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Reviewed, UniProtKB/Swiss-Prot P83373 (MDHM_FRAAN)

Last modified February 9, 2010. Version 55. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Malate dehydrogenase, mitochondrial
    EC=1.1.1.37
Gene names
Name: MMDHI
OrganismFragaria ananassa (Strawberry)
Taxonomic identifier3747 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidsfabidsRosalesRosaceaeRosoideaeFragaria

Protein attributes

Sequence length339 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Catalytic activity

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

Subunit structure

Homodimer By similarity.

Subcellular location

Mitochondrion matrix.

Sequence similarities

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

Ontologies

Keywords
   Biological processTricarboxylic acid cycle
   Cellular componentMitochondrion
   DomainTransit peptide
   LigandNAD
   Molecular functionOxidoreductase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processglycolysis

Inferred from electronic annotation. Source: InterPro

malate metabolic process

Inferred from electronic annotation. Source: InterPro

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

tricarboxylic acid cycle

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentmitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionL-malate dehydrogenase activity

Inferred from electronic annotation. Source: EC

binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 1919Mitochondrion Ref.1 UniProtKB P00346
Chain20 – 339320Malate dehydrogenase, mitochondrial UniProtKB P00346
PRO_0000018627

Regions

Nucleotide binding33 – 397NAD By similarity
Nucleotide binding142 – 1443NAD By similarity

Sites

Active site2021Proton acceptor By similarity
Binding site591NAD By similarity
Binding site1061Substrate By similarity
Binding site1121Substrate By similarity
Binding site1191NAD By similarity
Binding site1441Substrate By similarity
Binding site1781Substrate By similarity
Binding site2531NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
P83373-1 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: 22D4EF65E225A00C

FASTA33935,622
        10         20         30         40         50         60 
MRPSMSLIRS VSRVARRGYS SESVPQRKVA VLGAAGGIGQ PLALLMKLNP LVSQLSLYDI 

        70         80         90        100        110        120 
AGTPGVAADV SHINTRSEVK GYAGEEQLGE ALEGCDVVII PAGVPRKPGM TRDDLFNINA 

       130        140        150        160        170        180 
GIVRSLTAAI AKYCPHAIIN MISNPVNSTV PIASEVLKKA GVYDEKKLFG VTTLDVVRAK 

       190        200        210        220        230        240 
TFYAGKAGVP VAEVNVPVVG GHAGITILPL FSQATPKANL SDDYIKALTK RTQDGGTEVV 

       250        260        270        280        290        300 
EAKAGKGSAT LSMAYAGALF ADACLXGLNG VPDVVECSYV QSSITELPFF ASKVRLGKNG 

       310        320        330 
VEEVLDLGPL SDFEKEGLKQ LKPELKSSIE KGIKFANQS 

« Hide

References

[1]"Identification, cloning and expression analysis of strawberry (Fragaria x ananassa) mitochondrial citrate synthase and mitochondrial malate dehydrogenase."
Iannetta P.P.M., Escobar N.M., Ross H.A., Souleyre E.J., Hancock R.D., Witte C.P., Davies H.V.
Physiol. Plantarum 121:15-26(2004) [PubMed: 15086813] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE, PROTEIN SEQUENCE OF 20-37.
Strain: cv. Elsanta.
Tissue: Fruit.

Cross-references

3D structure databases

ModBaseSearch...

Enzyme and pathway databases

BRENDA1.1.1.37. 275939.

Family and domain databases

InterProIPR001557. L-lactate/malate_DH.
IPR001236. Lactate/malate_DH.
IPR015955. Lactate_DH/Glyco_Ohase_4_C.
IPR001252. Malate_DH_AS.
IPR010097. Malate_DH_NAD-dep_euk/g-bac.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
Gene3DG3DSA:3.90.110.10. lact_mal_DH. 1 hit.
G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PANTHERPTHR11540:SF1. MDH_euk_g_bac. 1 hit.
PfamPF02866. Ldh_1_C. 1 hit.
PF00056. Ldh_1_N. 1 hit.
[Graphical view]
PIRSFPIRSF000102. Lac_mal_DH. 1 hit.
TIGRFAMsTIGR01772. MDH_euk_gproteo. 1 hit.
PROSITEPS00068. MDH. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMDHM_FRAAN
AccessionPrimary (citable) accession number: P83373
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 2002
Last sequence update: October 1, 2002
Last modified: February 9, 2010
This is version 55 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents