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 Q21XH1

[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 MDH1_RHOFD
Primary accession number Q21XH1
Secondary accession numbers None
Integrated into Swiss-Prot on July 10, 2007
Sequence was last modified on April 18, 2006 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 20)
Name and origin of the protein
Protein name Malate dehydrogenase 1
Synonym EC 1.1.1.37
Gene name
Name: mdh1
OrderedLocusNames: Rfer_1803
From
Rhodoferax ferrireducens (strain DSM 15236 / ATCC BAA-621 / T118) [TaxID: 338969] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; Comamonadaceae; Rhodoferax.
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., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M., Kyrpides N., Ivanova N., Richardson P.;
"Complete sequence of chromosome of Rhodoferax ferrireducens DSM 15236.";
Submitted (FEB-2006) 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
CP000267; ABD69532.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_523063.1; -.
3D structure databases
SMR Q21XH1; 3-328.
ModBase Q21XH1.
Enzyme and pathway databases
BioCyc RFER338969:RFER_1803-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_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 Q21XH1.
Genome annotation databases
GeneID 3962200; -.
GenomeReviews CP000267_GR; Rfer_1803.
KEGG rfr:Rfer_1803; -.
NMPDR fig|338969.3.peg.2020; -.
Phylogenomic databases
HOGENOM Q21XH1; -.
Genome annotation databases
CMR Q21XH1; Rfer_1803.
Other
ProtoNet Q21XH1.
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
INIT_MET   1     1        Removed (By similarity). 
CHAIN   2   328  327     Malate dehydrogenase 1. PRO_0000294403
NP_BIND   12    18  7     NAD (By similarity). 
NP_BIND   132   134  3     NAD (By similarity). 
ACT_SITE   190   190        Proton acceptor (By similarity). 
BINDING   95    95        Substrate (By similarity). 
BINDING   101   101        Substrate (By similarity). 
BINDING   108   108        NAD (By similarity). 
BINDING   115   115        NAD (By similarity). 
BINDING   134   134        Substrate (By similarity). 
BINDING   165   165        Substrate (By similarity). 
Sequence information
Length: 328 AA [This is the length of the unprocessed precursor] Molecular weight: 35077 Da [This is the MW of the unprocessed precursor] CRC64: 2462BA46D0A8F272 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MSKKPVRVAV TGAAGQIGYA ILFRIASGEM LGKDQPVILQ LLEVPVEKAQ QALQGVMMEL 

        70         80         90        100        110        120 
QDCAFPLLAG MEAHSDPMTA FKDVDYALLI GSRPRGPGME RAELLAVNGA IFTAQGKALN 

       130        140        150        160        170        180 
AVASRNVKVL VVGNPANTNA YIAMKSAPDL PAKNFTAMLR LDHNRALSQL ASKTGKAVAD 

       190        200        210        220        230        240 
IEKMAVWGNH SPTMYADYRF ATINGESVKD MINDQDWNAN TFLPTVGKRG AAIIAARGVS 

       250        260        270        280        290        300 
SAASAANAAI DHMRDWALGT NGKWVTMGIP SDGQYGIPKE TMFGFPVTCE GGEYKVVQNL 

       310        320 
PIDAFSQECI NKTLKELQDE QAGVAHLL
Q21XH1 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!