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B2UKY5 (MDH_AKKM8) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 46. 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:Amuc_1436
OrganismAkkermansia muciniphila (strain ATCC BAA-835) [Complete proteome] [HAMAP]
Taxonomic identifier349741 [NCBI]
Taxonomic lineageBacteriaVerrucomicrobiaVerrucomicrobiaeVerrucomicrobialesVerrucomicrobiaceaeAkkermansia

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_1000191608

Regions

Nucleotide binding11 – 177NAD By similarity
Nucleotide binding129 – 1313NAD By similarity

Sites

Active site1871Proton acceptor By similarity
Binding site921Substrate By similarity
Binding site981Substrate By similarity
Binding site1051NAD By similarity
Binding site1121NAD By similarity
Binding site1311Substrate By similarity
Binding site1621Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
B2UKY5 [UniParc].

Last modified July 1, 2008. Version 1.
Checksum: 4B2DFD6D48B6DA04

FASTA32935,097
        10         20         30         40         50         60 
MKTPITVTVT GAAGQIAYSL LFRIASGSML GPDQPINLRL LEIPPAMNAL EGVVMELRDA 

        70         80         90        100        110        120 
AFPLVNEIVP TSDPDEAFAG ANWCLLVGSV PRKAGMERKD LLDINGKVFI GQGQAIARSA 

       130        140        150        160        170        180 
AKDVRVLVVG NPCNTNALIA MHNASGVPSD RFFAMTRLDE NRAKSQLAEK AGVHVTEVTN 

       190        200        210        220        230        240 
MAIWGNHSST QYPDFTNARI GGKPVTEVIK DTEWLKGDFI TTVQQRGAAI IKARGASSAA 

       250        260        270        280        290        300 
SAASAAVDTV RSLATQTPEG DWYSVAVCSD GSYGIEKGLI CSFPVRTTKD GGWEIVQGLP 

       310        320 
VDAFSREKID ATVNELKEER DAVSSLLKH 

« Hide

References

[1]"Complete sequence of Akkermansia muciniphila ATCC BAA-835."
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N. expand/collapse author list , Smidt H., Derrien M., Plugge C.M., Zoetendal E.G., de Vos W.M., Richardson P.
Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-835.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001071 Genomic DNA. Translation: ACD05258.1.
RefSeqYP_001878039.1. NC_010655.1.

3D structure databases

ProteinModelPortalB2UKY5.
SMRB2UKY5. Positions 1-326.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING349741.Amuc_1436.

Proteomic databases

PRIDEB2UKY5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACD05258; ACD05258; Amuc_1436.
GeneID6274593.
KEGGamu:Amuc_1436.
PATRIC20835794. VBIAkkMuc16855_1630.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0039.
HOGENOMHOG000220953.
KOK00024.
OMAAFSQECI.
OrthoDBEOG6PP9Q2.

Enzyme and pathway databases

BioCycAMUC349741:GHZ7-1482-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_AKKM8
AccessionPrimary (citable) accession number: B2UKY5
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: July 1, 2008
Last modified: May 14, 2014
This is version 46 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