ID MAO1_SHEFN Reviewed; 562 AA. AC Q086X9; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 31-OCT-2006, sequence version 1. DT 25-NOV-2008, entry version 24. DE RecName: Full=NAD-dependent malic enzyme; DE Short=NAD-ME; DE EC=1.1.1.38; GN Name=sfcA; OrderedLocusNames=Sfri_0833; OS Shewanella frigidimarina (strain NCIMB 400). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=318167; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Fredrickson J.K., Kolker E., McCuel L.A., DiChristina T., RA Nealson K.H., Newman D., Tiedje J.M., Zhou J., Romine M.F., RA Culley D.E., Serres M., Chertkov O., Brettin T., Bruce D., Han C., RA Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Hauser L., RA Kyrpides N., Mikhailova N., Richardson P.; RT "Complete sequence of Shewanella frigidimarina NCIMB 400."; RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: (S)-malate + NAD(+) = pyruvate + CO(2) + NADH. CC -!- COFACTOR: Divalent metal cations. Prefers magnesium or manganese CC (By similarity). CC -!- SUBUNIT: Homotetramer (By similarity). CC -!- SIMILARITY: Belongs to the malic enzymes family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000447; ABI70686.1; -; Genomic_DNA. DR RefSeq; YP_749524.1; -. DR GeneID; 4276930; -. DR GenomeReviews; CP000447_GR; Sfri_0833. DR KEGG; sfr:Sfri_0833; -. DR NMPDR; fig|318167.10.peg.792; -. DR HOGENOM; Q086X9; -. DR GO; GO:0016619; F:malate dehydrogenase (oxaloacetate-decarbox...; IEA:HAMAP. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0006108; P:malate metabolic process; IEA:InterPro. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR HAMAP; MF_01619; -; 1. DR InterPro; IPR015884; Malic_enzyme_CS. DR InterPro; IPR012301; Malic_N. DR InterPro; IPR012302; Malic_NAD_bd. DR InterPro; IPR001891; Malic_OxRdtase. DR InterPro; IPR016040; NAD(P)-bd. DR Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1. DR Pfam; PF00390; malic; 1. DR Pfam; PF03949; Malic_M; 1. DR PRINTS; PR00072; MALOXRDTASE. DR PROSITE; PS00331; MALIC_ENZYMES; 1. PE 3: Inferred from homology; KW Complete proteome; Metal-binding; NAD; Oxidoreductase. FT CHAIN 1 562 NAD-dependent malic enzyme. FT /FTId=PRO_1000069542. FT ACT_SITE 101 101 Proton donor (By similarity). FT ACT_SITE 172 172 Proton acceptor (By similarity). FT METAL 243 243 Divalent metal cation (By similarity). FT METAL 244 244 Divalent metal cation (By similarity). FT METAL 267 267 Divalent metal cation (By similarity). FT BINDING 154 154 NAD (By similarity). FT BINDING 267 267 NAD (By similarity). FT BINDING 415 415 NAD (By similarity). FT SITE 267 267 Important for activity (By similarity). SQ SEQUENCE 562 AA; 62258 MW; B19107A9328466BA CRC64; MDDNKRPLYL PFAGPAILES PLLNKGSAFS EEERIYFNLE GLIPWVIETI DEQAARAYAQ FKNFTNDLDK HIYLRNIQDT NETLFYRLVR NNISEMMPII YTPTVGLACE RFSKNYRRNR GLFISYPNKD RIDDILNNST RHKVKVIVVT DGERILGLGD QGIGGMGIPI GKLSLYTSCG GISPAYCLAV TLDVGTDNPQ LLEDPMYMGW RHQRIGGDEY AEFVEEFMQA VSRRWPDALI QFEDFAQKNA MPLLERYKDQ YCSFNDDIQG TAAVTVGSLL AACKAANSKL SEQRITFLGA GSAGCGIAEA IVATMVSEGI SDQQARSQVF MVDRWGLLLD NMPNLLPFQQ KLAQPCATIE AWDNYSDNIS LLDVVNNAKP TVLIGVSGSP GLFTEEIIKA MHSHCKRPIV FPLSNPTSRV EATPKDILNW TSGQALVATG SPFEPVIVNG ETFEIAQCNN SFIFPGIGLG VLSCGARRVS DEMLMASSRA LAECSPLGKD GVGSLLPRLE DIQTVSKYIA FAVAKAAIDQ GLALPCTDEL LQQSIEANFW EPEYRRYKRT SF //