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MAO1_SALNS
ID   MAO1_SALNS              Reviewed;         565 AA.
AC   B4T5V6;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=NAD-dependent malic enzyme {ECO:0000255|HAMAP-Rule:MF_01619};
DE            Short=NAD-ME {ECO:0000255|HAMAP-Rule:MF_01619};
DE            EC=1.1.1.38 {ECO:0000255|HAMAP-Rule:MF_01619};
GN   Name=maeA {ECO:0000255|HAMAP-Rule:MF_01619};
GN   OrderedLocusNames=SNSL254_A1680;
OS   Salmonella newport (strain SL254).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=423368;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SL254;
RX   PubMed=21602358; DOI=10.1128/jb.00297-11;
RA   Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G.,
RA   Leclerc J.E., Ravel J., Cebula T.A.;
RT   "Comparative genomics of 28 Salmonella enterica isolates: evidence for
RT   CRISPR-mediated adaptive sublineage evolution.";
RL   J. Bacteriol. 193:3556-3568(2011).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-malate + NAD(+) = CO2 + NADH + pyruvate;
CC         Xref=Rhea:RHEA:12653, ChEBI:CHEBI:15361, ChEBI:CHEBI:15589,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.38;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01619};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + oxaloacetate = CO2 + pyruvate; Xref=Rhea:RHEA:15641,
CC         ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:16452,
CC         ChEBI:CHEBI:16526; EC=1.1.1.38; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01619};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01619};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01619};
CC       Note=Divalent metal cations. Prefers magnesium or manganese.
CC       {ECO:0000255|HAMAP-Rule:MF_01619};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01619}.
CC   -!- SIMILARITY: Belongs to the malic enzymes family. {ECO:0000255|HAMAP-
CC       Rule:MF_01619}.
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DR   EMBL; CP001113; ACF61377.1; -; Genomic_DNA.
DR   RefSeq; WP_000450509.1; NZ_CCMR01000003.1.
DR   AlphaFoldDB; B4T5V6; -.
DR   SMR; B4T5V6; -.
DR   EnsemblBacteria; ACF61377; ACF61377; SNSL254_A1680.
DR   KEGG; see:SNSL254_A1680; -.
DR   HOGENOM; CLU_011405_5_2_6; -.
DR   OMA; QMWDPVY; -.
DR   Proteomes; UP000008824; Chromosome.
DR   GO; GO:0004471; F:malate dehydrogenase (decarboxylating) (NAD+) activity; IEA:UniProtKB-UniRule.
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-UniRule.
DR   Gene3D; 3.40.50.10380; -; 1.
DR   HAMAP; MF_01619; NAD_malic_enz; 1.
DR   InterPro; IPR046346; Aminiacid_DH-like_N_sf.
DR   InterPro; IPR015884; Malic_enzyme_CS.
DR   InterPro; IPR012301; Malic_N_dom.
DR   InterPro; IPR037062; Malic_N_dom_sf.
DR   InterPro; IPR012302; Malic_NAD-bd.
DR   InterPro; IPR001891; Malic_OxRdtase.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR023667; NAD_malic_enz_proteobac.
DR   Pfam; PF00390; malic; 1.
DR   Pfam; PF03949; Malic_M; 1.
DR   PIRSF; PIRSF000106; ME; 1.
DR   PRINTS; PR00072; MALOXRDTASE.
DR   SMART; SM01274; malic; 1.
DR   SMART; SM00919; Malic_M; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   SUPFAM; SSF53223; SSF53223; 1.
DR   PROSITE; PS00331; MALIC_ENZYMES; 1.
PE   3: Inferred from homology;
KW   Metal-binding; NAD; Oxidoreductase.
FT   CHAIN           1..565
FT                   /note="NAD-dependent malic enzyme"
FT                   /id="PRO_1000186008"
FT   ACT_SITE        104
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01619"
FT   ACT_SITE        175
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01619"
FT   BINDING         157
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01619"
FT   BINDING         246
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01619"
FT   BINDING         247
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01619"
FT   BINDING         270
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01619"
FT   BINDING         270
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01619"
FT   BINDING         418
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01619"
FT   SITE            270
FT                   /note="Important for activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01619"
SQ   SEQUENCE   565 AA;  62910 MW;  DC4355DD02B632FF CRC64;
     METTTKKARS LYIPYAGPVL LEFPLLNKGS AFSVEERRNF NLSGLLPEVV ESIEEQAERA
     WLQYQGFKTE IDKHIYLRNI QDTNETLFYR LVQNHLEEMM PVIYTPTVGA ACERFSEIYR
     RARGVFISYP NRHNMDDILQ NVPNHNIKVI VVTDGERILG LGDQGIGGMG IPIGKLSLYT
     ACGGISPAYT LPVVLDVGTN NQQLLNDPLY MGWRHPRITD DEYYAFVDEF IQAVKQRWPD
     ILLQFEDFAQ KNAMPLLTRY RDEICSFNDD IQGTAAVTVG TLIAASRAAG SQLSEQKIVF
     LGAGSAGCGI AEQIIAQTQR EGLSEDAARQ NVFMVDRFGL LTDRMPNLLP FQAKLVQKCD
     NLQHWDTEND VLSLLDVVRN VKPDILIGVS GQTGLFTEEI IREMHKHCPR PIVMPLSNPT
     SRVEATPQDI IAWTEGNALV ATGSPFSPVI WKDKIYPIAQ CNNAYIFPGI GLGVIASGAS
     RITDEMLMSA SETLAKHSPL VNNGEGLVLP ALKDIQVVSR AIAFAVGKMA QQQGVAVKTS
     AEALQQAIDD NFWKPEYRDY RRTSI
 
 
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