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UniProtKB/Swiss-Prot entry Q60176


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

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Entry information
Entry name MDH_METJA
Primary accession number Q60176
Secondary accession numbers None
Integrated into Swiss-Prot on November 1, 1997
Sequence was last modified on November 1, 1997 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 74)
Name and origin of the protein
Protein name Malate dehydrogenase
Synonyms EC 1.1.1.37
EC 1.1.1.82
Gene name
Name: mdh
Synonyms: mdhB
OrderedLocusNames: MJ0490
From
Methanocaldococcus jannaschii (Methanococcus jannaschii) [TaxID: 2190] [HAMAP proteome]
Taxonomy Archaea; Euryarchaeota; Methanococci; Methanococcales; Methanocaldococcaceae; Methanocaldococcus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
PubMed=8688087 [NCBI, ExPASy, EBI, Israel, Japan]
Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
"Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.";
Science 273:1058-1073(1996).
[2]
FUNCTION.
DOI=10.1128/JB.182.13.3688-3692.2000; PubMed=10850983 [NCBI, ExPASy, EBI, Israel, Japan]
Graupner M., Xu H., White R.H.;
"Identification of an archaeal 2-hydroxy acid dehydrogenase catalyzing reactions involved in coenzyme biosynthesis in methanoarchaea.";
J. Bacteriol. 182:3688-3692(2000).
[3]
FUNCTION.
PubMed=10998181 [NCBI, ExPASy, EBI, Israel, Japan]
Madern D.;
"The putative L-lactate dehydrogenase from Methanococcus jannaschii is an NADPH-dependent L-malate dehydrogenase.";
Mol. Microbiol. 37:1515-1520(2000).
[4]
SUBUNIT.
DOI=10.1021/bi010168c; PubMed=11513609 [NCBI, ExPASy, EBI, Israel, Japan]
Madern D., Ebel C., Dale H.A., Lien T., Steen I.H., Birkeland N.-K., Zaccai G.;
"Differences in the oligomeric states of the LDH-like L-MalDH from the hyperthermophilic archaea Methanococcus jannaschii and Archaeoglobus fulgidus.";
Biochemistry 40:10310-10316(2001).
[5]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH NADP, AND SUBUNIT.
DOI=10.1006/jmbi.2001.4532; PubMed=11292347 [NCBI, ExPASy, EBI, Israel, Japan]
Lee B.I., Chang C., Cho S.-J., Eom S.H., Kim K.K., Yu Y.G., Suh S.W.;
"Crystal structure of the MJ0490 gene product of the hyperthermophilic archaebacterium Methanococcus jannaschii, a novel member of the lactate/malate family of dehydrogenases.";
J. Mol. Biol. 307:1351-1362(2001).
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
L77117; AAB98481.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR B64361; B64361.
RefSeq NP_247466.1; -.
3D structure databases
PDB
1HYE; X-ray; 1.90 A; A=1-313.[ExPASy / RCSB / EBI]
1HYG; X-ray; 2.80 A; A/B=1-313.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1HYE; -.
1HYG; -.
ModBase Q60176.
Enzyme and pathway databases
BioCyc MJAN243232:MJ_0490-MON; -.
Ontologies
GO
GO:0030060; Molecular function: L-malate dehydrogenase activity (inferred from electronic annotation from HAMAP).
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.
BLOCKS Q60176.
Genome annotation databases
GeneID 1451352; -.
GenomeReviews L77117_GR; MJ0490.
KEGG mja:MJ0490; -.
NMPDR fig|243232.1.peg.503; -.
TIGR MJ0490; -.
Phylogenomic databases
HOGENOM Q60176; -.
Other
ProtoNet Q60176.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Complete proteome; Cytoplasm; NAD; NADP; Oxidoreductase; Tricarboxylic acid cycle.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   313  313     Malate dehydrogenase. PRO_0000113485
NP_BIND   7    13  7     NADP. 
NP_BIND   34    37  4     NADP. 
NP_BIND   121   123  3     NADP. 
ACT_SITE   178   178        Proton acceptor (By similarity). 
BINDING   86    86        Substrate (By similarity). 
BINDING   92    92        Substrate (By similarity). 
BINDING   99    99        NADP. 
BINDING   123   123        Substrate (By similarity). 
BINDING   154   154        Substrate (By similarity). 
STRAND   2     6  5      
TURN   7     9  3      
HELIX   11    21  11      
STRAND   28    33  6      
HELIX   35    37  3      
HELIX   38    52  15      
STRAND   60    65  6      
HELIX   69    72  4      
STRAND   76    80  5      
HELIX   92   113  22      
STRAND   117   120  4      
STRAND   122   124  3      
HELIX   125   136  12      
STRAND   142   145  4      
HELIX   149   163  15      
HELIX   167   169  3      
STRAND   174   176  3      
STRAND   182   184  3      
HELIX   186   188  3      
HELIX   196   198  3      
HELIX   200   204  5      
HELIX   207   217  11      
HELIX   232   244  13      
STRAND   249   263  15      
STRAND   265   276  12      
STRAND   279   283  5      
HELIX   290   310  21      
Sequence information
Length: 313 AA [This is the length of the unprocessed precursor] Molecular weight: 34609 Da [This is the MW of the unprocessed precursor] CRC64: A7C0DB67C50151CC [This is a checksum on the sequence]
        10         20         30         40         50         60 
MKVTIIGASG RVGSATALLL AKEPFMKDLV LIGREHSINK LEGLREDIYD ALAGTRSDAN 

        70         80         90        100        110        120 
IYVESDENLR IIDESDVVII TSGVPRKEGM SRMDLAKTNA KIVGKYAKKI AEICDTKIFV 

       130        140        150        160        170        180 
ITNPVDVMTY KALVDSKFER NQVFGLGTHL DSLRFKVAIA KFFGVHIDEV RTRIIGEHGD 

       190        200        210        220        230        240 
SMVPLLSATS IGGIPIQKFE RFKELPIDEI IEDVKTKGEQ IIRLKGGSEF GPAAAILNVV 

       250        260        270        280        290        300 
RCIVNNEKRL LTLSAYVDGE FDGIRDVCIG VPVKIGRDGI EEVVSIELDK DEIIAFRKSA 

       310 
EIIKKYCEEV KNL 

Q60176 in FASTA format

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