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 A4JM71


[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_BURVG
Primary accession number A4JM71
Secondary accession numbers None
Integrated into Swiss-Prot on January 15, 2008
Sequence was last modified on May 1, 2007 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 13)
Name and origin of the protein
Protein name Malate dehydrogenase 2
Synonym EC 1.1.1.37
Gene name
Name: mdh2
OrderedLocusNames: Bcep1808_4408
From
Burkholderia vietnamiensis (strain G4 / LMG 22486) (Burkholderia cepacia (strain R1808)) [TaxID: 269482] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
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., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Tiedje J., Richardson P.;
"Complete sequence of chromosome 2 of Burkholderia vietnamiensis G4.";
Submitted (MAR-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
CP000615; ABO57374.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_001116839.1; -.
3D structure databases
SMR A4JM71; 3-326.
ModBase A4JM71.
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_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.
BLOCKS A4JM71.
Genome annotation databases
GeneID 4950626; -.
GenomeReviews CP000615_GR; Bcep1808_4408.
KEGG bvi:Bcep1808_4408; -.
CMR A4JM71; Bcep1808_4408.
Other
ProtoNet A4JM71.
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   328  328     Malate dehydrogenase 2. PRO_0000315546
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: 328 AA [This is the length of the unprocessed precursor] Molecular weight: 35163 Da [This is the MW of the unprocessed precursor] CRC64: 95C89EFD7DF9265A [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAKPAKRVAV TGAAGQIAYS LLFRIANGDL LGKDQPVILQ LLDLPQAQAA VKGVVMELED 

        70         80         90        100        110        120 
CAFPLLAGVV ITDDPKVAFK DADVALLVGA RPRSKGMERK DLLSANAEIF TVQGAALNEV 

       130        140        150        160        170        180 
ASRDVKVLVV GNPANTNAYI AMKSAPDLPK KNFTAMLRLD HNRALSQLAA KTGKPVASIE 

       190        200        210        220        230        240 
KLAVWGNHSP TMYPDFRFAT AEGESMLKLV NDDVWNRETF IPTVGKRGAA IIEARGLSSA 

       250        260        270        280        290        300 
ASAANAAIDH VRDWVLGTNG KWVTMGIPSD GSYGIPEDII YGVPVTCENG EYKRVEGLEI 

       310        320 
DAFSREKMDG TLAELLEERD GVAHLLKN 

A4JM71 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 ch flag SIB Switzerland Mirror sites: Australia  Brazil  Canada  China  Korea
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!