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

A8GRV2 (MDH_RICRS) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 45. 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:A1G_02950
OrganismRickettsia rickettsii (strain Sheila Smith) [Complete proteome] [HAMAP]
Taxonomic identifier392021 [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_1000026491

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
A8GRV2 [UniParc].

Last modified November 13, 2007. Version 1.
Checksum: 6421EB23A0783113

FASTA31433,714
        10         20         30         40         50         60 
MKQHPKISLI GSGNIGGTLA HLISLRELGN IVLFDVTEGV PQGKALDLMQ AVTIAGSDIK 

        70         80         90        100        110        120 
IKGTNDYKDI KGSDAIIITA GLPRKPGMSR DDLISINTGI 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 KRQILTCAAY LQGEYGVHDL YVGVPIMIGK EGVLKVIELQ LTTEEKALFD 

       310 
KSVEGVKKLI ETIK 

« Hide

References

[1]"Complete genome sequence of Rickettsia rickettsii."
Madan A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A., Dasch G., Eremeeva M.
Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Sheila Smith.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000848 Genomic DNA. Translation: ABV76127.1.
RefSeqYP_001494635.1. NC_009882.1.

3D structure databases

ProteinModelPortalA8GRV2.
SMRA8GRV2. Positions 1-314.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING392021.A1G_02950.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABV76127; ABV76127; A1G_02950.
GeneID5648234.
KEGGrri:A1G_02950.
PATRIC17903911. VBIRicRic5337_0619.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0039.
HOGENOMHOG000213794.
KOK00024.
OMAGANSYEA.
OrthoDBEOG6091FG.
ProtClustDBPRK06223.

Enzyme and pathway databases

BioCycRRIC392021:GIY1-542-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_RICRS
AccessionPrimary (citable) accession number: A8GRV2
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: November 13, 2007
Last modified: February 19, 2014
This is version 45 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