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Entry: A4SVD1_POLSQ
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ID   A4SVD1_POLSQ            Unreviewed;       773 AA.
AC   A4SVD1;
DT   15-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   15-MAY-2007, sequence version 1.
DT   14-MAY-2014, entry version 52.
DE   SubName: Full=Malate dehydrogenase (Oxaloacetate-decarboxylating) (NADP(+))., Phosphate acetyltransferase;
DE            EC=1.1.1.40;
DE            EC=2.3.1.8;
GN   OrderedLocusNames=Pnuc_0224;
OS   Polynucleobacter necessarius subsp. asymbioticus (strain DSM 18221 /
OS   CIP 109841 / QLW-P1DMWA-1).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Polynucleobacter.
OX   NCBI_TaxID=312153;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18221 / CIP 109841 / QLW-P1DMWA-1;
RX   PubMed=22675600; DOI=10.4056/sigs.2395367;
RA   Meincke L., Copeland A., Lapidus A., Lucas S., Berry K.W.,
RA   Del Rio T.G., Hammon N., Dalin E., Tice H., Pitluck S., Richardson P.,
RA   Bruce D., Goodwin L., Han C., Tapia R., Detter J.C., Schmutz J.,
RA   Brettin T., Larimer F., Land M., Hauser L., Kyrpides N.C., Ivanova N.,
RA   Goker M., Woyke T., Wu Q.L., Pockl M., Hahn M.W., Klenk H.P.;
RT   "Complete genome sequence of Polynucleobacter necessarius subsp.
RT   asymbioticus type strain (QLW-P1DMWA-1(T)).";
RL   Stand. Genomic Sci. 6:74-83(2012).
CC   -!- SIMILARITY: Belongs to the malic enzymes family.
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DR   EMBL; CP000655; ABP33445.1; -; Genomic_DNA.
DR   RefSeq; YP_001155009.1; NC_009379.1.
DR   ProteinModelPortal; A4SVD1; -.
DR   STRING; 312153.Pnuc_0224; -.
DR   EnsemblBacteria; ABP33445; ABP33445; Pnuc_0224.
DR   GeneID; 5053370; -.
DR   KEGG; pnu:Pnuc_0224; -.
DR   PATRIC; 22964797; VBIPolNec12025_0231.
DR   eggNOG; COG0281; -.
DR   HOGENOM; HOG000132448; -.
DR   KO; K00029; -.
DR   OMA; CFVVERK; -.
DR   OrthoDB; EOG6QCD9W; -.
DR   BioCyc; PNEC312153:GH50-235-MONOMER; -.
DR   GO; GO:0005829; C:cytosol; IEA:InterPro.
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:0030145; F:manganese ion binding; IEA:InterPro.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0008948; F:oxaloacetate decarboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008959; F:phosphate acetyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006108; P:malate metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.50.10380; -; 1.
DR   Gene3D; 3.40.50.720; -; 1.
DR   InterPro; IPR015884; Malic_enzyme_CS.
DR   InterPro; IPR012301; Malic_N_dom.
DR   InterPro; IPR012302; Malic_NAD-bd.
DR   InterPro; IPR012188; ME_PTA.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   InterPro; IPR002505; PTA_PTB.
DR   Pfam; PF00390; malic; 1.
DR   Pfam; PF03949; Malic_M; 1.
DR   Pfam; PF01515; PTA_PTB; 1.
DR   PIRSF; PIRSF036684; ME_PTA; 1.
DR   SMART; SM00919; Malic_M; 1.
DR   PROSITE; PS00331; MALIC_ENZYMES; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Complete proteome; Metal-binding; Oxidoreductase;
KW   Transferase.
SQ   SEQUENCE   773 AA;  83196 MW;  6E03068CE7AE2002 CRC64;
     MSKENNKEQQ IAALREAALQ YHEFPVPGKI EIAPTKQLTN QRDLALAYTP GVAAPCEEIV
     KDPANAFKYT ARGNLVGVIT NGTAVLGLGN IGPLASKPVM EGKAVLFKKF AGIDVFDIEV
     NENDPDKLVE IIAALEPTFG GINLEDIKAP DCFVVERKLQ ARMKIPVFHD DQHGTAIVVA
     AAILNGLKVV GKDVGNVKLV TSGAGAAALA CLDLLVDLGI PRKNIWVTDL AGVAYKGRKE
     LMDPEKEPFC QETDLRTLDQ AIEGADIFLG LSAGGVLKPE MVKKMADKPL VYALANPTPE
     ILPEEVKAVR PDAVMATGRT DYPNQVNNVL CFPFIFRGAL DVGATTITRG MEVAAVKAVA
     ELAQAEQSEV VTSVYGIENL SFGPEYLIPK PFDPRLITVI APAVAKAAMD DGVALRPIKD
     FDAYRNQLQQ FVYHSGTLMK PLFSIAKRVP ANQKRIVFAE GEDERVLRAV QIILDEHLAT
     PILIGRPAVI EHRIEKFGLR MKAGDDFEIV NPENDLRFRD FWQTYLGLTE RKGVTQSFAK
     LEVRRRNSLI GSLLIEKGMA DGMISGTVGN IATHLKYIDE VIGHEEGANV YGAMSGLILP
     GRQVFLVDTH INIDPTAQQL SDLTLMAASE MRKLGLIPKV ALLSHSNFGS SNAPSAIKMR
     EVLALLQKAD PTLEVDGEMH GDSALDASIR EGAVSSSTLK GDANLLVLPN IDAANISYNL
     LKTAAGNGIA IGPLLLGVAK PIHILTPAAT VRRIVNVTTL AVVEAASNAR GIS
//
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