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Reviewed, UniProtKB/Swiss-Prot P17783 (MDHM_CITLA)

Last modified June 16, 2009. Version 71. 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

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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 lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids I › Cucurbitales › Cucurbitaceae › Citrullus

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Protein attributes

Sequence length347 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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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.

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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...

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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

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Sequences

Sequence LengthMass (Da)Tools
P17783-1 [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

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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: 2102869] [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.

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Cross-references

Sequence databases

X17362 mRNA. Translation: CAA35239.1.
PIRDEPUMW. S10162.

3D structure databases

HSSPHSSP built from PDB template 1MLD based on UniProtKB P00346.
ModBaseSearch...

Enzyme and pathway databases

BRENDA1.1.1.37. 81664.

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...

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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: June 16, 2009
This is version 71 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

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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