. K-12 substr. MG1655

NCBI (Protein) (EcoliWiki Page)

GeneID:947854

Escherichia coli str. K-12 substr. MG1655

ASAP

ASAP:ABE-0010613

Escherichia coli str. K-12 substr. MG1655

UniProt (EcoliWiki Page)

UniProtKB/Swiss-Prot:P61889

Escherichia coli str. K-12 substr. MG1655

EcoCyc

EcoCyc:EG10576

Escherichia coli str. K-12 substr. MG1655

EcoGene

EcoGene:EG10576

Escherichia coli str. K-12 substr. MG1655

NCBI (Gene) (EcoliWiki Page)

GeneID:947854

Escherichia coli str. K-12 substr. MG1655

RegulonDB

RegulonDB:ECK120000569

Escherichia coli str. K-12 substr. MG1655

EchoBASE

EchoBASE:EB0571

Escherichia coli str. K-12 substr. MG1655

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Notes

Links

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References

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See Help:References for how to manage references in EcoliWiki.

  1. ↑ 1.0 1.1 1.2 1.3 1.4 Riley, M. et al. (2006) Nucleic Acids Res 34:1-6 (corrected supplemental data from B. Wanner)
  2. ↑ 2.0 2.1 2.2 2.3 EcoCyc (release 10.6; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  3. ↑ 3.0 3.1 EcoCyc (release 11.1; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  4. ↑ EcoGene: Rudd, KE (2000) EcoGene: a genome sequence database for Escherichia coli K-12. Nucleic Acids Res 28:60-4.
  5. ↑ 5.0 5.1 5.2 Courtright, JB & Henning, U (1970) Malate dehydrogenase mutants in Escherichia coli K-12. J. Bacteriol. 102 722-8 PubMed
  6. ↑ 6.0 6.1 Amarneh, B & Vik, SB (2005) Direct transfer of NADH from malate dehydrogenase to complex I in Escherichia coli. Cell Biochem. Biophys. 42 251-61 PubMed
  7. ↑ 7.0 7.1 Lasserre, JP et al. (2006) A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis. Electrophoresis 27 3306-21 PubMed
  8. ↑ 8.0 8.1 8.2 Murphey, WH et al. (1967) Malate dehydrogenases. II. Purification and properties of Bacillus subtilis, Bacillus stearothermophilus, and Escherichia coli malate dehydrogenases. J. Biol. Chem. 242 1548-59 PubMed
  9. ↑ 9.0 9.1 9.2 9.3 9.4 Sutherland, P & McAlister-Henn, L (1985) Isolation and expression of the Escherichia coli gene encoding malate dehydrogenase. J. Bacteriol. 163 1074-9 PubMed
  10. ↑ 10.0 10.1 Arifuzzaman, M et al. (2006) Large-scale identification of protein-protein interaction of Escherichia coli K-12. Genome Res. 16 686-91 PubMed
  11. ↑ Fernley, RT et al. (1981) Malate dehydrogenase: isolation from E. coli and comparison with the eukaryotic mitochondrial and cytoplasmic forms. Biosci. Rep. 1 497-507 PubMed
  12. ↑ 12.0 12.1 12.2 12.3 Macek, B et al. (2008) Phosphoproteome analysis of E. coli reveals evolutionary conservation of bacterial Ser/Thr/Tyr phosphorylation. Mol. Cell Proteomics 7 299-307 PubMed
  13. ↑ 13.0 13.1 Finn, RD et al. (2010) The Pfam protein families database. Nucleic Acids Res. 38 D211-22 PubMed

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