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MAO1_SHEFN
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   03-AUG-2022, entry version 93.
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}; 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].
RC   STRAIN=NCIMB 400;
RG   US DOE Joint Genome Institute;
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., Pitluck S.,
RA   Fredrickson J.K., Kolker E., McCuel L.A., DiChristina T., Nealson K.H.,
RA   Newman D., Tiedje J.M., Zhou J., Romine M.F., Culley D.E., Serres M.,
RA   Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., 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:
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; CP000447; ABI70686.1; -; Genomic_DNA.
DR   RefSeq; WP_011636309.1; NC_008345.1.
DR   AlphaFoldDB; Q086X9; -.
DR   SMR; Q086X9; -.
DR   STRING; 318167.Sfri_0833; -.
DR   EnsemblBacteria; ABI70686; ABI70686; Sfri_0833.
DR   KEGG; sfr:Sfri_0833; -.
DR   eggNOG; COG0281; Bacteria.
DR   HOGENOM; CLU_011405_5_2_6; -.
DR   OMA; QMWDPVY; -.
DR   OrthoDB; 654531at2; -.
DR   Proteomes; UP000000684; 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; Reference proteome.
FT   CHAIN           1..562
FT                   /note="NAD-dependent malic enzyme"
FT                   /id="PRO_1000069542"
FT   ACT_SITE        101
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01619"
FT   ACT_SITE        172
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01619"
FT   BINDING         154
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01619"
FT   BINDING         243
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01619"
FT   BINDING         244
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01619"
FT   BINDING         267
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01619"
FT   BINDING         267
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01619"
FT   BINDING         415
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01619"
FT   SITE            267
FT                   /note="Important for activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01619"
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
 
 
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