ID   MAO2_SALTY              Reviewed;         759 AA.
AC   Q9ZFV8;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   13-DEC-2001, sequence version 2.
DT   16-JUN-2009, entry version 62.
DE   RecName: Full=NADP-dependent malic enzyme;
DE            Short=NADP-ME;
DE            EC=1.1.1.40;
GN   Name=maeB; OrderedLocusNames=STM2472;
OS   Salmonella typhimurium.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=90371;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   MEDLINE=21534948; PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M.,
RA   Waterston R., Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium
RT   LT2.";
RL   Nature 413:852-856(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 610-759.
RC   STRAIN=LT2;
RX   MEDLINE=99395039; PubMed=10464203;
RA   Kofoid E.C., Rappleye C.A., Stojiljkovic I., Roth J.R.;
RT   "The 17-gene ethanolamine (eut) operon of Salmonella typhimurium
RT   encodes five homologues of carboxysome shell proteins.";
RL   J. Bacteriol. 181:5317-5329(1999).
CC   -!- CATALYTIC ACTIVITY: (S)-malate + NADP(+) = pyruvate + CO(2) +
CC       NADPH.
CC   -!- COFACTOR: Divalent metal cations. Prefers magnesium or manganese
CC       (By similarity).
CC   -!- SIMILARITY: In the N-terminal section; belongs to the malic
CC       enzymes family.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the phosphate
CC       acetyltransferase and butyryltransferase family.
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DR   EMBL; AE008811; AAL21366.1; -; Genomic_DNA.
DR   EMBL; AF093749; AAC78109.1; -; Genomic_DNA.
DR   RefSeq; NP_461407.1; -.
DR   GeneID; 1253994; -.
DR   GenomeReviews; AE006468_GR; STM2472.
DR   KEGG; stm:STM2472; -.
DR   NMPDR; fig|99287.1.peg.2388; -.
DR   HOGENOM; Q9ZFV8; -.
DR   OMA; Q9ZFV8; EIRPELA.
DR   BioCyc; STYP99287:STM2472-MON; -.
DR   BRENDA; 1.1.1.40; 2.
DR   GO; GO:0008415; F:acyltransferase activity; IEA:InterPro.
DR   GO; GO:0004473; F:malate dehydrogenase (oxaloacetate-decarbox...; IEA:EC.
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:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR015884; Malic_enzyme_CS.
DR   InterPro; IPR012301; Malic_N.
DR   InterPro; IPR012302; Malic_NAD_bd.
DR   InterPro; IPR012188; ME_PTA.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   InterPro; IPR002505; PTA_PTB.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   Pfam; PF00390; malic; 1.
DR   Pfam; PF03949; Malic_M; 1.
DR   Pfam; PF01515; PTA_PTB; 1.
DR   PIRSF; PIRSF036684; ME_PTA; 1.
DR   PROSITE; PS00331; MALIC_ENZYMES; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Metal-binding; Multifunctional enzyme; NADP;
KW   Oxidoreductase.
FT   CHAIN         1    759       NADP-dependent malic enzyme.
FT                                /FTId=PRO_0000160244.
FT   NP_BIND      76     83       NADP (By similarity).
FT   REGION        1    428       Malic enzyme.
FT   REGION      429    759       Phosphate acetyltransferase.
FT   ACT_SITE     94     94       Proton acceptor (By similarity).
FT   METAL       136    136       Divalent metal cation (By similarity).
FT   METAL       137    137       Divalent metal cation (By similarity).
FT   BINDING     162    162       NAD (By similarity).
FT   BINDING     288    288       NAD (By similarity).
FT   CONFLICT    610    610       A -> G (in Ref. 2; AAC78109).
FT   CONFLICT    613    613       A -> P (in Ref. 2; AAC78109).
FT   CONFLICT    621    621       R -> H (in Ref. 2; AAC78109).
FT   CONFLICT    626    626       E -> G (in Ref. 2; AAC78109).
FT   CONFLICT    635    635       S -> C (in Ref. 2; AAC78109).
FT   CONFLICT    643    643       L -> P (in Ref. 2; AAC78109).
FT   CONFLICT    679    679       R -> C (in Ref. 2; AAC78109).
FT   CONFLICT    754    754       A -> G (in Ref. 2; AAC78109).
FT   CONFLICT    757    757       T -> Q (in Ref. 2; AAC78109).
SQ   SEQUENCE   759 AA;  82322 MW;  D5120B020158EF18 CRC64;
     MDEQLKQSAL DFHEFPVPGK IQVSPTKPLA TQRDLALAYS PGVAAPCLEI EKDPLAAYKY
     TARGNLVAVI SNGTAVLGLG NIGALAGKPV MEGKGVLFKK FAGIDVFDIE VDELDPDKFI
     NVVAALEPTF GGINLEDIKA PECFYIEQKL RERMNIPVFH DDQHGTAIIS TAAILNGLRV
     VEKNISDVRM VVSGAGAAAI ACMNLLVALG MQKHNIVVCD SKGVIYKGRE PNMAETKAAY
     AVDDSGKRTL DEVIDGADIF LGCSGPKVLT QEMVKKMARA PMILALANPE PEILPPLAKE
     VRPDAIICTG RSDYPNQVNN VLCFPFIFRG ALDVGATAIN EEMKLAAVRA IAELAHAEQS
     EVVASAYGDQ DLSFGPEYII PKPFDPRLIV KIAPAVAKAA MDSGVATRPI ADFDAYIDKL
     TEFVYKTNLF MKPIFSQARK DPKRVVLPEG EEARVLHATQ ELITLGLAKP ILIGRPSVIE
     MRIQKLGLQI KAGVDFEIVN NESDPRFKEY WSEYYQIMKR RGITQEQAQR AMIGNHTAIG
     AIMVQRGEAD AMICGTIGDY HEHFSVVKAV FGYRDGVHTA GAMNALLLPS GNTFIADTYV
     NEDPTPEQLA EIAVMAAETV RRFGIEPKVA LLSHSNFGSS NSLSASKMRE TLERVRERAP
     DLMIDGEMHG DAALVESIRN DRMPDSPLKG AANILVMPNM EAARISYNLL RVSSSEGVTV
     GPVLMGVSKP VHVLTPIASV RRIVNMVALA VVEAQTTPL
//