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P61889

- MDH_ECOLI

UniProt

P61889 - MDH_ECOLI

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Protein

Malate dehydrogenase

Gene

mdh

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Catalyzes the reversible oxidation of malate to oxaloacetate.

Catalytic activityi

(S)-malate + NAD+ = oxaloacetate + NADH.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei34 – 341NAD2 Publications
Binding sitei81 – 811Substrate
Binding sitei87 – 871Substrate
Binding sitei94 – 941NAD2 Publications
Binding sitei119 – 1191Substrate
Binding sitei153 – 1531Substrate
Active sitei177 – 1771Proton acceptor
Binding sitei227 – 2271NAD2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi7 – 137NAD2 Publications
Nucleotide bindingi117 – 1193NAD2 Publications

GO - Molecular functioni

  1. L-malate dehydrogenase activity Source: UniProtKB-HAMAP
  2. malate dehydrogenase activity Source: EcoliWiki
  3. oxidoreductase activity Source: EcoliWiki

GO - Biological processi

  1. anaerobic respiration Source: EcoliWiki
  2. cellular carbohydrate metabolic process Source: InterPro
  3. fermentation Source: EcoliWiki
  4. glycolytic process Source: EcoliWiki
  5. malate metabolic process Source: EcoliWiki
  6. tricarboxylic acid cycle Source: EcoliWiki
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Tricarboxylic acid cycle

Keywords - Ligandi

NAD

Enzyme and pathway databases

BioCyciEcoCyc:MALATE-DEHASE-MONOMER.
ECOL316407:JW3205-MONOMER.
MetaCyc:MALATE-DEHASE-MONOMER.
SABIO-RKP61889.

Names & Taxonomyi

Protein namesi
Recommended name:
Malate dehydrogenase (EC:1.1.1.37)
Gene namesi
Name:mdh
Ordered Locus Names:b3236, JW3205
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10576. mdh.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: EcoliWiki
  2. cytosol Source: UniProtKB
  3. extrinsic component of membrane Source: EcoliWiki
  4. membrane Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi153 – 1531R → C: Loss of interaction with substrate. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 312312Malate dehydrogenasePRO_0000113301Add
BLAST

Proteomic databases

PRIDEiP61889.

2D gel databases

SWISS-2DPAGEP61889.

PTM databases

PhosSiteiP0809413.

Expressioni

Gene expression databases

GenevestigatoriP61889.

Interactioni

Subunit structurei

Homodimer.3 Publications

Protein-protein interaction databases

DIPiDIP-35924N.
IntActiP61889. 10 interactions.

Structurei

Secondary structure

1
312
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 65Combined sources
Turni7 – 93Combined sources
Helixi11 – 2313Combined sources
Beta strandi28 – 336Combined sources
Helixi39 – 479Combined sources
Beta strandi51 – 588Combined sources
Helixi64 – 674Combined sources
Beta strandi71 – 755Combined sources
Helixi87 – 10822Combined sources
Beta strandi112 – 1165Combined sources
Beta strandi118 – 1203Combined sources
Helixi121 – 13414Combined sources
Beta strandi142 – 1454Combined sources
Helixi148 – 16215Combined sources
Helixi166 – 1683Combined sources
Beta strandi173 – 1753Combined sources
Helixi179 – 1813Combined sources
Beta strandi182 – 1843Combined sources
Helixi186 – 1883Combined sources
Helixi196 – 20712Combined sources
Helixi209 – 2168Combined sources
Turni217 – 2193Combined sources
Helixi225 – 24218Combined sources
Beta strandi249 – 2557Combined sources
Beta strandi262 – 27110Combined sources
Beta strandi274 – 2785Combined sources
Helixi286 – 31025Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CMEmodel-A1-312[»]
1EMDX-ray1.90A1-312[»]
1IB6X-ray2.10A/B/C/D1-312[»]
1IE3X-ray2.50A/B/C/D1-312[»]
2CMDX-ray1.87A1-312[»]
2PWZX-ray2.20A/C/E/G1-312[»]
3HHPX-ray1.45A/B/C/D1-312[»]
ProteinModelPortaliP61889.
SMRiP61889. Positions 1-312.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP61889.

Family & Domainsi

Sequence similaritiesi

Belongs to the LDH/MDH superfamily. MDH type 1 family.Curated

Phylogenomic databases

InParanoidiP61889.
KOiK00024.
OMAiKARGVYN.
OrthoDBiEOG6091FG.
PhylomeDBiP61889.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
3.90.110.10. 1 hit.
HAMAPiMF_01516. Malate_dehydrog_1.
InterProiIPR001557. L-lactate/malate_DH.
IPR022383. Lactate/malate_DH_C.
IPR001236. Lactate/malate_DH_N.
IPR015955. Lactate_DH/Glyco_Ohase_4_C.
IPR001252. Malate_DH_AS.
IPR010097. Malate_DH_type1.
IPR023958. Malate_DH_type1_bac.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR11540. PTHR11540. 1 hit.
PfamiPF02866. Ldh_1_C. 1 hit.
PF00056. Ldh_1_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000102. Lac_mal_DH. 1 hit.
SUPFAMiSSF56327. SSF56327. 1 hit.
TIGRFAMsiTIGR01772. MDH_euk_gproteo. 1 hit.
PROSITEiPS00068. MDH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P61889-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKVAVLGAAG GIGQALALLL KTQLPSGSEL SLYDIAPVTP GVAVDLSHIP
60 70 80 90 100
TAVKIKGFSG EDATPALEGA DVVLISAGVA RKPGMDRSDL FNVNAGIVKN
110 120 130 140 150
LVQQVAKTCP KACIGIITNP VNTTVAIAAE VLKKAGVYDK NKLFGVTTLD
160 170 180 190 200
IIRSNTFVAE LKGKQPGEVE VPVIGGHSGV TILPLLSQVP GVSFTEQEVA
210 220 230 240 250
DLTKRIQNAG TEVVEAKAGG GSATLSMGQA AARFGLSLVR ALQGEQGVVE
260 270 280 290 300
CAYVEGDGQY ARFFSQPLLL GKNGVEERKS IGTLSAFEQN ALEGMLDTLK
310
KDIALGEEFV NK
Length:312
Mass (Da):32,337
Last modified:June 7, 2004 - v1
Checksum:i17741A3B5AD068BA
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti37 – 371P → S(PubMed:2993232)Curated
Sequence conflicti70 – 701A → R(PubMed:3322223)Curated
Sequence conflicti80 – 801A → R(PubMed:3299262)Curated
Sequence conflicti80 – 801A → R(PubMed:3322223)Curated
Sequence conflicti116 – 1161I → N(PubMed:3322223)Curated
Sequence conflicti144 – 1441F → L(PubMed:3299262)Curated
Sequence conflicti305 – 3128LGEEFVNK → WAKSSLISN(PubMed:3322223)Curated
Sequence conflicti307 – 3071E → Q(PubMed:3299262)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti71 – 711D → N in strain: EC47, EC49, EC50 and RT272.
Natural varianti106 – 1061A → S in strain: ECOR 27 and RT082.
Natural varianti209 – 2091A → P in strain: MB001D.
Natural varianti218 – 2181A → R in strain: A8190, E2666-74, E830587, E851819, E3406, EC10, EC14, EC32, EC35, EC38, EC40, EC44, EC46, EC47, EC49, EC50, EC52, EC58, E64 and EC70.
Natural varianti232 – 2321A → T in strain: ECO R37.
Natural varianti249 – 2491V → I in strain: RT083.
Natural varianti289 – 2891Q → K in strain: EC35, EC38, EC40, EC44, EC46, EC47 and RT272.
Natural varianti290 – 2901N → S in strain: E2666-74, ECOR 27, ECOR 45, RL012A, RT104 and RT174.
Natural varianti291 – 2911A → S in strain: EC35.
Natural varianti294 – 2941G → A in strain: ECOR 45.
Natural varianti297 – 2971D → N in strain: E830587.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y00129 Genomic DNA. Translation: CAA68326.1.
M24777 Unassigned DNA. Translation: AAA16107.1.
U18997 Genomic DNA. Translation: AAA58038.1.
U00096 Genomic DNA. Translation: AAC76268.1.
AP009048 Genomic DNA. Translation: BAE77279.1.
M10417 Genomic DNA. Translation: AAA24147.1.
U04742 Genomic DNA. Translation: AAC43730.1.
U04743 Genomic DNA. Translation: AAC43731.1.
U04744 Genomic DNA. Translation: AAC43732.1.
U04745 Genomic DNA. Translation: AAC43733.1.
U04746 Genomic DNA. Translation: AAC43734.1.
U04747 Genomic DNA. Translation: AAC43735.1.
U04748 Genomic DNA. Translation: AAC43736.1.
U04749 Genomic DNA. Translation: AAC43737.1.
U04750 Genomic DNA. Translation: AAC43738.1.
U04751 Genomic DNA. Translation: AAC43739.1.
U04752 Genomic DNA. Translation: AAC43740.1.
U04753 Genomic DNA. Translation: AAC43741.1.
U04754 Genomic DNA. Translation: AAC43742.1.
U04755 Genomic DNA. Translation: AAC43743.1.
U04756 Genomic DNA. Translation: AAC43744.1.
U04757 Genomic DNA. Translation: AAC43745.1.
U04758 Genomic DNA. Translation: AAC43746.1.
U04759 Genomic DNA. Translation: AAC43747.1.
U04760 Genomic DNA. Translation: AAC43748.1.
U04770 Genomic DNA. Translation: AAC43758.1.
AF004170 Genomic DNA. Translation: AAB87003.1.
AF004171 Genomic DNA. Translation: AAB87004.1.
AF004172 Genomic DNA. Translation: AAB87005.1.
AF004173 Genomic DNA. Translation: AAB87006.1.
AF004174 Genomic DNA. Translation: AAB87007.1.
AF004175 Genomic DNA. Translation: AAB87008.1.
AF004176 Genomic DNA. Translation: AAB87009.1.
AF004177 Genomic DNA. Translation: AAB87010.1.
AF004179 Genomic DNA. Translation: AAB87012.1.
AF004180 Genomic DNA. Translation: AAB87013.1.
AF004182 Genomic DNA. Translation: AAB87015.1.
AF004183 Genomic DNA. Translation: AAB87016.1.
AF004184 Genomic DNA. Translation: AAB87017.1.
AF004186 Genomic DNA. Translation: AAB87019.1.
AF004187 Genomic DNA. Translation: AAB87020.1.
AF004188 Genomic DNA. Translation: AAB87021.1.
AF004190 Genomic DNA. Translation: AAB87023.1.
AF004191 Genomic DNA. Translation: AAB87024.1.
AF004195 Genomic DNA. Translation: AAB87028.1.
AF004196 Genomic DNA. Translation: AAB87029.1.
AF004199 Genomic DNA. Translation: AAB87032.1.
AF004200 Genomic DNA. Translation: AAB87033.1.
AF004201 Genomic DNA. Translation: AAB87034.1.
AF004202 Genomic DNA. Translation: AAB87035.1.
AF004203 Genomic DNA. Translation: AAB87036.1.
AF004204 Genomic DNA. Translation: AAB87037.1.
AF004205 Genomic DNA. Translation: AAB87038.1.
AF004206 Genomic DNA. Translation: AAB87039.1.
AF004207 Genomic DNA. Translation: AAB87040.1.
AF004208 Genomic DNA. Translation: AAB87041.1.
AF004209 Genomic DNA. Translation: AAB87042.1.
AF091758 Genomic DNA. Translation: AAF97988.1.
AF091759 Genomic DNA. Translation: AAF97989.1.
AF091760 Genomic DNA. Translation: AAF97990.1.
AF091761 Genomic DNA. Translation: AAF97991.1.
AF091762 Genomic DNA. Translation: AAF97992.1.
AF091763 Genomic DNA. Translation: AAF97993.1.
AF091764 Genomic DNA. Translation: AAF97994.1.
AF091765 Genomic DNA. Translation: AAF97995.1.
AF091766 Genomic DNA. Translation: AAF97996.1.
AF091767 Genomic DNA. Translation: AAF97997.1.
AF091768 Genomic DNA. Translation: AAF97998.1.
AF091769 Genomic DNA. Translation: AAF97999.1.
AF091770 Genomic DNA. Translation: AAF98000.1.
AF091771 Genomic DNA. Translation: AAF98001.1.
AF091772 Genomic DNA. Translation: AAF98002.1.
AF091773 Genomic DNA. Translation: AAF98003.1.
AF091774 Genomic DNA. Translation: AAF98004.1.
AF091775 Genomic DNA. Translation: AAF98005.1.
AF091776 Genomic DNA. Translation: AAF98006.1.
AF091777 Genomic DNA. Translation: AAF98007.1.
AF091778 Genomic DNA. Translation: AAF98008.1.
PIRiF65115. DEECM.
RefSeqiNP_417703.1. NC_000913.3.
YP_491420.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC76268; AAC76268; b3236.
BAE77279; BAE77279; BAE77279.
GeneIDi12931785.
947854.
KEGGiecj:Y75_p3156.
eco:b3236.
PATRICi32121898. VBIEscCol129921_3333.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y00129 Genomic DNA. Translation: CAA68326.1 .
M24777 Unassigned DNA. Translation: AAA16107.1 .
U18997 Genomic DNA. Translation: AAA58038.1 .
U00096 Genomic DNA. Translation: AAC76268.1 .
AP009048 Genomic DNA. Translation: BAE77279.1 .
M10417 Genomic DNA. Translation: AAA24147.1 .
U04742 Genomic DNA. Translation: AAC43730.1 .
U04743 Genomic DNA. Translation: AAC43731.1 .
U04744 Genomic DNA. Translation: AAC43732.1 .
U04745 Genomic DNA. Translation: AAC43733.1 .
U04746 Genomic DNA. Translation: AAC43734.1 .
U04747 Genomic DNA. Translation: AAC43735.1 .
U04748 Genomic DNA. Translation: AAC43736.1 .
U04749 Genomic DNA. Translation: AAC43737.1 .
U04750 Genomic DNA. Translation: AAC43738.1 .
U04751 Genomic DNA. Translation: AAC43739.1 .
U04752 Genomic DNA. Translation: AAC43740.1 .
U04753 Genomic DNA. Translation: AAC43741.1 .
U04754 Genomic DNA. Translation: AAC43742.1 .
U04755 Genomic DNA. Translation: AAC43743.1 .
U04756 Genomic DNA. Translation: AAC43744.1 .
U04757 Genomic DNA. Translation: AAC43745.1 .
U04758 Genomic DNA. Translation: AAC43746.1 .
U04759 Genomic DNA. Translation: AAC43747.1 .
U04760 Genomic DNA. Translation: AAC43748.1 .
U04770 Genomic DNA. Translation: AAC43758.1 .
AF004170 Genomic DNA. Translation: AAB87003.1 .
AF004171 Genomic DNA. Translation: AAB87004.1 .
AF004172 Genomic DNA. Translation: AAB87005.1 .
AF004173 Genomic DNA. Translation: AAB87006.1 .
AF004174 Genomic DNA. Translation: AAB87007.1 .
AF004175 Genomic DNA. Translation: AAB87008.1 .
AF004176 Genomic DNA. Translation: AAB87009.1 .
AF004177 Genomic DNA. Translation: AAB87010.1 .
AF004179 Genomic DNA. Translation: AAB87012.1 .
AF004180 Genomic DNA. Translation: AAB87013.1 .
AF004182 Genomic DNA. Translation: AAB87015.1 .
AF004183 Genomic DNA. Translation: AAB87016.1 .
AF004184 Genomic DNA. Translation: AAB87017.1 .
AF004186 Genomic DNA. Translation: AAB87019.1 .
AF004187 Genomic DNA. Translation: AAB87020.1 .
AF004188 Genomic DNA. Translation: AAB87021.1 .
AF004190 Genomic DNA. Translation: AAB87023.1 .
AF004191 Genomic DNA. Translation: AAB87024.1 .
AF004195 Genomic DNA. Translation: AAB87028.1 .
AF004196 Genomic DNA. Translation: AAB87029.1 .
AF004199 Genomic DNA. Translation: AAB87032.1 .
AF004200 Genomic DNA. Translation: AAB87033.1 .
AF004201 Genomic DNA. Translation: AAB87034.1 .
AF004202 Genomic DNA. Translation: AAB87035.1 .
AF004203 Genomic DNA. Translation: AAB87036.1 .
AF004204 Genomic DNA. Translation: AAB87037.1 .
AF004205 Genomic DNA. Translation: AAB87038.1 .
AF004206 Genomic DNA. Translation: AAB87039.1 .
AF004207 Genomic DNA. Translation: AAB87040.1 .
AF004208 Genomic DNA. Translation: AAB87041.1 .
AF004209 Genomic DNA. Translation: AAB87042.1 .
AF091758 Genomic DNA. Translation: AAF97988.1 .
AF091759 Genomic DNA. Translation: AAF97989.1 .
AF091760 Genomic DNA. Translation: AAF97990.1 .
AF091761 Genomic DNA. Translation: AAF97991.1 .
AF091762 Genomic DNA. Translation: AAF97992.1 .
AF091763 Genomic DNA. Translation: AAF97993.1 .
AF091764 Genomic DNA. Translation: AAF97994.1 .
AF091765 Genomic DNA. Translation: AAF97995.1 .
AF091766 Genomic DNA. Translation: AAF97996.1 .
AF091767 Genomic DNA. Translation: AAF97997.1 .
AF091768 Genomic DNA. Translation: AAF97998.1 .
AF091769 Genomic DNA. Translation: AAF97999.1 .
AF091770 Genomic DNA. Translation: AAF98000.1 .
AF091771 Genomic DNA. Translation: AAF98001.1 .
AF091772 Genomic DNA. Translation: AAF98002.1 .
AF091773 Genomic DNA. Translation: AAF98003.1 .
AF091774 Genomic DNA. Translation: AAF98004.1 .
AF091775 Genomic DNA. Translation: AAF98005.1 .
AF091776 Genomic DNA. Translation: AAF98006.1 .
AF091777 Genomic DNA. Translation: AAF98007.1 .
AF091778 Genomic DNA. Translation: AAF98008.1 .
PIRi F65115. DEECM.
RefSeqi NP_417703.1. NC_000913.3.
YP_491420.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1CME model - A 1-312 [» ]
1EMD X-ray 1.90 A 1-312 [» ]
1IB6 X-ray 2.10 A/B/C/D 1-312 [» ]
1IE3 X-ray 2.50 A/B/C/D 1-312 [» ]
2CMD X-ray 1.87 A 1-312 [» ]
2PWZ X-ray 2.20 A/C/E/G 1-312 [» ]
3HHP X-ray 1.45 A/B/C/D 1-312 [» ]
ProteinModelPortali P61889.
SMRi P61889. Positions 1-312.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-35924N.
IntActi P61889. 10 interactions.

Chemistry

DrugBanki DB00336. Nitrofural.

PTM databases

PhosSitei P0809413.

2D gel databases

SWISS-2DPAGE P61889.

Proteomic databases

PRIDEi P61889.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC76268 ; AAC76268 ; b3236 .
BAE77279 ; BAE77279 ; BAE77279 .
GeneIDi 12931785.
947854.
KEGGi ecj:Y75_p3156.
eco:b3236.
PATRICi 32121898. VBIEscCol129921_3333.

Organism-specific databases

EchoBASEi EB0571.
EcoGenei EG10576. mdh.

Phylogenomic databases

InParanoidi P61889.
KOi K00024.
OMAi KARGVYN.
OrthoDBi EOG6091FG.
PhylomeDBi P61889.

Enzyme and pathway databases

BioCyci EcoCyc:MALATE-DEHASE-MONOMER.
ECOL316407:JW3205-MONOMER.
MetaCyc:MALATE-DEHASE-MONOMER.
SABIO-RK P61889.

Miscellaneous databases

EvolutionaryTracei P61889.
PROi P61889.

Gene expression databases

Genevestigatori P61889.

Family and domain databases

Gene3Di 3.40.50.720. 1 hit.
3.90.110.10. 1 hit.
HAMAPi MF_01516. Malate_dehydrog_1.
InterProi IPR001557. L-lactate/malate_DH.
IPR022383. Lactate/malate_DH_C.
IPR001236. Lactate/malate_DH_N.
IPR015955. Lactate_DH/Glyco_Ohase_4_C.
IPR001252. Malate_DH_AS.
IPR010097. Malate_DH_type1.
IPR023958. Malate_DH_type1_bac.
IPR016040. NAD(P)-bd_dom.
[Graphical view ]
PANTHERi PTHR11540. PTHR11540. 1 hit.
Pfami PF02866. Ldh_1_C. 1 hit.
PF00056. Ldh_1_N. 1 hit.
[Graphical view ]
PIRSFi PIRSF000102. Lac_mal_DH. 1 hit.
SUPFAMi SSF56327. SSF56327. 1 hit.
TIGRFAMsi TIGR01772. MDH_euk_gproteo. 1 hit.
PROSITEi PS00068. MDH. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Complete nucleotide sequence of the Escherichia coli gene encoding malate dehydrogenase."
    McAlister-Henn L., Blaber M., Bradshaw R.A., Nisco S.J.
    Nucleic Acids Res. 15:4993-4993(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Cloning and sequence of the mdh structural gene of Escherichia coli coding for malate dehydrogenase."
    Vogel R.F., Entian K.-D., Mecke D.
    Arch. Microbiol. 149:36-42(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. 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. "Isolation and expression of the Escherichia coli gene encoding malate dehydrogenase."
    Sutherland P., McAlister-Henn L.
    J. Bacteriol. 163:1074-1079(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-40.
  6. "Malate dehydrogenase: isolation from E. coli and comparison with the eukaryotic mitochondrial and cytoplasmic forms."
    Fernley R.T., Lentz S.R., Bradshaw R.A.
    Biosci. Rep. 1:497-507(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-36.
  7. "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
    Link A.J., Robison K., Church G.M.
    Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-26.
    Strain: K12 / EMG2.
  8. "Structural studies of malate dehydrogenases (MDHs): MDHs in Brevundimonas species are the first reported MDHs in Proteobacteria which resemble lactate dehydrogenases in primary structure."
    Charnock C.
    J. Bacteriol. 179:4066-4070(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-26.
  9. "Identifying proteins from two-dimensional gels by molecular mass searching of peptide fragments in protein sequence databases."
    Henzel W.J., Billeci T.M., Stults J.T., Wong S.C., Grimley C., Watanabe C.
    Proc. Natl. Acad. Sci. U.S.A. 90:5011-5015(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-16.
  10. "Bacterial defense against aging: role of the Escherichia coli ArcA regulator in gene expression, readjusted energy flux and survival during stasis."
    Nystroem T., Larsson C., Gustafsson L.
    EMBO J. 15:3219-3228(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-13.
  11. Frutiger S., Hughes G.J., Pasquali C., Hochstrasser D.F.
    Submitted (FEB-1996) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 1-11.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  12. Cited for: PROTEIN SEQUENCE OF 1-4.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  13. "Molecular genetic basis of allelic polymorphism in malate dehydrogenase (mdh) in natural populations of Escherichia coli and Salmonella enterica."
    Boyd E.F., Nelson K., Wang F.-S., Whittam T.S., Selander R.K.
    Proc. Natl. Acad. Sci. U.S.A. 91:1280-1284(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 12-299.
    Strain: Various strains.
  14. "Evolutionary relationships among pathogenic and nonpathogenic Escherichia coli strains inferred from multilocus enzyme electrophoresis and mdh sequence studies."
    Pupo G.M., Karaolis D.K., Lan R., Reeves P.R.
    Infect. Immun. 65:2685-2692(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 12-299.
    Strain: Various strains.
  15. "Population genetics of Escherichia coli in a natural population of native Australian rats."
    Pupo G.M., Lan R., Reeves P.R., Baverstock P.R.
    Environ. Microbiol. 2:594-610(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 12-299.
    Strain: Various strains.
  16. "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.
  17. "Crystal structure of Escherichia coli malate dehydrogenase. A complex of the apoenzyme and citrate at 1.87-A resolution."
    Hall M.D., Levitt D.G., Banaszak L.J.
    J. Mol. Biol. 226:867-882(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.87 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG, SUBUNIT.
  18. "Crystal structure of a ternary complex of Escherichia coli malate dehydrogenase citrate and NAD at 1.9 A resolution."
    Hall M.D., Banaszak L.J.
    J. Mol. Biol. 232:213-222(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH NAD AND SUBSTRATE ANALOG, SUBUNIT.
  19. "Structural analyses of a malate dehydrogenase with a variable active site."
    Bell J.K., Yennawar H.P., Wright S.K., Thompson J.R., Viola R.E., Banaszak L.J.
    J. Biol. Chem. 276:31156-31162(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH NAD AND SUBSTRATE ANALOG, SUBUNIT, MUTAGENESIS OF ARG-153.

Entry informationi

Entry nameiMDH_ECOLI
AccessioniPrimary (citable) accession number: P61889
Secondary accession number(s): O30401
, O30402, O30403, P06994, Q2M8X7, Q59343, Q59344, Q59345, Q59346, Q59347, Q59348, Q60133, Q60150, Q933J3, Q93R02, Q9FDQ3, Q9FDQ4, Q9FDQ5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: June 7, 2004
Last modified: October 29, 2014
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3