ID MAO1_VIBPA Reviewed; 562 AA. AC Q87Q92; DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 16-JUN-2009, entry version 41. DE RecName: Full=NAD-dependent malic enzyme; DE Short=NAD-ME; DE EC=1.1.1.38; GN Name=sfcA; OrderedLocusNames=VP1258; OS Vibrio parahaemolyticus. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=670; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RIMD 2210633 / Serotype O3:K6; RX MEDLINE=22508454; PubMed=12620739; DOI=10.1016/S0140-6736(03)12659-1; RA Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K., RA Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S., RA Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.; RT "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism RT distinct from that of V. cholerae."; RL Lancet 361:743-749(2003). 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; BA000031; BAC59521.1; -; Genomic_DNA. DR RefSeq; NP_797637.1; -. DR HSSP; P40927; 1GQ2. DR GeneID; 1188763; -. DR GenomeReviews; BA000031_GR; VP1258. DR KEGG; vpa:VP1258; -. DR NMPDR; fig|223926.1.peg.1258; -. DR HOGENOM; Q87Q92; -. DR OMA; Q87Q92; IQDNNET. DR BioCyc; VPAR223926:VP1258-MON; -. DR BRENDA; 1.1.1.38; 3063. 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 or NADH 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_dom. 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_0000160236. 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; 62299 MW; E1B8D7A80CF073F3 CRC64; MNNDKRPLYI PYAGPALMAT PLLNKGSAFS AEERSSFNLE GLLPETTETI QEQVERAYQQ YKSFESDMDK HIYLRNIQDT NETLFYRLVQ NHISEMMPII YTPTVGAACE NFSNIYRRGR GLFISYPNRD RIDDLLNNAA NHNVKVIVVT DGERILGLGD QGIGGMGIPI GKLSLYTACG GISPAYTLPI VLDVGTNNPQ RLADPMYMGW RHPRITGPDY DAFVEEFIQA VQRRWPDALI QFEDFAQKNA MPLLERYKDR ICCFNDDIQG TAAVTVGSLL AACKAAGTQL SKQRITFLGA GSAGCGIAEA IIAQMVSEGI SDEKARSQVY MVDRWGLLQE GMPNLLDFQQ RLVQKHSNTK EWENEGNGFS LLDVMRNAKP TVLIGVSGAP GLFSQEVIEE MHKHCKRPIV FPLSNPTSRV EATPNDIIRW TNGEALVATG SPFDPVVHEG RTYPIAQCNN SYIFPGIGLG VLAVNAKRVT DEMLMESSRA LATCSPLAIN GRGALLPPLE EIHLVSKKIA FAVAKKAIEQ GVALEITDEA LNDAIDQAFW QPVYRRYKRT AF //