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Q9ZF99 (MDH_AQUAR) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 95. 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

EC=1.1.1.37
Gene names
Name:mdh
OrganismAquaspirillum arcticum
Taxonomic identifier87645 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesOxalobacteraceae

Protein attributes

Sequence length329 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the reversible oxidation of malate to oxaloacetate By similarity. HAMAP-Rule MF_01517

Catalytic activity

(S)-malate + NAD+ = oxaloacetate + NADH. HAMAP-Rule MF_01517

Subunit structure

Homodimer. Ref.1

Sequence similarities

Belongs to the LDH/MDH superfamily. MDH type 2 family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.1
Chain2 – 329328Malate dehydrogenase HAMAP-Rule MF_01517
PRO_0000113346

Regions

Nucleotide binding12 – 187NAD HAMAP-Rule MF_01517
Nucleotide binding132 – 1343NAD HAMAP-Rule MF_01517

Sites

Active site1901Proton acceptor
Binding site951Substrate By similarity
Binding site1011Substrate By similarity
Binding site1081NAD By similarity
Binding site1151NAD
Binding site1341Substrate By similarity
Binding site1651Substrate

Secondary structure

......................................................... 329
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9ZF99 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: F02E2826E5028F27

FASTA32935,251
        10         20         30         40         50         60 
MAKTPMRVAV TGAAGQICYS LLFRIANGDM LGKDQPVILQ LLEIPNEKAQ KALQGVMMEI 

        70         80         90        100        110        120 
DDCAFPLLAG MTAHADPMTA FKDADVALLV GARPRGPGME RKDLLEANAQ IFTVQGKAID 

       130        140        150        160        170        180 
AVASRNIKVL VVGNPANTNA YIAMKSAPSL PAKNFTAMLR LDHNRALSQI AAKTGKPVSS 

       190        200        210        220        230        240 
IEKLFVWGNH SPTMYADYRY AQIDGASVKD MINDDAWNRD TFLPTVGKRG AAIIDARGVS 

       250        260        270        280        290        300 
SAASAANAAI DHIHDWVLGT AGKWTTMGIP SDGSYGIPEG VIFGFPVTTE NGEYKIVQGL 

       310        320 
SIDAFSQERI NVTLNELLEE QNGVQHLLG 

« Hide

References

[1]"Structural basis for cold adaptation. Sequence, biochemical properties, and crystal structure of malate dehydrogenase from a psychrophile Aquaspirillium arcticum."
Kim S.-Y., Hwang K.Y., Kim S.-H., Sung H.-C., Han Y.S., Cho Y.
J. Biol. Chem. 274:11761-11767(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-22 AND 103-123, X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH NAD AND SUBSTRATE ANALOG, SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF109682 Genomic DNA. Translation: AAD13225.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1B8PX-ray1.90A1-329[»]
1B8UX-ray2.50A1-329[»]
1B8VX-ray2.10A1-329[»]
ProteinModelPortalQ9ZF99.
SMRQ9ZF99. Positions 3-329.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKQ9ZF99.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
3.90.110.10. 1 hit.
HAMAPMF_01517. Malate_dehydrog_2.
InterProIPR001557. L-lactate/malate_DH.
IPR022383. Lactate/malate_DH_C.
IPR001236. Lactate/malate_DH_N.
IPR015955. Lactate_DH/Glyco_Ohase_4_C.
IPR010945. Malate_DH_type2.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERPTHR23382. PTHR23382. 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.
TIGRFAMsTIGR01759. MalateDH-SF1. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ9ZF99.

Entry information

Entry nameMDH_AQUAR
AccessionPrimary (citable) accession number: Q9ZF99
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 23, 2007
Last modified: February 19, 2014
This is version 95 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references