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P17783 (MDHM_CITLA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Malate dehydrogenase, mitochondrial

EC=1.1.1.37
Gene names
Name:MMDH
OrganismCitrullus lanatus (Watermelon) (Citrullus vulgaris)
Taxonomic identifier3654 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsCucurbitalesCucurbitaceaeBenincaseaeCitrullus

Protein attributes

Sequence length347 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.

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_processcellular carbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

malate metabolic process

Inferred from electronic annotation. Source: InterPro

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: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2727Mitochondrion Ref.2
Chain28 – 347320Malate dehydrogenase, mitochondrial
PRO_0000018625

Regions

Nucleotide binding41 – 477NAD By similarity
Nucleotide binding150 – 1523NAD By similarity

Sites

Active site2101Proton acceptor By similarity
Binding site671NAD By similarity
Binding site1141Substrate By similarity
Binding site1201Substrate By similarity
Binding site1271NAD By similarity
Binding site1521Substrate By similarity
Binding site1861Substrate By similarity
Binding site2611NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
P17783 [UniParc].

Last modified August 1, 1990. Version 1.
Checksum: 31474F15018D30CC

FASTA34736,201
        10         20         30         40         50         60 
MKASILRSVR SAVSRSSSSN RLLSRSFATE SVPERKVAVL GAAGGIGQPL ALLMKLNPLV 

        70         80         90        100        110        120 
SKLALYDIAG TPGVAADVGH VNTRSEVTGY VGEEQLGKAL EGSDVVIIPA GVPRKPGMTR 

       130        140        150        160        170        180 
DDLFNINAGI VKSLCTAIAK YCPNALINMI SNPVNSTVPI AAEVFKKAGT YDEKKLFGVT 

       190        200        210        220        230        240 
TLDVVRAKTF YAGKANVPVA EVNVPVIGGH AGITILPLFS QATPRANLSD DTIVALTKRT 

       250        260        270        280        290        300 
QDGGTEVVEA KAGKGSATLS MAYAGALFAD ACLKGLNGVP DVVECSFVQS TVTELPFFAS 

       310        320        330        340 
KVKLGKNGVE SVLDLGPLSD FEKEGLEKLK PELKASIEKG IQFANAN 

« Hide

References

[1]"Mitochondrial malate dehydrogenase from watermelon: sequence of cDNA clones and primary structure of the higher-plant precursor protein."
Gietl C., Lehnerer M., Olsen O.
Plant Mol. Biol. 14:1019-1030(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
Strain: cv. Sugar Baby.
Tissue: Cotyledon.
[2]"Sequence homologies between glyoxysomal and mitochondrial malate dehydrogenase."
Gietl C., Lottspeich F., Hock B.
Planta 169:555-558(1986)
Cited for: PROTEIN SEQUENCE OF 28-55.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X17362 mRNA. Translation: CAA35239.1.
PIRDEPUMW. S10162.

3D structure databases

ProteinModelPortalP17783.
SMRP17783. Positions 36-343.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

Allergome6159. Cit la MDH.

Proteomic databases

PRIDEP17783.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.40.50.720. 1 hit.
3.90.110.10. 1 hit.
InterProIPR001557. 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]
PANTHERPTHR11540. PTHR11540. 1 hit.
PTHR11540:SF1. PTHR11540:SF1. 1 hit.
PfamPF02866. Ldh_1_C. 1 hit.
PF00056. Ldh_1_N. 1 hit.
[Graphical view]
PIRSFPIRSF000102. Lac_mal_DH. 1 hit.
SUPFAMSSF56327. SSF56327. 1 hit.
TIGRFAMsTIGR01772. MDH_euk_gproteo. 1 hit.
PROSITEPS00068. MDH. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMDHM_CITLA
AccessionPrimary (citable) accession number: P17783
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1990
Last modified: February 19, 2014
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families