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 P40927


[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 MAOX_COLLI
Primary accession number P40927
Secondary accession numbers None
Integrated into Swiss-Prot on February 1, 1995
Sequence was last modified on February 1, 1995 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 56)
Name and origin of the protein
Protein name NADP-dependent malic enzyme
Synonyms NADP-ME
EC 1.1.1.40
Gene name
Name: ME1
From
Columba livia (Domestic pigeon) [TaxID: 8932] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Archosauria; Dinosauria; Saurischia; Theropoda; Coelurosauria; Aves; Neognathae; Columbiformes; Columbidae; Columba.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
DOI=10.1006/abbi.1994.1152; PubMed=8161199 [NCBI, ExPASy, EBI, Israel, Japan]
Chou W.-Y., Huang S.-M., Liu Y.H., Chang G.-G.;
"Cloning and expression of pigeon liver cytosolic NADP(+)-dependent malic enzyme cDNA and some of its abortive mutants.";
Arch. Biochem. Biophys. 310:158-166(1994).
[2]
PROTEIN SEQUENCE OF 259-283.
DOI=10.1021/bi00191a021; PubMed=8011656 [NCBI, ExPASy, EBI, Israel, Japan]
Wei C.H., Chou W.-Y., Huang S.-M., Lin C.C., Chang G.-G.;
"Affinity cleavage at the putative metal-binding site of pigeon liver malic enzyme by the Fe(2+)-ascorbate system.";
Biochemistry 33:7931-7936(1994).
[3]
MUTAGENESIS OF LYS-162 AND LYS-340.
DOI=10.1006/bbrc.2000.2502; PubMed=10772909 [NCBI, ExPASy, EBI, Israel, Japan]
Kuo C.C., Tsai L.C., Chin T.Y., Chang G.G., Chou W.Y.;
"Lysine residues 162 and 340 are involved in the catalysis and coenzyme binding of NADP(+)-dependent malic enzyme from pigeon.";
Biochem. Biophys. Res. Commun. 270:821-825(2000).
[4]
MUTAGENESIS OF ASP-141; ASP-194 AND ASP-464.
PubMed=10716176 [NCBI, ExPASy, EBI, Israel, Japan]
Chou W.Y., Chang H.P., Huang C.H., Kuo C.C., Tong L., Chang G.G.;
"Characterization of the functional role of Asp141, Asp194, and Asp464 residues in the Mn2+-L-malate binding of pigeon liver malic enzyme.";
Protein Sci. 9:242-251(2000).
[5]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 2-556 IN COMPLEX WITH NADP; MANGANESE AND SUBSTRATE.
DOI=10.1110/ps.38002; PubMed=11790843 [NCBI, ExPASy, EBI, Israel, Japan]
Yang Z., Zhang H., Huang H.-C., Kuo C.-C., Tsai L.-C., Yuan H.S., Chou W.-Y., Chang G.-G., Tong L.;
"Structural studies of the pigeon cytosolic NADP(+)-dependent malic enzyme.";
Protein Sci. 11:332-341(2002).
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
L09233; AAA49450.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S43231; S43231.
3D structure databases
PDB
1GQ2; X-ray; 2.50 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=2-556.[ExPASy / RCSB / EBI]
PDBsum 1GQ2; -.
ModBase P40927.
Family and domain databases
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.
BLOCKS P40927.
Phylogenomic databases
HOVERGEN P40927; -.
Other
ProtoNet P40927.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Cytoplasm; Direct protein sequencing; Metal-binding; NADP; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   557  557     NADP-dependent malic enzyme. PRO_0000160198
NP_BIND   290   307  18     NADP. 
ACT_SITE   91    91        Proton donor. 
ACT_SITE   162   162        Proton acceptor. 
METAL   234   234        Divalent metal cation. 
METAL   235   235        Divalent metal cation. 
METAL   258   258        Divalent metal cation. 
BINDING   144   144        NADP. 
BINDING   258   258        NADP. 
BINDING   397   397        NADP. 
SITE   258   258  1     Important for activity. 
SITE   340   340  1     Confers specificity for NADP. 
MUTAGEN   141   141        D->N: Increases Km for manganese 14-fold. Increases Km for malate 5-fold. 
MUTAGEN   162   162        K->A: Decreases Kcat 235-fold. no effect on Km for NADP. 
MUTAGEN   194   194        D->N: No effect on Km for manganese. Increases Km for malate 8-fold. 
MUTAGEN   340   340        K->A: Increases Km for NADP 65-fold. No effect on Kcat. 
MUTAGEN   464   464        D->N: No effect. 
CONFLICT   279   279        N -> D (in Ref. 2; AA sequence). 
HELIX   6     9  4      
TURN   11    13  3      
HELIX   16    18  3      
HELIX   21    26  6      
HELIX   40    53  14      
HELIX   57    70  14      
HELIX   72    81  10      
HELIX   83    90  8      
HELIX   94   100  7      
HELIX   102   105  4      
STRAND   111   115  5      
HELIX   116   118  3      
HELIX   122   127  6      
STRAND   136   140  5      
STRAND   142   144  3      
HELIX   146   148  3      
HELIX   152   156  5      
HELIX   157   168  12      
HELIX   174   176  3      
STRAND   177   184  8      
HELIX   189   193  5      
HELIX   208   225  18      
STRAND   230   233  4      
HELIX   238   248  11      
TURN   249   251  3      
STRAND   252   256  5      
TURN   257   259  3      
HELIX   260   277  18      
HELIX   281   283  3      
STRAND   286   289  4      
HELIX   293   308  16      
HELIX   313   317  5      
STRAND   320   324  5      
HELIX   340   343  4      
HELIX   353   360  8      
STRAND   363   367  5      
HELIX   377   386  10      
STRAND   391   394  4      
HELIX   399   401  3      
HELIX   406   412  7      
TURN   413   415  3      
STRAND   418   423  6      
HELIX   443   445  3      
HELIX   447   457  11      
HELIX   464   476  13      
HELIX   480   484  5      
HELIX   492   494  3      
HELIX   495   512  18      
HELIX   525   530  6      
STRAND   550   553  4      
Sequence information
Length: 557 AA [This is the length of the unprocessed precursor] Molecular weight: 62054 Da [This is the MW of the unprocessed precursor] CRC64: 7489A2E6741567C8 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MKKGYEVLRD PHLNKGMAFT LEERQQLNIH GLLPPCFLGQ DAQVYSILKN FERLTSDLDR 

        70         80         90        100        110        120 
YILLMSLQDR NEKLFYKVLT SDIERFMPIV YTPTVGLACQ HYGLAFRRPR GLFITIHDRG 

       130        140        150        160        170        180 
HIATMLQSWP ESVIKAIVVT DGERILGLGD LGCYGMGIPV GKLALYTACG GVKPHQCLPV 

       190        200        210        220        230        240 
MLDVGTDNET LLKDPLYIGL RHKRIRGQAY DDLLDEFMEA VTSRYGMNCL IQFEDFANAN 

       250        260        270        280        290        300 
AFRLLHKYRN KYCTFNDDIQ GTASVAVAGL LAALRITKNR LSDHTVLFQG AGEAALGIAN 

       310        320        330        340        350        360 
LIVMAMQKEG VSKEEAIKRI WMVDSKGLIV KGRASLTPEK EHFAHEHCEM KNLEDIVKDI 

       370        380        390        400        410        420 
KPTVLIGVAA IGGAFTQQIL QDMAAFNKRP IIFALSNPTS KAECTAEQLY KYTEGRGIFA 

       430        440        450        460        470        480 
SGSPFDPVTL PSGQTLYPGQ GNNSYVFPGV ALGVISCGLK HIGDDVFLTT AEVIAQEVSE 

       490        500        510        520        530        540 
ENLQEGRLYP PLVTIQQVSL KIAVRIAKEA YRNNTASTYP QPEDLEAFIR SQVYSTDYNC 

       550 
FVADSYTWPE EAMKVKL 

P40927 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!