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P0C890

- MDH_PROVB

UniProt

P0C890 - MDH_PROVB

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Protein

Malate dehydrogenase

Gene

mdh

Organism
Prosthecochloris vibrioformis (Chlorobium vibrioforme)
Status
Reviewed - Annotation score: 3 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 sitei32 – 321NADBy similarity
Binding sitei81 – 811SubstrateBy similarity
Binding sitei87 – 871SubstrateBy similarity
Binding sitei94 – 941NADBy similarity
Binding sitei119 – 1191SubstrateBy similarity
Binding sitei150 – 1501SubstrateBy similarity
Active sitei174 – 1741Proton acceptorBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi7 – 126NADBy similarity
Nucleotide bindingi117 – 1193NADBy similarity

GO - Molecular functioni

  1. L-malate dehydrogenase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. cellular carbohydrate metabolic process Source: InterPro
  2. malate metabolic process Source: InterPro
  3. tricarboxylic acid cycle Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Tricarboxylic acid cycle

Keywords - Ligandi

NAD

Names & Taxonomyi

Protein namesi
Recommended name:
Malate dehydrogenase (EC:1.1.1.37)
Gene namesi
Name:mdh
OrganismiProsthecochloris vibrioformis (Chlorobium vibrioforme)
Taxonomic identifieri1098 [NCBI]
Taxonomic lineageiBacteriaChlorobiChlorobiaChlorobialesChlorobiaceaeProsthecochloris

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 310310Malate dehydrogenasePRO_0000113449Add
BLAST

Interactioni

Subunit structurei

Homotetramer; arranged as a dimer of dimers.1 Publication

Structurei

Secondary structure

1
310
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 65
Helixi10 – 2112
Beta strandi26 – 316
Beta strandi33 – 364
Helixi37 – 4610
Helixi49 – 524
Beta strandi57 – 626
Helixi64 – 674
Beta strandi71 – 755
Helixi87 – 10519
Turni106 – 1083
Beta strandi113 – 1164
Helixi121 – 13212
Helixi136 – 1383
Beta strandi139 – 1413
Helixi144 – 15916
Helixi163 – 1653
Beta strandi170 – 1723
Helixi175 – 1773
Beta strandi178 – 1803
Helixi182 – 1843
Helixi192 – 1943
Helixi198 – 20912
Helixi211 – 2199
Beta strandi220 – 2223
Helixi226 – 24015
Beta strandi245 – 25511
Helixi256 – 2583
Beta strandi260 – 27112
Beta strandi274 – 2785
Helixi285 – 30117

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GUZX-ray2.00A/B/C/D72-310[»]
1GV1X-ray2.50A/B/C/D1-310[»]
ProteinModelPortaliP0C890.
SMRiP0C890. Positions 1-305.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0C890.

Family & Domainsi

Sequence similaritiesi

Belongs to the LDH/MDH superfamily. MDH type 3 family.Curated

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
3.90.110.10. 1 hit.
HAMAPiMF_00487. Malate_dehydrog_3.
InterProiIPR001557. L-lactate/malate_DH.
IPR022383. Lactate/malate_DH_C.
IPR001236. Lactate/malate_DH_N.
IPR015955. Lactate_DH/Glyco_Ohase_4_C.
IPR011275. Malate_DH_type3.
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.
PRINTSiPR00086. LLDHDRGNASE.
SUPFAMiSSF56327. SSF56327. 1 hit.
TIGRFAMsiTIGR01763. MalateDH_bact. 1 hit.

Sequencei

Sequence statusi: Complete.

P0C890 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKITVIGAGN VGATTAFRIA DKKLARELVL LDVVEGIPQG KGLDMYETGP
60 70 80 90 100
VGLFDTKITG SNDYADTADS DIVIITAGLP RKPGMTREDL LMKNAGIVKE
110 120 130 140 150
VTDNIMKHSK NPIIIVVSNP LDIMTHVAWV RSGLPKERVI GMAGVLDAAR
160 170 180 190 200
FRSFIAMELG VSMQDINACV LGGHGDAMVP VVKYTTVAGI PISDLLPAET
210 220 230 240 250
IDKLVERTRN GGAEIVEHLK QGSAFYSPGS SVVEMVESIV LDRKRVLPCA
260 270 280 290 300
VGLEGQYGID KTFVGVPVKL GRNGVEQIYE INLDQADLDL LQKSAKIVDE
310
NCKMLESTIG
Length:310
Mass (Da):33,273
Last modified:October 14, 2008 - v1
Checksum:iDFF3033B27FEC714
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X80837 Genomic DNA. Translation: CAA56809.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X80837 Genomic DNA. Translation: CAA56809.1 .

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1GUZ X-ray 2.00 A/B/C/D 72-310 [» ]
1GV1 X-ray 2.50 A/B/C/D 1-310 [» ]
ProteinModelPortali P0C890.
SMRi P0C890. Positions 1-305.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P0C890.

Family and domain databases

Gene3Di 3.40.50.720. 1 hit.
3.90.110.10. 1 hit.
HAMAPi MF_00487. Malate_dehydrog_3.
InterProi IPR001557. L-lactate/malate_DH.
IPR022383. Lactate/malate_DH_C.
IPR001236. Lactate/malate_DH_N.
IPR015955. Lactate_DH/Glyco_Ohase_4_C.
IPR011275. Malate_DH_type3.
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.
PRINTSi PR00086. LLDHDRGNASE.
SUPFAMi SSF56327. SSF56327. 1 hit.
TIGRFAMsi TIGR01763. MalateDH_bact. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "Malate dehydrogenase from the mesophile Chlorobium vibrioforme and from the mild thermophile Chlorobium tepidum: molecular cloning, construction of a hybrid, and expression in Escherichia coli."
    Naterstad K., Lauvrak V., Sirevag R.
    J. Bacteriol. 178:7047-7052(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Structural basis for thermophilic protein stability: structures of thermophilic and mesophilic malate dehydrogenases."
    Dalhus B., Saarinen M., Sauer U.H., Eklund P., Johansson K., Karlsson A., Ramaswamy S., Bjoerk A., Synstad B., Naterstad K., Sirevaag R., Eklund H.
    J. Mol. Biol. 318:707-721(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), SUBUNIT.

Entry informationi

Entry nameiMDH_PROVB
AccessioniPrimary (citable) accession number: P0C890
Secondary accession number(s): P80038, P94687
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 14, 2008
Last sequence update: October 14, 2008
Last modified: October 1, 2014
This is version 30 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

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3