(data stored in SCRATCH zone)

SWISSPROT: A8FQM7_SHESH

ID   A8FQM7_SHESH            Unreviewed;       415 AA.
AC   A8FQM7;
DT   13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2007, sequence version 1.
DT   05-JUL-2017, entry version 69.
DE   SubName: Full=Malate dehydrogenase (Oxaloacetate-decarboxylating) (NADP(+)) {ECO:0000313|EMBL:ABV35150.1};
DE            EC=1.1.1.40 {ECO:0000313|EMBL:ABV35150.1};
GN   OrderedLocusNames=Ssed_0538 {ECO:0000313|EMBL:ABV35150.1};
OS   Shewanella sediminis (strain HAW-EB3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=425104 {ECO:0000313|EMBL:ABV35150.1, ECO:0000313|Proteomes:UP000002015};
RN   [1] {ECO:0000313|EMBL:ABV35150.1, ECO:0000313|Proteomes:UP000002015}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAW-EB3 {ECO:0000313|EMBL:ABV35150.1,
RC   ECO:0000313|Proteomes:UP000002015};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D.,
RA   Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella sediminis HAW-EB3.";
RL   Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000106-3};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000106-3};
CC       Note=Divalent metal cations. Prefers magnesium or manganese.
CC       {ECO:0000256|PIRSR:PIRSR000106-3};
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DR   EMBL; CP000821; ABV35150.1; -; Genomic_DNA.
DR   RefSeq; WP_012140887.1; NC_009831.1.
DR   ProteinModelPortal; A8FQM7; -.
DR   STRING; 425104.Ssed_0538; -.
DR   EnsemblBacteria; ABV35150; ABV35150; Ssed_0538.
DR   KEGG; sse:Ssed_0538; -.
DR   eggNOG; ENOG4105C6K; Bacteria.
DR   eggNOG; COG0281; LUCA.
DR   HOGENOM; HOG000132447; -.
DR   KO; K00029; -.
DR   OMA; ILFKQFG; -.
DR   OrthoDB; POG091H02AU; -.
DR   BioCyc; SSED425104:GH7Q-560-MONOMER; -.
DR   Proteomes; UP000002015; Chromosome.
DR   GO; GO:0004471; F:malate dehydrogenase (decarboxylating) (NAD+) activity; IEA:InterPro.
DR   GO; GO:0004473; F:malate dehydrogenase (decarboxylating) (NADP+) activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0008948; F:oxaloacetate decarboxylase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.50.10380; -; 1.
DR   InterPro; IPR015884; Malic_enzyme_CS.
DR   InterPro; IPR012301; Malic_N_dom.
DR   InterPro; IPR012302; Malic_NAD-bd.
DR   InterPro; IPR001891; Malic_OxRdtase.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   Pfam; PF00390; malic; 1.
DR   Pfam; PF03949; Malic_M; 1.
DR   PIRSF; PIRSF000106; ME; 1.
DR   SMART; SM01274; malic; 1.
DR   SMART; SM00919; Malic_M; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS00331; MALIC_ENZYMES; 1.
PE   4: Predicted;
DR   PRODOM; A8FQM7.
DR   SWISS-2DPAGE; A8FQM7.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002015};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000106-3};
KW   Oxidoreductase {ECO:0000313|EMBL:ABV35150.1}.
FT   DOMAIN       17    150       malic. {ECO:0000259|SMART:SM01274}.
FT   DOMAIN      162    399       Malic_M. {ECO:0000259|SMART:SM00919}.
FT   ACT_SITE     38     38       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR000106-1}.
FT   ACT_SITE     93     93       Proton acceptor. {ECO:0000256|PIRSR:
FT                                PIRSR000106-1}.
FT   METAL       135    135       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000106-3}.
FT   METAL       136    136       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000106-3}.
FT   METAL       161    161       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000106-3}.
SQ   SEQUENCE   415 AA;  44703 MW;  19B81F8A7954F508 CRC64;
     MSDLRQQALD YHEFPVAGKT AVCLTKPAET SMDLALAYSP GVAEPVREIA ANPDDAYRYT
     AKGNTVAVIS NGTAILGLGN LGPLASKPVM EGKALLFKHF ANIDATDIEV KHRTAEEFIN
     TVEAIADTFG GINLEDIKAP ECFEIEKALI ERCNVPVFHD DQHGTAIVTA AGMINALEIQ
     GKEIDKAIFV CMGAGAAAIA CMTMLVKCGV QRENVYMLDR KGVIHTRRED INEYKALFAN
     NTDKRTLQEV IKGADAFLGL SGPDVLAAED VALMADKPVI FACSNPDPEI RPEIAHDVRK
     DLIMGTGRSD YPNQVNNVLC FPFIFRGALD VRASRINDEM KIAAVNAIAA LAREEVPASV
     LAAYPNVSEL SFGPDYVIPK PMDPRLLSNV AKAVAQAAID SGVAAIETLP DNYML
//

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