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UniProtKB/Swiss-Prot entry O08349


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

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Entry information
Entry name MDH_ARCFU
Primary accession number O08349
Secondary accession numbers None
Integrated into Swiss-Prot on May 30, 2000
Sequence was last modified on July 1, 1997 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 81)
Name and origin of the protein
Protein name Malate dehydrogenase
Synonym EC 1.1.1.37
Gene name
Name: mdh
OrderedLocusNames: AF_0855
From
Archaeoglobus fulgidus [TaxID: 2234] [HAMAP proteome]
Taxonomy Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae; Archaeoglobus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
DOI=10.1007/s002030050470; PubMed=9211715 [NCBI, ExPASy, EBI, Israel, Japan]
Langelandsvik A.S., Steen I.H., Birkeland N.K., Lien T.;
"Properties and primary structure of a thermostable L-malate dehydrogenase from Archaeoglobus fulgidus.";
Arch. Microbiol. 168:59-67(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126;
DOI=10.1038/37052; PubMed=9389475 [NCBI, ExPASy, EBI, Israel, Japan]
Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A., Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L., Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D., Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F., Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N., Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R., Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D., Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P., Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
"The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.";
Nature 390:364-370(1997).
[3]
X-RAY CRYSTALLOGRAPHY (2.79 ANGSTROMS) IN COMPLEX WITH NAD, AND SUBUNIT.
DOI=10.1016/j.jmb.2003.10.054; PubMed=14659762 [NCBI, ExPASy, EBI, Israel, Japan]
Irimia A., Vellieux F.M.D., Madern D., Zaccai G., Karshikoff A., Tibbelin G., Ladenstein R., Lien T., Birkeland N.-K.;
"The 2.9A resolution crystal structure of malate dehydrogenase from Archaeoglobus fulgidus: mechanisms of oligomerisation and thermal stabilisation.";
J. Mol. Biol. 335:343-356(2004).
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
Z85985; CAB06654.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AE000782; AAB90384.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR G69356; G69356.
RefSeq NP_069689.1; -.
3D structure databases
PDB
1OJS; X-ray; 2.91 A; A=1-294.[ExPASy / RCSB / EBI]
1OJU; X-ray; 2.79 A; A=1-294.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1OJS; -.
1OJU; -.
ModBase O08349.
Enzyme and pathway databases
BioCyc AFUL224325:AF_0855-MON; -.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
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.
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 1484074; -.
GenomeReviews AE000782_GR; AF_0855.
KEGG afu:AF0855; -.
NMPDR fig|224325.1.peg.848; -.
TIGR AF_0855; -.
Phylogenomic databases
HOGENOM O08349; -.
Other
ProtoNet O08349.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Complete proteome; Cytoplasm; NAD; Oxidoreductase; Tricarboxylic acid cycle.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   294  294     Malate dehydrogenase. PRO_0000113480
NP_BIND   7    12  6     NAD. 
NP_BIND   117   119  3     NAD. 
ACT_SITE   172   172        Proton acceptor. 
BINDING   32    32        NAD. 
BINDING   81    81        Substrate (By similarity). 
BINDING   87    87        Substrate (By similarity). 
BINDING   94    94        NAD. 
BINDING   119   119        Substrate (By similarity). 
BINDING   150   150        Substrate (By similarity). 
STRAND   2     6  5      
HELIX   10    22  13      
STRAND   26    31  6      
HELIX   35    50  16      
TURN   51    53  3      
STRAND   57    62  6      
HELIX   64    67  4      
STRAND   71    75  5      
HELIX   87   106  20      
STRAND   113   116  4      
STRAND   118   120  3      
HELIX   121   131  11      
STRAND   138   141  4      
HELIX   144   157  14      
STRAND   168   173  6      
HELIX   180   182  3      
HELIX   191   209  19      
HELIX   214   228  15      
STRAND   234   243  10      
HELIX   244   246  3      
STRAND   248   259  12      
STRAND   262   265  4      
HELIX   272   290  19      
TURN   291   293  3      
Sequence information
Length: 294 AA [This is the length of the unprocessed precursor] Molecular weight: 31874 Da [This is the MW of the unprocessed precursor] CRC64: 90389DBC189B944F [This is a checksum on the sequence]
        10         20         30         40         50         60 
MKLGFVGAGR VGSTSAFTCL LNLDVDEIAL VDIAEDLAVG EAMDLAHAAA GIDKYPKIVG 

        70         80         90        100        110        120 
GADYSLLKGS EIIVVTAGLA RKPGMTRLDL AHKNAGIIKD IAKKIVENAP ESKILVVTNP 

       130        140        150        160        170        180 
MDVMTYIMWK ESGKPRNEVF GMGNQLDSQR LKERLYNAGA RNIRRAWIIG EHGDSMFVAK 

       190        200        210        220        230        240 
SLADFDGEVD WEAVENDVRF VAAEVIKRKG ATIFGPAVAI YRMVKAVVED TGEIIPTSMI 

       250        260        270        280        290 
LQGEYGIENV AVGVPAKLGK NGAEVADIKL SDEEIEKLRN SAKILRERLE ELGY 

O08349 in FASTA format

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View entry in raw text format (no links)
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