MAO1_ECOLI
ID MAO1_ECOLI Reviewed; 565 AA.
AC P26616; P78224;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 4.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=NAD-dependent malic enzyme;
DE Short=NAD-ME;
DE EC=1.1.1.38;
GN Name=maeA; Synonyms=sfcA; OrderedLocusNames=b1479, JW5238;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-431.
RC STRAIN=K12;
RX PubMed=2199308; DOI=10.1093/genetics/125.2.261;
RA Mahajan S.K., Chu C.C., Willis D.K., Templin A., Clark A.J.;
RT "Physical analysis of spontaneous and mutagen-induced mutants of
RT Escherichia coli K-12 expressing DNA exonuclease VIII activity.";
RL Genetics 125:261-273(1990).
RN [5]
RP BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, ACTIVITY REGULATION, AND SUBUNIT.
RC STRAIN=K12;
RX PubMed=17557829; DOI=10.1128/jb.00428-07;
RA Bologna F.P., Andreo C.S., Drincovich M.F.;
RT "Escherichia coli malic enzymes: two isoforms with substantial differences
RT in kinetic properties, metabolic regulation, and structure.";
RL J. Bacteriol. 189:5937-5946(2007).
RN [6]
RP BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY REGULATION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=17215140; DOI=10.1016/j.pep.2006.11.017;
RA Wang J., Tan H., Zhao Z.K.;
RT "Over-expression, purification, and characterization of recombinant NAD-
RT malic enzyme from Escherichia coli K12.";
RL Protein Expr. Purif. 53:97-103(2007).
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 -!- 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;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:17557829};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:17557829};
CC Note=Divalent metal cations. Prefers magnesium or manganese.
CC {ECO:0000269|PubMed:17557829};
CC -!- ACTIVITY REGULATION: Non-competitively inhibited by high concentrations
CC of NAD(+) and L-malate. Also inhibited by CoA, acetyl-phosphate,
CC palmitoyl-CoA, and oxaloacetate. Activated by aspartate.
CC {ECO:0000269|PubMed:17215140, ECO:0000269|PubMed:17557829}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.420 mM for L-malate {ECO:0000269|PubMed:17215140,
CC ECO:0000269|PubMed:17557829};
CC KM=0.66 mM for L-malate {ECO:0000269|PubMed:17215140,
CC ECO:0000269|PubMed:17557829};
CC KM=0.097 mM for NAD(+) {ECO:0000269|PubMed:17215140,
CC ECO:0000269|PubMed:17557829};
CC KM=0.0688 mM for NAD(+) {ECO:0000269|PubMed:17215140,
CC ECO:0000269|PubMed:17557829};
CC KM=2.59 mM for pyruvate {ECO:0000269|PubMed:17215140,
CC ECO:0000269|PubMed:17557829};
CC Vmax=125.47 umol/min/mg enzyme {ECO:0000269|PubMed:17215140,
CC ECO:0000269|PubMed:17557829};
CC Note=At pH 7.2.;
CC pH dependence:
CC Optimum pH is 7.2 to 7.5 for L-malate. {ECO:0000269|PubMed:17215140,
CC ECO:0000269|PubMed:17557829};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:17557829}.
CC -!- MISCELLANEOUS: Can also use NADP(+) but is more effective with NAD(+).
CC -!- SIMILARITY: Belongs to the malic enzymes family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA39419.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA39419.1; Type=Miscellaneous discrepancy; Note=The sequence differs from position 433 onward for unknown reasons.; Evidence={ECO:0000305};
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DR EMBL; U00096; AAC74552.2; -; Genomic_DNA.
DR EMBL; AP009048; BAA15127.2; -; Genomic_DNA.
DR EMBL; X55956; CAA39419.1; ALT_SEQ; Genomic_DNA.
DR PIR; B64901; B64901.
DR RefSeq; NP_415996.2; NC_000913.3.
DR RefSeq; WP_000433476.1; NZ_SSZK01000038.1.
DR PDB; 6AGS; X-ray; 2.31 A; A=1-565.
DR PDBsum; 6AGS; -.
DR AlphaFoldDB; P26616; -.
DR SMR; P26616; -.
DR BioGRID; 4260208; 273.
DR BioGRID; 850392; 3.
DR IntAct; P26616; 3.
DR STRING; 511145.b1479; -.
DR ChEMBL; CHEMBL3286080; -.
DR jPOST; P26616; -.
DR PaxDb; P26616; -.
DR PRIDE; P26616; -.
DR EnsemblBacteria; AAC74552; AAC74552; b1479.
DR EnsemblBacteria; BAA15127; BAA15127; BAA15127.
DR GeneID; 946031; -.
DR KEGG; ecj:JW5238; -.
DR KEGG; eco:b1479; -.
DR PATRIC; fig|1411691.4.peg.788; -.
DR EchoBASE; EB0941; -.
DR eggNOG; COG0281; Bacteria.
DR HOGENOM; CLU_011405_5_2_6; -.
DR InParanoid; P26616; -.
DR OMA; QMWDPVY; -.
DR PhylomeDB; P26616; -.
DR BioCyc; EcoCyc:MALIC-NAD-MON; -.
DR BioCyc; MetaCyc:MALIC-NAD-MON; -.
DR BRENDA; 1.1.1.38; 2026.
DR SABIO-RK; P26616; -.
DR PRO; PR:P26616; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0004471; F:malate dehydrogenase (decarboxylating) (NAD+) activity; IDA:EcoCyc.
DR GO; GO:0004470; F:malic enzyme activity; IBA:GO_Central.
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 GO; GO:0006094; P:gluconeogenesis; IMP:EcoCyc.
DR GO; GO:0006108; P:malate metabolic process; IBA:GO_Central.
DR GO; GO:0006090; P:pyruvate metabolic process; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; Metal-binding; NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..565
FT /note="NAD-dependent malic enzyme"
FT /id="PRO_0000160215"
FT ACT_SITE 104
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 175
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 157
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 246
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 247
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 270
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 270
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 418
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT SITE 270
FT /note="Important for activity"
FT /evidence="ECO:0000250"
FT STRAND 11..13
FT /evidence="ECO:0007829|PDB:6AGS"
FT HELIX 17..21
FT /evidence="ECO:0007829|PDB:6AGS"
FT TURN 24..26
FT /evidence="ECO:0007829|PDB:6AGS"
FT HELIX 29..31
FT /evidence="ECO:0007829|PDB:6AGS"
FT HELIX 34..39
FT /evidence="ECO:0007829|PDB:6AGS"
FT HELIX 53..65
FT /evidence="ECO:0007829|PDB:6AGS"
FT HELIX 70..81
FT /evidence="ECO:0007829|PDB:6AGS"
FT HELIX 85..93
FT /evidence="ECO:0007829|PDB:6AGS"
FT HELIX 96..103
FT /evidence="ECO:0007829|PDB:6AGS"
FT HELIX 107..113
FT /evidence="ECO:0007829|PDB:6AGS"
FT HELIX 115..118
FT /evidence="ECO:0007829|PDB:6AGS"
FT STRAND 124..128
FT /evidence="ECO:0007829|PDB:6AGS"
FT HELIX 129..131
FT /evidence="ECO:0007829|PDB:6AGS"
FT HELIX 135..140
FT /evidence="ECO:0007829|PDB:6AGS"
FT STRAND 149..153
FT /evidence="ECO:0007829|PDB:6AGS"
FT TURN 159..161
FT /evidence="ECO:0007829|PDB:6AGS"
FT HELIX 165..169
FT /evidence="ECO:0007829|PDB:6AGS"
FT HELIX 170..183
FT /evidence="ECO:0007829|PDB:6AGS"
FT HELIX 187..189
FT /evidence="ECO:0007829|PDB:6AGS"
FT STRAND 190..196
FT /evidence="ECO:0007829|PDB:6AGS"
FT HELIX 202..205
FT /evidence="ECO:0007829|PDB:6AGS"
FT HELIX 220..237
FT /evidence="ECO:0007829|PDB:6AGS"
FT STRAND 242..245
FT /evidence="ECO:0007829|PDB:6AGS"
FT HELIX 250..260
FT /evidence="ECO:0007829|PDB:6AGS"
FT TURN 261..263
FT /evidence="ECO:0007829|PDB:6AGS"
FT STRAND 264..268
FT /evidence="ECO:0007829|PDB:6AGS"
FT TURN 269..271
FT /evidence="ECO:0007829|PDB:6AGS"
FT HELIX 272..288
FT /evidence="ECO:0007829|PDB:6AGS"
FT STRAND 289..291
FT /evidence="ECO:0007829|PDB:6AGS"
FT TURN 293..295
FT /evidence="ECO:0007829|PDB:6AGS"
FT STRAND 298..301
FT /evidence="ECO:0007829|PDB:6AGS"
FT HELIX 305..319
FT /evidence="ECO:0007829|PDB:6AGS"
FT TURN 320..322
FT /evidence="ECO:0007829|PDB:6AGS"
FT HELIX 325..330
FT /evidence="ECO:0007829|PDB:6AGS"
FT STRAND 332..335
FT /evidence="ECO:0007829|PDB:6AGS"
FT STRAND 337..339
FT /evidence="ECO:0007829|PDB:6AGS"
FT HELIX 350..353
FT /evidence="ECO:0007829|PDB:6AGS"
FT HELIX 359..362
FT /evidence="ECO:0007829|PDB:6AGS"
FT HELIX 374..381
FT /evidence="ECO:0007829|PDB:6AGS"
FT STRAND 384..388
FT /evidence="ECO:0007829|PDB:6AGS"
FT HELIX 398..405
FT /evidence="ECO:0007829|PDB:6AGS"
FT STRAND 412..415
FT /evidence="ECO:0007829|PDB:6AGS"
FT HELIX 420..422
FT /evidence="ECO:0007829|PDB:6AGS"
FT HELIX 427..432
FT /evidence="ECO:0007829|PDB:6AGS"
FT TURN 433..436
FT /evidence="ECO:0007829|PDB:6AGS"
FT STRAND 439..444
FT /evidence="ECO:0007829|PDB:6AGS"
FT STRAND 449..451
FT /evidence="ECO:0007829|PDB:6AGS"
FT STRAND 454..456
FT /evidence="ECO:0007829|PDB:6AGS"
FT HELIX 463..465
FT /evidence="ECO:0007829|PDB:6AGS"
FT HELIX 467..477
FT /evidence="ECO:0007829|PDB:6AGS"
FT HELIX 484..496
FT /evidence="ECO:0007829|PDB:6AGS"
FT HELIX 499..502
FT /evidence="ECO:0007829|PDB:6AGS"
FT STRAND 503..506
FT /evidence="ECO:0007829|PDB:6AGS"
FT HELIX 512..514
FT /evidence="ECO:0007829|PDB:6AGS"
FT HELIX 515..532
FT /evidence="ECO:0007829|PDB:6AGS"
FT HELIX 541..550
FT /evidence="ECO:0007829|PDB:6AGS"
FT STRAND 560..562
FT /evidence="ECO:0007829|PDB:6AGS"
SQ SEQUENCE 565 AA; 63197 MW; FFD61212F709EE3A CRC64;
MEPKTKKQRS LYIPYAGPVL LEFPLLNKGS AFSMEERRNF NLLGLLPEVV ETIEEQAERA
WIQYQGFKTE IDKHIYLRNI QDTNETLFYR LVNNHLDEMM PVIYTPTVGA ACERFSEIYR
RSRGVFISYQ NRHNMDDILQ NVPNHNIKVI VVTDGERILG LGDQGIGGMG IPIGKLSLYT
ACGGISPAYT LPVVLDVGTN NQQLLNDPLY MGWRNPRITD DEYYEFVDEF IQAVKQRWPD
VLLQFEDFAQ KNAMPLLNRY RNEICSFNDD IQGTAAVTVG TLIAASRAAG GQLSEKKIVF
LGAGSAGCGI AEMIISQTQR EGLSEEAARQ KVFMVDRFGL LTDKMPNLLP FQTKLVQKRE
NLSDWDTDSD VLSLLDVVRN VKPDILIGVS GQTGLFTEEI IREMHKHCPR PIVMPLSNPT
SRVEATPQDI IAWTEGNALV ATGSPFNPVV WKDKIYPIAQ CNNAFIFPGI GLGVIASGAS
RITDEMLMSA SETLAQYSPL VLNGEGMVLP ELKDIQKVSR AIAFAVGKMA QQQGVAVKTS
AEALQQAIDD NFWQAEYRDY RRTSI
