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Q4FQU7 (MDH_PSYA2) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 62. 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

EC=1.1.1.37
Gene names
Name:mdh
Ordered Locus Names:Psyc_1763
OrganismPsychrobacter arcticus (strain DSM 17307 / 273-4) [Complete proteome] [HAMAP]
Taxonomic identifier259536 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaePsychrobacter

Protein attributes

Sequence length329 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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 By similarity. HAMAP-Rule MF_01517

Sequence similarities

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

Ontologies

Keywords
   Biological processTricarboxylic acid cycle
   LigandNAD
   Molecular functionOxidoreductase
   Technical termComplete proteome
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-HAMAP

   Molecular_functionL-malate dehydrogenase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 329329Malate dehydrogenase HAMAP-Rule MF_01517
PRO_0000113389

Regions

Nucleotide binding13 – 197NAD By similarity
Nucleotide binding131 – 1333NAD By similarity

Sites

Active site1891Proton acceptor By similarity
Binding site941Substrate By similarity
Binding site1001Substrate By similarity
Binding site1071NAD By similarity
Binding site1141NAD By similarity
Binding site1331Substrate By similarity
Binding site1641Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q4FQU7 [UniParc].

Last modified August 30, 2005. Version 1.
Checksum: 57C35528006AD4D9

FASTA32935,235
        10         20         30         40         50         60 
MSMKQPVRVA VTGAAGNISY AMLFRIASGE MLGKDQPVIL QLLEIAPALD ALKGVVMELE 

        70         80         90        100        110        120 
DCAFPLLAGI VQTDDATVAF KDVDYALLVG SRPRGPGMER KDLLEANAAI FSAQGKALND 

       130        140        150        160        170        180 
VASRDVKVLV VGNPANTNAL IAQRNAPDLD PRNFTAMTRL DHNRAMAQLA GKTDSTVNDV 

       190        200        210        220        230        240 
KKMIIWGNHS STQYPDLTAS TVNGKLALDL VDRTWYEGTY IPEVQQRGAA IIKARGASSA 

       250        260        270        280        290        300 
ASAANAAIAH MRTWVLGTDE NDWVSMGVYS NGEYGIAKGL IYSFPCTCTN GDWSIVDGVD 

       310        320 
VSSAFSKEKM AATEQELSEE RDAVAHLLP 

« Hide

References

[1]"The genome sequence of Psychrobacter arcticus 273-4, a psychroactive Siberian permafrost bacterium, reveals mechanisms for adaptation to low-temperature growth."
Ayala-del-Rio H.L., Chain P.S., Grzymski J.J., Ponder M.A., Ivanova N., Bergholz P.W., Di Bartolo G., Hauser L., Land M., Bakermans C., Rodrigues D., Klappenbach J., Zarka D., Larimer F., Richardson P., Murray A., Thomashow M., Tiedje J.M.
Appl. Environ. Microbiol. 76:2304-2312(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 17307 / 273-4.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000082 Genomic DNA. Translation: AAZ19611.1.
RefSeqYP_265045.1. NC_007204.1.

3D structure databases

ProteinModelPortalQ4FQU7.
SMRQ4FQU7. Positions 3-327.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING259536.Psyc_1763.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAZ19611; AAZ19611; Psyc_1763.
GeneID3515731.
KEGGpar:Psyc_1763.
PATRIC23058341. VBIPsyArc98534_2077.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0039.
HOGENOMHOG000220953.
KOK00024.
OMANCLIASK.
OrthoDBEOG6PP9Q2.
ProtClustDBPRK05442.

Enzyme and pathway databases

BioCycPARC259536:GI3A-1806-MONOMER.

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.
IPR001252. Malate_DH_AS.
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.
PROSITEPS00068. MDH. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMDH_PSYA2
AccessionPrimary (citable) accession number: Q4FQU7
Entry history
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: August 30, 2005
Last modified: February 19, 2014
This is version 62 of the entry and version 1 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