ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry O67581

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name MDH2_AQUAE
Primary accession number O67581
Secondary accession numbers None
Integrated into Swiss-Prot on August 16, 2004
Sequence was last modified on August 1, 1998 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 51)
Name and origin of the protein
Protein name Malate dehydrogenase 2
Synonym EC 1.1.1.37
Gene name
Name: mdh2
OrderedLocusNames: aq_1665
From
Aquifex aeolicus [TaxID: 63363] [HAMAP proteome]
Taxonomy Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=VF5;
DOI=10.1038/32831; PubMed=9537320 [NCBI, ExPASy, EBI, Israel, Japan]
Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L., Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R., Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
"The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
Nature 392:353-358(1998).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AE000657; AAC07547.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR D70444; D70444.
RefSeq NP_214147.1; -.
3D structure databases
HSSP P80039; 1GV0. [HSSP ENTRY / PDB]
ModBase O67581.
Enzyme and pathway databases
BioCyc AAEO224324:AQ_1665-MON; -.
Ontologies
GO
GO:0005488; Molecular function: binding (inferred from electronic annotation from InterPro).
GO:0030060; Molecular function: L-malate dehydrogenase activity (inferred from electronic annotation from HAMAP).
GO:0006096; Biological process: glycolysis (inferred from electronic annotation from InterPro).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0006099; Biological process: tricarboxylic acid cycle (inferred from electronic annotation from HAMAP).
QuickGo view.
Family and domain databases
HAMAP MF_00487; -; 1.
PBIL [Tree]
InterPro IPR001557; L-lactate/malate_DHase.
IPR001236; Lactate/malate_DHase.
IPR015955; Lactate_DHase/Glyco_Ohase_4_C.
IPR001252; Malate_DHase_AS.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.
Gene3D G3DSA:3.90.110.10; lact_mal_DH; 1.
G3DSA:3.40.50.720; NAD(P)-bd; 1.
Pfam PF02866; Ldh_1_C; 1.
PF00056; Ldh_1_N; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000102; Lac_mal_DH; 1.
PRINTS PR00086; LLDHDRGNASE.
Genome annotation databases
GeneID 1193297; -.
GenomeReviews AE000657_GR; aq_1665.
KEGG aae:aq_1665; -.
NMPDR fig|224324.1.peg.1162; -.
Phylogenomic databases
HOGENOM O67581; -.
Genome annotation databases
CMR O67581; aq_1665.
Other
ProtoNet O67581.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; NAD; Oxidoreductase; Tricarboxylic acid cycle.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   334  334     Malate dehydrogenase 2. PRO_0000113423
NP_BIND   20    25  6     NAD (By similarity). 
NP_BIND   136   138  3     NAD (By similarity). 
ACT_SITE   193   193        Proton acceptor (By similarity). 
BINDING   100   100        Substrate (By similarity). 
BINDING   106   106        Substrate (By similarity). 
BINDING   113   113        NAD (By similarity). 
BINDING   138   138        Substrate (By similarity). 
BINDING   169   169        Substrate (By similarity). 
Sequence information
Length: 334 AA [This is the length of the unprocessed precursor] Molecular weight: 36698 Da [This is the MW of the unprocessed precursor] CRC64: 18E64807D16B7C96 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MKGKLINSFL MKKPKISVIG AGKVGENVAY LLTILGLGDV YLFARYKKGL EPAKAKALDL 

        70         80         90        100        110        120 
KQMAVLMDID INVKGISYDK EGFEELKGSD IVVITAGIPR REGMSREDLL YENLKILKKF 

       130        140        150        160        170        180 
TDAIKEYAKD SIIIVVSNPV DTLTYATIKL TGFEPRRVIG MAGVLDSARF KNFVKEKIGI 

       190        200        210        220        230        240 
SNADIRTLVL GTHGDLMVPV TSHSFIGDKP IEEVFSASEI DELIEKTRKG GAQIVSLMGT 

       250        260        270        280        290        300 
SAYYAPAASV VIMVESIIND RKRVMPCSVY VEGEAAKHYE IEGVCIGLPV VLGKKGVEDF 

       310        320        330 
ELVNLSGYEK RELLRSAKTL KEMVSLADKL LNEL
O67581 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA) 		Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Hosted by kr flag YPRC Korea Mirror sites: Australia Brazil Canada China Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!