MAO1_SHEAM
ID MAO1_SHEAM Reviewed; 562 AA.
AC A1S8W7;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, 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=Sama_2621;
OS Shewanella amazonensis (strain ATCC BAA-1098 / SB2B).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=326297;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1098 / SB2B;
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 Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Fredrickson J.,
RA Richardson P.;
RT "Complete sequence of Shewanella amazonensis SB2B.";
RL Submitted (DEC-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; CP000507; ABM00824.1; -; Genomic_DNA.
DR RefSeq; WP_011760729.1; NC_008700.1.
DR AlphaFoldDB; A1S8W7; -.
DR SMR; A1S8W7; -.
DR STRING; 326297.Sama_2621; -.
DR EnsemblBacteria; ABM00824; ABM00824; Sama_2621.
DR KEGG; saz:Sama_2621; -.
DR eggNOG; COG0281; Bacteria.
DR HOGENOM; CLU_011405_5_2_6; -.
DR OMA; QMWDPVY; -.
DR OrthoDB; 654531at2; -.
DR Proteomes; UP000009175; 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_1000069538"
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; 62483 MW; 5658C73136CA57AB CRC64;
MDDNKRPLYL PFAGPAILEA PLINKGSAFT EEERIFFNLE GLLPYAIETI EEQASRAYDQ
FRSFNNDLDK HIYLRNIQDT NETLFYRLVQ NNIAEMMPII YTPTVGLACE RFSKNYRRNR
GLFISYPNKD RIDDILNNST RHKVKIIVVT DGERILGLGD QGIGGMGIPI GKLSLYTSCG
GISPAYTLPI TLDVGTDNPH LLEDPMYMGW RHPRIGGEEY SEFIEAFMEA VHRRWPDVLI
QFEDFAQKNA MPILERYKDR YCCFNDDIQG TAAVTVGSLL AACQAAGTKL SDQRITFLGA
GSAGCGIAEA IVAQMVSEGI SDDQARSQVF MVDRWGLLLD NMPNLLPFQQ KLAQKIDNIN
HWDDFSDNVS LLNVVNNAKP TVLIGVSGAP GLFTEEIIRA MHSHCARPIV FPLSNPTSRV
EATPKDILHW TSGQALVATG SPFEPVVVDD VTYDIAQCNN SYIFPGIGLG VLACGANRVS
NEMLMASSRA LAECSPLAKD GSGPLLPPLE EIHDVSKHIA FAVAKVAIEQ GHALDTTDEL
LMQSIEANFW YPEYRRYKRT SF
