MAO1_ACIAD
ID MAO1_ACIAD Reviewed; 566 AA.
AC Q6FFL8;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 111.
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=ACIAD0166;
OS Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=62977;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33305 / BD413 / ADP1;
RX PubMed=15514110; DOI=10.1093/nar/gkh910;
RA Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L.,
RA Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N.,
RA Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
RT "Unique features revealed by the genome sequence of Acinetobacter sp. ADP1,
RT a versatile and naturally transformation competent bacterium.";
RL Nucleic Acids Res. 32:5766-5779(2004).
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; CR543861; CAG67139.1; -; Genomic_DNA.
DR RefSeq; WP_004930582.1; NC_005966.1.
DR AlphaFoldDB; Q6FFL8; -.
DR SMR; Q6FFL8; -.
DR STRING; 62977.ACIAD0166; -.
DR PRIDE; Q6FFL8; -.
DR EnsemblBacteria; CAG67139; CAG67139; ACIAD0166.
DR GeneID; 45232685; -.
DR KEGG; aci:ACIAD0166; -.
DR eggNOG; COG0281; Bacteria.
DR HOGENOM; CLU_011405_5_2_6; -.
DR OMA; QMWDPVY; -.
DR OrthoDB; 654531at2; -.
DR BioCyc; ASP62977:ACIAD_RS00775-MON; -.
DR Proteomes; UP000000430; 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..566
FT /note="NAD-dependent malic enzyme"
FT /id="PRO_0000160212"
FT ACT_SITE 105
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01619"
FT ACT_SITE 176
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01619"
FT BINDING 158
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
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 248
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01619"
FT BINDING 271
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01619"
FT BINDING 271
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01619"
FT BINDING 419
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01619"
FT SITE 271
FT /note="Important for activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01619"
SQ SEQUENCE 566 AA; 62969 MW; 2122BE03FE5FFC65 CRC64;
MTAETNTNKH PLYIPYAGYT LLELPLLNKG SAFTQEERSH FNLHGLIPHV IETIEEQSQR
SYQQYGAFND DINKHIYLRN IQDTNETLFY RLINDHLEEM MPIIYTPTVG EACQRFSDIY
RRHRGIFISY PDREHIDDIL QNVSKRNVKV IVITDGERIL GLGDQGIGGM GIPIGKLSLY
TACGGISPAY TLPITIDVGT NNQQLLNDPI YMGWRQPRIS GDEYYEFIDQ VLTGIRRRWP
HALIQFEDFA QKNAMPLLTK YRDKFCCFND DIQGTAAVSV GSLIAASRAA GKQLKDQTIT
FLGAGSAGCG IAEQIVAQMV AEGLTDAQAR ARVYMVDRFG LITENQPNLL DFQRKLAQKA
EVVSDWGNVE EVISLLDVVK NAKPTVLIGV SGQPGLFTEE VIRTLAENCE RPIVMPLSNP
TSRVEALPSD VIQWTNGRAL IATGSPFAPV NYQGKLYNIS QCNNSYIFPG IGLGVIASGA
KRVTDNMLMA SSNALADCSP LLQNPNADLL PAIADIQDVS KRIAFKVAKA AIEDGVALNM
SDEVLLQNIE KEFWKPKYRG YKRVPF
