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UniProtKB/Swiss-Prot entry Q12RA0

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

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Entry information
Entry name MAO1_SHEDO
Primary accession number Q12RA0
Secondary accession numbers None
Integrated into Swiss-Prot on February 5, 2008
Sequence was last modified on August 22, 2006 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 27)
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: Sden_0736
From
Shewanella denitrificans (strain OS217 / ATCC BAA-1090 / DSM 15013) [TaxID: 318161] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; Shewanellaceae; Shewanella.
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., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Richardson P.;
"Complete sequence of Shewanella denitrificans OS217.";
Submitted (MAR-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
CP000302; ABE54026.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_561749.1; -.
3D structure databases
ModBase Q12RA0.
Enzyme and pathway databases
BioCyc SDEN318161:SDEN_0736-MON; -.
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.
Genome annotation databases
GeneID 4016842; -.
GenomeReviews CP000302_GR; Sden_0736.
KEGG sdn:Sden_0736; -.
NMPDR fig|318161.14.peg.718; -.
Phylogenomic databases
HOGENOM Q12RA0; -.
Genome annotation databases
CMR Q12RA0; Sden_0736.
Other
ProtoNet Q12RA0.
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   562  562     NAD-dependent malic enzyme. PRO_1000069541
ACT_SITE   101   101        Proton donor (By similarity). 
ACT_SITE   172   172        Proton acceptor (By similarity). 
METAL   243   243        Divalent metal cation (By similarity). 
METAL   244   244        Divalent metal cation (By similarity). 
METAL   267   267        Divalent metal cation (By similarity). 
BINDING   154   154        NAD (By similarity). 
BINDING   267   267        NAD (By similarity). 
BINDING   415   415        NAD (By similarity). 
SITE   267   267  1     Important for activity (By similarity). 
Sequence information
Length: 562 AA [This is the length of the unprocessed precursor] Molecular weight: 62265 Da [This is the MW of the unprocessed precursor] CRC64: 942252D30AF25265 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MDDTKRPLYL PFAGPAILEA PLINKGSAFS EEERIFFNLE GLLPYVIETI EEQAARAYAQ 

        70         80         90        100        110        120 
FSNFSNDLDK HIYLRNIQDT NETLFYRLVR NNITEMMPII YTPTVGLACE RFSKNYRRNR 

       130        140        150        160        170        180 
GLFISYSNKD RIDDILNNST RHKVKVIVVT DGERILGLGD QGIGGMGIPI GKLSLYTSCG 

       190        200        210        220        230        240 
GISPAYTLPI TLDVGTDNQE LLDDPMYMGW RHRRIEGQDY ADFVEAFMEA VHRRWPDVLI 

       250        260        270        280        290        300 
QFEDFAQRNA MPLLERYKDQ YCCFNDDIQG TAAVTVGSLL AASKAANTQL SKQRVVFLGA 

       310        320        330        340        350        360 
GSAGCGIAEA IVAQMISEGI SEAQARSQVF MVDRLGLLQD NTANLLPFQQ KLAQSSATVS 

       370        380        390        400        410        420 
QWHIEGDSVS LLNVINNAKP TVLIGVSGSP GQFTEAVIRA MHLHCPRPIV FPLSNPTSRV 

       430        440        450        460        470        480 
EATPEDVLNW TNGQALVATG SPFEPVTIGD ETFEIAQCNN SFIFPGIGLG VLACRAKRVS 

       490        500        510        520        530        540 
DEMLMASSRA LAECSPLGTT RTGSLLPKLD DIQKVSKYIA FAVAKVAMAQ GLALPLTDEL 

       550        560 
LNKSIEKNFW EPKYRRYKRT SF
Q12RA0 in FASTA format

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