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Protein

Malate dehydrogenase

Gene

mdh

Organism
Thermus thermophilus
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the reversible oxidation of malate to oxaloacetate.UniRule annotation

Catalytic activityi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei92SubstrateUniRule annotation1
Binding sitei98SubstrateUniRule annotation1
Binding sitei105NADUniRule annotation1
Binding sitei112NADUniRule annotation1 Publication1
Binding sitei131SubstrateUniRule annotation1
Binding sitei162SubstrateUniRule annotation1
Active sitei187Proton acceptorUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi11 – 17NADUniRule annotation2 Publications7
Nucleotide bindingi129 – 131NADUniRule annotation2 Publications3

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Tricarboxylic acid cycle

Keywords - Ligandi

NAD

Enzyme and pathway databases

BRENDAi1.1.1.37. 2305.
SABIO-RKP10584.

Names & Taxonomyi

Protein namesi
Recommended name:
Malate dehydrogenaseUniRule annotation (EC:1.1.1.37UniRule annotation)
Gene namesi
Name:mdhUniRule annotation
OrganismiThermus thermophilus
Taxonomic identifieri274 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL4255.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001134001 – 327Malate dehydrogenaseAdd BLAST327

Proteomic databases

PRIDEiP10584.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi262724.TTC0168.

Chemistry databases

BindingDBiP10584.

Structurei

Secondary structure

1327
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi5 – 11Combined sources7
Helixi15 – 25Combined sources11
Turni26 – 30Combined sources5
Beta strandi36 – 41Combined sources6
Helixi44 – 46Combined sources3
Helixi47 – 58Combined sources12
Turni59 – 61Combined sources3
Beta strandi65 – 72Combined sources8
Helixi74 – 77Combined sources4
Turni78 – 80Combined sources3
Beta strandi82 – 86Combined sources5
Helixi98 – 119Combined sources22
Beta strandi125 – 128Combined sources4
Beta strandi130 – 132Combined sources3
Helixi133 – 142Combined sources10
Helixi149 – 151Combined sources3
Beta strandi152 – 154Combined sources3
Helixi157 – 171Combined sources15
Helixi175 – 177Combined sources3
Beta strandi182 – 185Combined sources4
Beta strandi192 – 194Combined sources3
Helixi205 – 207Combined sources3
Helixi211 – 216Combined sources6
Helixi218 – 233Combined sources16
Helixi238 – 253Combined sources16
Beta strandi262 – 267Combined sources6
Helixi271 – 273Combined sources3
Beta strandi278 – 287Combined sources10
Beta strandi290 – 293Combined sources4
Helixi301 – 323Combined sources23

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BDMX-ray1.80A/B1-327[»]
1BMDX-ray1.90A/B1-327[»]
1IZ9X-ray2.00A/B1-327[»]
1WZEX-ray2.00A/B1-327[»]
1WZIX-ray2.00A/B1-327[»]
1Y7TX-ray1.65A/B1-327[»]
2CVQX-ray2.08A/B1-321[»]
4KDEX-ray1.80A/B1-327[»]
4KDFX-ray2.36A/B/C/D1-327[»]
ProteinModelPortaliP10584.
SMRiP10584.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP10584.

Family & Domainsi

Sequence similaritiesi

Belongs to the LDH/MDH superfamily. MDH type 2 family.UniRule annotationCurated

Phylogenomic databases

eggNOGiENOG4105D9Z. Bacteria.
COG0039. LUCA.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
3.90.110.10. 1 hit.
HAMAPiMF_01517. Malate_dehydrog_2. 1 hit.
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.
IPR010945. Malate_DH_type2.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR23382. PTHR23382. 1 hit.
PfamiPF02866. Ldh_1_C. 1 hit.
PF00056. Ldh_1_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000102. Lac_mal_DH. 1 hit.
SUPFAMiSSF51735. SSF51735. 1 hit.
SSF56327. SSF56327. 1 hit.
TIGRFAMsiTIGR01759. MalateDH-SF1. 1 hit.
PROSITEiPS00068. MDH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P10584-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKAPVRVAVT GAAGQIGYSL LFRIAAGEML GKDQPVILQL LEIPQAMKAL
60 70 80 90 100
EGVVMELEDC AFPLLAGLEA TDDPKVAFKD ADYALLVGAA PRKAGMERRD
110 120 130 140 150
LLQVNGKIFT EQGRALAEVA KKDVKVLVVG NPANTNALIA YKNAPGLNPR
160 170 180 190 200
NFTAMTRLDH NRAKAQLAKK TGTGVDRIRR MTVWGNHSST MFPDLFHAEV
210 220 230 240 250
DGRPALELVD MEWYEKVFIP TVAQRGAAII QARGASSAAS AANAAIEHIR
260 270 280 290 300
DWALGTPEGD WVSMAVPSQG EYGIPEGIVY SFPVTAKDGA YRVVEGLEIN
310 320
EFARKRMEIT AQELLDEMEQ VKALGLI
Length:327
Mass (Da):35,426
Last modified:July 1, 1989 - v1
Checksum:i31FA90DED2393DF2
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti190T → I in strain: F428; produces a 2 to 3 times higher enzyme activity. 1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02598 Genomic DNA. Translation: AAA27499.1.
X54073 Genomic DNA. Translation: CAA38008.1.
X56033 Genomic DNA. Translation: CAA39508.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02598 Genomic DNA. Translation: AAA27499.1.
X54073 Genomic DNA. Translation: CAA38008.1.
X56033 Genomic DNA. Translation: CAA39508.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BDMX-ray1.80A/B1-327[»]
1BMDX-ray1.90A/B1-327[»]
1IZ9X-ray2.00A/B1-327[»]
1WZEX-ray2.00A/B1-327[»]
1WZIX-ray2.00A/B1-327[»]
1Y7TX-ray1.65A/B1-327[»]
2CVQX-ray2.08A/B1-321[»]
4KDEX-ray1.80A/B1-327[»]
4KDFX-ray2.36A/B/C/D1-327[»]
ProteinModelPortaliP10584.
SMRiP10584.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi262724.TTC0168.

Chemistry databases

BindingDBiP10584.
ChEMBLiCHEMBL4255.

Proteomic databases

PRIDEiP10584.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4105D9Z. Bacteria.
COG0039. LUCA.

Enzyme and pathway databases

BRENDAi1.1.1.37. 2305.
SABIO-RKP10584.

Miscellaneous databases

EvolutionaryTraceiP10584.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
3.90.110.10. 1 hit.
HAMAPiMF_01517. Malate_dehydrog_2. 1 hit.
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.
IPR010945. Malate_DH_type2.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR23382. PTHR23382. 1 hit.
PfamiPF02866. Ldh_1_C. 1 hit.
PF00056. Ldh_1_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000102. Lac_mal_DH. 1 hit.
SUPFAMiSSF51735. SSF51735. 1 hit.
SSF56327. SSF56327. 1 hit.
TIGRFAMsiTIGR01759. MalateDH-SF1. 1 hit.
PROSITEiPS00068. MDH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMDH_THETH
AccessioniPrimary (citable) accession number: P10584
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: November 2, 2016
This is version 131 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, Direct protein sequencing

Documents

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.