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UniProtKB/Swiss-Prot entry A5G320

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

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Entry information
Entry name MDH_ACICJ
Primary accession number A5G320
Secondary accession numbers None
Integrated into Swiss-Prot on February 5, 2008
Sequence was last modified on June 12, 2007 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 15)
Name and origin of the protein
Protein name Malate dehydrogenase
Synonym EC 1.1.1.37
Gene name
Name: mdh
OrderedLocusNames: Acry_3063
From
Acidiphilium cryptum (strain JF-5) [TaxID: 349163] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; Acetobacteraceae; Acidiphilium.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Magnuson T., Richardson P.;
"Complete sequence of chromosome of Acidiphilium cryptum JF-5.";
Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
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
CP000697; ABQ32252.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_001236171.1; -.
3D structure databases
ModBase A5G320.
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:0006108; Biological process: malate metabolic process (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_01517; -; 1.
PBIL [Tree]
InterPro IPR001557; L-lactate/malate_DHase.
IPR001236; Lactate/malate_DHase.
IPR015955; Lactate_DHase/Glyco_Ohase_4_C.
IPR001252; Malate_DHase_AS.
IPR010945; Malate_DHase_SF1.
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.
PANTHER PTHR23382; MDH_SF1; 1.
Pfam PF02866; Ldh_1_C; 1.
PF00056; Ldh_1_N; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000102; Lac_mal_DH; 1.
ProDom PD003052; Mal_dehydrog; 1.
[Domain structure / List of seq. sharing at least 1 domain]
TIGRFAMs TIGR01759; MalateDH-SF1; 1.
PROSITE PS00068; MDH; FALSE_NEG.
Genome annotation databases
GeneID 5161153; -.
GenomeReviews CP000697_GR; Acry_3063.
KEGG acr:Acry_3063; -.
CMR A5G320; Acry_3063.
Other
ProtoNet A5G320.
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   327  327     Malate dehydrogenase. PRO_1000068598
NP_BIND   12    18  7     NAD (By similarity). 
NP_BIND   130   132  3     NAD (By similarity). 
ACT_SITE   188   188        Proton acceptor (By similarity). 
BINDING   93    93        Substrate (By similarity). 
BINDING   99    99        Substrate (By similarity). 
BINDING   106   106        NAD (By similarity). 
BINDING   113   113        NAD (By similarity). 
BINDING   132   132        Substrate (By similarity). 
BINDING   163   163        Substrate (By similarity). 
Sequence information
Length: 327 AA [This is the length of the unprocessed precursor] Molecular weight: 34474 Da [This is the MW of the unprocessed precursor] CRC64: F60BC6BF6DD37EFB [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MAKSPVRIAV TGAAGQIAYA LVFRIASGAL LGPDQPVILH LLDLPQMQGA LGGVMMELED 

        70         80         90        100        110        120 
CAFPLLAGMV ATDDPKVAFK DIDIGFLVGA RPRGKGMERK DLLGANAEIF TVQGRALNEV 

       130        140        150        160        170        180 
AKRSARVLVV GNPANTNAYI AMKSAPDLSP DCFSAMIRLD HNRAASMLAA KAGVNVGDVG 

       190        200        210        220        230        240 
KLIVWGNHSP TMYPDYRFAE AGGRKLAEAI NDEAWNRDVF IPTVGKRGAA VIEARGASSA 

       250        260        270        280        290        300 
ASAANAAIDQ VRDWVVGSDG RWVSMAIPSD GSYGIPEGIM FGVPVTTQGG VVTRVPNLAI 

       310        320 
DAFAQSRLDI TLNELKEERE AIAHLLA
A5G320 in FASTA format

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