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UniProtKB/Swiss-Prot entry Q9YEA1

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

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Entry information
Entry name MDH_AERPE
Primary accession number Q9YEA1
Secondary accession numbers None
Integrated into Swiss-Prot on May 30, 2000
Sequence was last modified on June 26, 2007 (Sequence version 2)
Annotations were last modified on    July 22, 2008 (Entry version 63)
Name and origin of the protein
Protein name Malate dehydrogenase
Synonym EC 1.1.1.37
Gene name
Name: mdh
OrderedLocusNames: APE_0672.1
From
Aeropyrum pernix [TaxID: 56636] [HAMAP proteome]
Taxonomy Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales; Desulfurococcaceae; Aeropyrum.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K1;
DOI=10.1093/dnares/6.2.83; PubMed=10382966 [NCBI, ExPASy, EBI, Israel, Japan]
Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K., Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S., Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Kubota K., Nakamura Y., Nomura N., Sako Y., Kikuchi H.;
"Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon, Aeropyrum pernix K1.";
DNA Res. 6:83-101(1999).
[2]
 X-RAY CRYSTALLOGRAPHY (2.87 ANGSTROMS) OF 2-308, AND SUBUNIT.
Kawakami R., Sakuraba H., Tsuge H., Ohshima T.;
"Crystal structure of the malate dehydrogenase from hyperthermophilic archaeon Aeropyrum pernix.";
Submitted (NOV-2006) to the PDB data bank.
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
BA000002; BAA79645.2; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR E72655; E72655.
RefSeq NP_147405.2; -.
3D structure databases
PDB
2D4A; X-ray; 2.87 A; A/D=2-308, B/C=1-308.[ExPASy / RCSB / EBI]
PDBsum 2D4A; -.
SMR Q9YEA1; 6-313.
ModBase Q9YEA1.
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.
IPR011304; L-lactate_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.
BLOCKS Q9YEA1.
Genome annotation databases
GeneID 1444806; -.
GenomeReviews BA000002_GR; APE_0672.1.
KEGG ape:APE_0672.1; -.
NMPDR fig|272557.1.peg.513; -.
Phylogenomic databases
HOGENOM Q9YEA1; -.
Genome annotation databases
CMR Q9YEA1; APE_0672.1.
Other
ProtoNet Q9YEA1.
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   308  308     Malate dehydrogenase. PRO_0000113479
NP_BIND   6    11  6     NAD (By similarity). 
NP_BIND   115   117  3     NAD (By similarity). 
ACT_SITE   172   172        Proton acceptor (By similarity). 
BINDING   79    79        Substrate (By similarity). 
BINDING   85    85        Substrate (By similarity). 
BINDING   92    92        NAD (By similarity). 
BINDING   117   117        Substrate (By similarity). 
BINDING   148   148        Substrate (By similarity). 
STRAND   2     5  4      
HELIX   9    21  13      
STRAND   26    29  4      
STRAND   31    34  4      
HELIX   35    50  16      
STRAND   56    60  5      
HELIX   62    65  4      
STRAND   69    73  5      
HELIX   89   106  18      
STRAND   111   114  4      
STRAND   116   118  3      
HELIX   119   130  12      
HELIX   134   136  3      
STRAND   137   139  3      
HELIX   142   157  16      
HELIX   161   163  3      
STRAND   164   170  7      
STRAND   177   185  9      
HELIX   190   193  4      
HELIX   196   207  12      
HELIX   209   217  9      
HELIX   223   237  15      
STRAND   242   252  11      
HELIX   253   255  3      
STRAND   257   268  12      
STRAND   271   275  5      
HELIX   282   300  19      
HELIX   304   307  4      
Sequence information
Length: 308 AA [This is the length of the unprocessed precursor] Molecular weight: 33490 Da [This is the MW of the unprocessed precursor] CRC64: C2A14F224650B8CE [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MITILGAGKV GMATAVMLMM RGYDDLLLIA RTPGKPQGEA LDLAHAAAEL GVDIRISGSN 

        70         80         90        100        110        120 
SYEDMRGSDI VLVTAGIGRK PGMTREQLLE ANANTMADLA EKIKAYAKDA IVVITTNPVD 

       130        140        150        160        170        180 
AMTYVMYKKT GFPRERVIGF SGILDSARMA YYISQKLGVS FKSVNAIVLG MHGQKMFPVP 

       190        200        210        220        230        240 
RLSSVGGVPL EHLMSKEEIE EVVSETVNAG AKITELRGYS SNYGPAAGLV LTVEAIKRDS 

       250        260        270        280        290        300 
KRIYPYSLYL QGEYGYNDIV AEVPAVIGKS GIERIIELPL TEDEKRKFDE AVQAVKKLVE 


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Q9YEA1 in FASTA format

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