Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

C3PN92 (MDH_RICAE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 37. 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:RAF_ORF0481
OrganismRickettsia africae (strain ESF-5) [Complete proteome] [HAMAP]
Taxonomic identifier347255 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesRickettsiaceaeRickettsieaeRickettsiaspotted fever group

Protein attributes

Sequence length314 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 – 314314Malate dehydrogenase HAMAP-Rule MF_00487
PRO_1000206445

Regions

Nucleotide binding11 – 166NAD By similarity
Nucleotide binding120 – 1223NAD By similarity

Sites

Active site1771Proton acceptor By similarity
Binding site351NAD By similarity
Binding site841Substrate By similarity
Binding site901Substrate By similarity
Binding site971NAD By similarity
Binding site1221Substrate By similarity
Binding site1531Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
C3PN92 [UniParc].

Last modified June 16, 2009. Version 1.
Checksum: D3F66A98E3A00418

FASTA31433,653
        10         20         30         40         50         60 
MKQNPKISLI GSGNIGGTLA HLISLRELGD IVLFDVTEGV PQGKALDLMQ AGTIAGSDIN 

        70         80         90        100        110        120 
IKGTNDYKDI EGSDAIIITA GLPRKPGMSR EDLISINTGI MKTVAANVKK YAPDAFVIVI 

       130        140        150        160        170        180 
TNPLDVMVYV MLKESGLPHN KVIGMAGVLD SSRFNLFLAE EFKVSVSNVN SMVLGGHGDA 

       190        200        210        220        230        240 
MVPLARYSTI SGVPIPDLIK MGLSSNENIE KIIDRTRNGG GEIVALLKTG SAYYAPAASA 

       250        260        270        280        290        300 
IEMLESYLKD KRQILTCAAH LQGEYGVHDL YVGVPIMIGK EGVLRVIELQ LTTEEKALFD 

       310 
KSVEGVKKLI ETIK 

« Hide

References

[1]"Analysis of the Rickettsia africae genome reveals that virulence acquisition in Rickettsia species may be explained by genome reduction."
Fournier P.-E., El Karkouri K., Leroy Q., Robert C., Giumelli B., Renesto P., Socolovschi C., Parola P., Audic S., Raoult D.
BMC Genomics 10:166-166(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ESF-5.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001612 Genomic DNA. Translation: ACP53402.1.
RefSeqYP_002845145.1. NC_012633.1.

3D structure databases

ProteinModelPortalC3PN92.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING347255.RAF_ORF0481.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACP53402; ACP53402; RAF_ORF0481.
GeneID7815545.
KEGGraf:RAF_ORF0481.
PATRIC17872891. VBIRicAfr6986_0583.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0039.
HOGENOMHOG000213794.
KOK00024.
OMAYGQNDIC.
OrthoDBEOG6091FG.

Enzyme and pathway databases

BioCycRAFR347255:GJCT-451-MONOMER.

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_RICAE
AccessionPrimary (citable) accession number: C3PN92
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: June 16, 2009
Last modified: May 14, 2014
This is version 37 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