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P19446 (MDHG_CITLA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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, glyoxysomal

EC=1.1.1.37
OrganismCitrullus lanatus (Watermelon) (Citrullus vulgaris)
Taxonomic identifier3654 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsCucurbitalesCucurbitaceaeBenincaseaeCitrullus

Protein attributes

Sequence length356 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. Ref.3

Subcellular location

Glyoxysome.

Sequence similarities

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

Biophysicochemical properties

Kinetic parameters:

KM=146 µM for NADH

KM=76 mM for oxaloacetate

Ontologies

Keywords
   Biological processGlyoxylate bypass
Tricarboxylic acid cycle
   Cellular componentGlyoxysome
Peroxisome
   DomainTransit peptide
   LigandNAD
   Molecular functionOxidoreductase
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processglyoxylate cycle

Inferred from electronic annotation. Source: UniProtKB-KW

malate metabolic process

Inferred from electronic annotation. Source: InterPro

tricarboxylic acid cycle

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentglyoxysome

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 – 3636Glyoxysome Ref.2 Ref.3
Chain37 – 356320Malate dehydrogenase, glyoxysomal
PRO_0000018638

Regions

Nucleotide binding51 – 577NAD By similarity
Nucleotide binding160 – 1623NAD By similarity

Sites

Active site2201Proton acceptor
Binding site771NAD By similarity
Binding site1241Substrate
Binding site1301Substrate
Binding site1371NAD By similarity
Binding site1621Substrate
Binding site1961Substrate
Binding site2711NAD By similarity

Secondary structure

............................................. 356
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P19446 [UniParc].

Last modified February 1, 1991. Version 1.
Checksum: 4B0C8101DC11FC7F

FASTA35637,637
        10         20         30         40         50         60 
MQPIPDVNQR IARISAHLHP PKSQMEESSA LRRANCRAKG GAPGFKVAIL GAAGGIGQPL 

        70         80         90        100        110        120 
AMLMKMNPLV SVLHLYDVVN APGVTADISH MDTGAVVRGF LGQQQLEAAL TGMDLIIVPA 

       130        140        150        160        170        180 
GVPRKPGMTR DDLFKINAGI VKTLCEGIAK CCPRAIVNLI SNPVNSTVPI AAEVFKKAGT 

       190        200        210        220        230        240 
YDPKRLLGVT MLDVVRANTF VAEVLGLDPR DVDVPVVGGH AGVTILPLLS QVKPPSSFTQ 

       250        260        270        280        290        300 
EEISYLTDRI QNGGTEVVEA KAGAGSATLS MAYAAVKFAD ACLRGLRGDA GVIECAFVSS 

       310        320        330        340        350 
QVTELPFFAS KVRLGRNGIE EVYSLGPLNE YERIGLEKAK KELAGSIEKG VSFIRS 

« Hide

References

[1]"Glyoxysomal malate dehydrogenase from watermelon is synthesized with an amino-terminal transit peptide."
Gietl C.
Proc. Natl. Acad. Sci. U.S.A. 87:5773-5777(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
Strain: cv. Sugar Baby.
[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 37-65.
[3]"Organelle and translocatable forms of glyoxysomal malate dehydrogenase. The effect of the N-terminal presequence."
Cox B., Chit M.M., Weaver T., Gietl C., Bailey J., Bell E., Banaszak L.
FEBS J. 272:643-654(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF N-TERMINUS, X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG, PHYSICOCHEMICAL PROPERTIES, SUBUNIT, IDENTIFICATION BY MASS SPECTROMETRY.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M33148 mRNA. Translation: AAA33041.1.
PIRDEPUGW. A35957.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1SEVX-ray2.55A/B1-356[»]
1SMKX-ray2.50A/B/C/D/E/F/G/H37-356[»]
ProteinModelPortalP19446.
SMRP19446. Positions 44-356.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEP19446.

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...

Other

EvolutionaryTraceP19446.

Entry information

Entry nameMDHG_CITLA
AccessionPrimary (citable) accession number: P19446
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: April 16, 2014
This is version 101 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references