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UniProtKB/Swiss-Prot entry Q02QW0


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

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Entry information
Entry name MAO1_PSEAB
Primary accession number Q02QW0
Secondary accession numbers None
Integrated into Swiss-Prot on February 5, 2008
Sequence was last modified on November 14, 2006 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 21)
Name and origin of the protein
Protein name NAD-dependent malic enzyme
Synonyms NAD-ME
EC 1.1.1.38
Gene name
Name: sfcA
OrderedLocusNames: PA14_19190
From
Pseudomonas aeruginosa (strain UCBPP-PA14) [TaxID: 208963] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; Pseudomonadaceae; Pseudomonas.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1186/gb-2006-7-10-r90; PubMed=17038190 [NCBI, ExPASy, EBI, Israel, Japan]
Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S., Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L., Grills G., Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.;
"Genomic analysis reveals that Pseudomonas aeruginosa virulence is combinatorial.";
Genome Biol. 7:RESEARCH90.1-RESEARCH90.14(2006).
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
CP000438; ABJ12726.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_789676.1; -.
3D structure databases
ModBase Q02QW0.
Ontologies
GO
GO:0016619; Molecular function: malate dehydrogenase (oxaloacetate-decarboxylating) activity (inferred from electronic annotation from HAMAP).
GO:0046872; Molecular function: metal ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0051287; Molecular function: NAD binding (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).
QuickGo view.
Family and domain databases
HAMAP MF_01619; -; 1.
PBIL [Tree]
InterPro IPR015884; Malic_enzyme_CS.
IPR012301; Malic_N.
IPR012302; Malic_NAD_bd.
IPR001891; Malic_OxRdtase.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.720; NAD(P)-bd; 1.
Pfam PF00390; malic; 1.
PF03949; Malic_M; 1.
Pfam graphical view of domain structure.
PRINTS PR00072; MALOXRDTASE.
PROSITE PS00331; MALIC_ENZYMES; 1.
ProtoNet Q02QW0.
Genome annotation databases
GeneID 4381436; -.
GenomeReviews CP000438_GR; PA14_19190.
KEGG pau:PA14_19190; -.
NMPDR fig|208963.3.peg.1024; -.
CMR Q02QW0; PA14_19190.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Metal-binding; NAD; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   564  564     NAD-dependent malic enzyme. PRO_1000069534
ACT_SITE   102   102        Proton donor (By similarity). 
ACT_SITE   173   173        Proton acceptor (By similarity). 
METAL   244   244        Divalent metal cation (By similarity). 
METAL   245   245        Divalent metal cation (By similarity). 
METAL   268   268        Divalent metal cation (By similarity). 
BINDING   155   155        NAD (By similarity). 
BINDING   268   268        NAD (By similarity). 
BINDING   417   417        NAD (By similarity). 
SITE   268   268  1     Important for activity (By similarity). 
Sequence information
Length: 564 AA [This is the length of the unprocessed precursor] Molecular weight: 62448 Da [This is the MW of the unprocessed precursor] CRC64: C11DD287882BA4AD [This is a checksum on the sequence]
        10         20         30         40         50         60 
MTETAKRPLY VPHAGPSLLE MPLLNKGSAF STQERIDFNL QGLLPHNIET IEEQTERAYS 

        70         80         90        100        110        120 
QYNLCNTDLD RHIFLRSIQD NNETLFFRLL EEHLEEMMPI IYTPTVGQAC QEFSKIYRTH 

       130        140        150        160        170        180 
RGLFISYPDR ERIDDILRSA TKNNVKIVVV TDSERILGLG DQGIGGMGIP IGKLSLYTAC 

       190        200        210        220        230        240 
GGISPAYTLP VVLDVGTNNP DLLNDPMYMG WRHERVSGAQ YEEFVDLFIQ AIKRRWPNVL 

       250        260        270        280        290        300 
LQFEDFAQTN AMPLLERYKD ELCCFNDDIQ GTAAVAVGTL LAACKAKGEK LSEQTVTFVG 

       310        320        330        340        350        360 
AGSAGCGIAE QIIAAMQLEG LDEAQARRRI FMVDRWGLLT DDMSNLLDFQ HRLAQKRADL 

       370        380        390        400        410        420 
GAWGGQQGDD LALLEVIRNA RPTVLIGVSG QRGLFSEEVI RELHSHCKQP LVMPLSNPTS 

       430        440        450        460        470        480 
RVEATPQEIL NWTDGQALVA TGSPFQPVQV GDKRIPIAQC NNAYIFPGIG LGVIAARANR 

       490        500        510        520        530        540 
VTEGMLMAAA NALANCSPIV TRGEGAVLPA LGDIREVSKR IAVAVAKQAQ AEGKALHTSD 

       550        560 
EVLNDAIEAN FWFPRYRAYR RTSF 

Q02QW0 in FASTA format

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BLAST logo BLAST submission on ExPASy/SIB
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Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
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