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Protein

Malate dehydrogenase, mitochondrial

Gene

MDH

Organism
Eucalyptus gunnii (Cider gum)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei67 – 671NADBy similarity
Binding sitei114 – 1141SubstratePROSITE-ProRule annotation
Binding sitei120 – 1201SubstratePROSITE-ProRule annotation
Binding sitei127 – 1271NADBy similarity
Binding sitei152 – 1521SubstratePROSITE-ProRule annotation
Binding sitei186 – 1861SubstratePROSITE-ProRule annotation
Active sitei210 – 2101Proton acceptorBy similarity
Binding sitei261 – 2611NADBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi41 – 477NADBy similarity
Nucleotide bindingi150 – 1523NADBy similarity

GO - Molecular functioni

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

GO - Biological processi

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

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Tricarboxylic acid cycle

Keywords - Ligandi

NAD

Names & Taxonomyi

Protein namesi
Recommended name:
Malate dehydrogenase, mitochondrial (EC:1.1.1.37)
Gene namesi
Name:MDH
OrganismiEucalyptus gunnii (Cider gum)
Taxonomic identifieri3933 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsMyrtalesMyrtaceaeEucalyptus

Subcellular locationi

GO - Cellular componenti

  1. mitochondrial matrix Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2727MitochondrionSequence AnalysisAdd
BLAST
Chaini28 – 347320Malate dehydrogenase, mitochondrialPRO_0000018626Add
BLAST

Proteomic databases

PRIDEiP46487.

Interactioni

Subunit structurei

Homodimer.By similarity

Structurei

3D structure databases

ProteinModelPortaliP46487.
SMRiP46487. Positions 36-344.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Keywords - Domaini

Transit peptide

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
3.90.110.10. 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.
IPR010097. Malate_DH_type1.
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.

Sequence processingi: The displayed sequence is further processed into a mature form.

P46487-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRASMLRLIR SRSSSAAPRP HLLRRAYGSE SVPERKVAVL GAAGGIGQPL
60 70 80 90 100
ALLMKLNPLV SQLALYDIAG TPGVAADVGH INTRSEVAGY VGEEQLGQAL
110 120 130 140 150
EGSDVVIIPA GVPRKPGMTR DDLFNINAGI VKSLCTAIAK YCPNAVVNMI
160 170 180 190 200
SNPVNSTVPI AAEIFKKAGT YNEKKLLGVT TLDVVRAKTF YAGKAKVPVE
210 220 230 240 250
EVNVPVVGGH AGITILPLFS QAVPKANLAD EDIKALTKRT QDGGTEVVEA
260 270 280 290 300
KAGKGSATLS MAYAGALFAD ACLKGLNGVP DVVECSFVQS SIITELPFFA
310 320 330 340
SKVKLGKNGV EEVLELGPMS DYEKQGLEIL IPELKASIEK GIKFANQ
Length:347
Mass (Da):36,462
Last modified:November 1, 1995 - v1
Checksum:i450F8254CCC84789
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X78800 mRNA. Translation: CAA55383.1.
PIRiS44167.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X78800 mRNA. Translation: CAA55383.1.
PIRiS44167.

3D structure databases

ProteinModelPortaliP46487.
SMRiP46487. Positions 36-344.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiP46487.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
3.90.110.10. 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.
IPR010097. Malate_DH_type1.
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]
ProtoNetiSearch...

Publicationsi

  1. "Nucleotide sequence of a cDNA encoding mitochondrial malate dehydrogenase from Eucalyptus."
    Poeydomenge O., Boudet A.M., Grima-Pettenati J., Marolda M.
    Plant Physiol. 107:1455-1456(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Entry informationi

Entry nameiMDHM_EUCGU
AccessioniPrimary (citable) accession number: P46487
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: January 7, 2015
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.