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Q5PAV3 (MDH_ANAMM) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 64. 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:AM564
OrganismAnaplasma marginale (strain St. Maries) [Complete proteome] [HAMAP]
Taxonomic identifier234826 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesAnaplasmataceaeAnaplasma

Protein attributes

Sequence length317 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the reversible oxidation of malate to oxaloacetate By similarity. HAMAP-Rule MF_00487

Catalytic activity

(S)-malate + NAD+ = oxaloacetate + NADH. HAMAP-Rule MF_00487

Sequence similarities

Belongs to the LDH/MDH superfamily. MDH type 3 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 – 317317Malate dehydrogenase HAMAP-Rule MF_00487
PRO_0000113420

Regions

Nucleotide binding13 – 186NAD By similarity
Nucleotide binding123 – 1253NAD By similarity

Sites

Active site1801Proton acceptor By similarity
Binding site381NAD By similarity
Binding site871Substrate By similarity
Binding site931Substrate By similarity
Binding site1001NAD By similarity
Binding site1251Substrate By similarity
Binding site1561Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5PAV3 [UniParc].

Last modified January 4, 2005. Version 1.
Checksum: 65C4ED86C35C6D0B

FASTA31733,379
        10         20         30         40         50         60 
MRSSRSAKVS LVGAGNIGGA LAHMLGASQV VKELVLVDVA GGMTEGKVLD VGQALALLGS 

        70         80         90        100        110        120 
DVYITGGSDY AAIEHSDAVV VTAGIPRKEG MSREDLLNTN AAVVRNIAEN IAKYSPGALV 

       130        140        150        160        170        180 
IVVTNPLDAM VWCMYKYSGL PANRVVGMAG VLDSARFSFF LARHMNVSVS SVSAMVLGGH 

       190        200        210        220        230        240 
GDLMLPLLRY STVGGVPVES LIESGRLNRD DIAAIVERTR KGGEEIVKLL KTGSAYCAPA 

       250        260        270        280        290        300 
ASCAHMLESY VRDKRSIMPC SAYLDGQYGV RDLFVGVPVI IGEKGVEEVV EFPLTAEEQA 

       310 
VFDQSVELIR GSVSAIS 

« Hide

References

[1]"Complete genome sequencing of Anaplasma marginale reveals that the surface is skewed to two superfamilies of outer membrane proteins."
Brayton K.A., Kappmeyer L.S., Herndon D.R., Dark M.J., Tibbals D.L., Palmer G.H., McGuire T.C., Knowles D.P. Jr.
Proc. Natl. Acad. Sci. U.S.A. 102:844-849(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: St. Maries.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000030 Genomic DNA. Translation: AAV86577.1.
RefSeqYP_153832.1. NC_004842.2.

3D structure databases

ProteinModelPortalQ5PAV3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING234826.AM564.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAV86577; AAV86577; AM564.
GeneID3171816.
KEGGama:AM564.
PATRIC20947151. VBIAnaMar46146_0496.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0039.
HOGENOMHOG000213794.
KOK00024.
OMAFVGVPVI.
OrthoDBEOG6091FG.
ProtClustDBPRK06223.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
3.90.110.10. 1 hit.
HAMAPMF_00487. Malate_dehydrog_3.
InterProIPR001557. L-lactate/malate_DH.
IPR022383. Lactate/malate_DH_C.
IPR001236. Lactate/malate_DH_N.
IPR015955. Lactate_DH/Glyco_Ohase_4_C.
IPR011275. Malate_DH_type3.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERPTHR11540. PTHR11540. 1 hit.
PfamPF02866. Ldh_1_C. 1 hit.
PF00056. Ldh_1_N. 1 hit.
[Graphical view]
PIRSFPIRSF000102. Lac_mal_DH. 1 hit.
PRINTSPR00086. LLDHDRGNASE.
SUPFAMSSF56327. SSF56327. 1 hit.
TIGRFAMsTIGR01763. MalateDH_bact. 1 hit.
ProtoNetSearch...

Entry information

Entry nameMDH_ANAMM
AccessionPrimary (citable) accession number: Q5PAV3
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: January 4, 2005
Last modified: February 19, 2014
This is version 64 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