MAO3_BACSU
ID MAO3_BACSU Reviewed; 566 AA.
AC O34389;
DT 28-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=NAD-dependent malic enzyme 3 {ECO:0000305};
DE Short=NAD-ME 3;
DE EC=1.1.1.38 {ECO:0000269|PubMed:16788182};
DE AltName: Full=Malate dehydrogenase MalS {ECO:0000305};
GN Name=malS; OrderedLocusNames=BSU29880;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9387221; DOI=10.1099/00221287-143-11-3431;
RA Lapidus A., Galleron N., Sorokin A., Ehrlich S.D.;
RT "Sequencing and functional annotation of the Bacillus subtilis genes in the
RT 200 kb rrnB-dnaB region.";
RL Microbiology 143:3431-3441(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=168;
RX PubMed=16788182; DOI=10.1128/jb.00167-06;
RA Lerondel G., Doan T., Zamboni N., Sauer U., Aymerich S.;
RT "YtsJ has the major physiological role of the four paralogous malic enzyme
RT isoforms in Bacillus subtilis.";
RL J. Bacteriol. 188:4727-4736(2006).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=168;
RX PubMed=23136871; DOI=10.1111/1574-6968.12041;
RA Meyer F.M., Stuelke J.;
RT "Malate metabolism in Bacillus subtilis: distinct roles for three classes
RT of malate-oxidizing enzymes.";
RL FEMS Microbiol. Lett. 339:17-22(2013).
RN [5]
RP DISRUPTION PHENOTYPE.
RX PubMed=33824210; DOI=10.1128/mbio.03438-20;
RA Hoerl M., Fuhrer T., Zamboni N.;
RT "Bifunctional malic/malolactic enzyme provides a novel mechanism for NADPH-
RT balancing in Bacillus subtilis.";
RL MBio 12:0-0(2021).
CC -!- FUNCTION: Catalyzes the decarboxylation of malate to pyruvate. Can use
CC NAD and NADP, but with a strong preference for NAD. Can also catalyze
CC the decarboxylation of oxaloacetate (PubMed:16788182). Involved in
CC keeping the ATP levels high (PubMed:23136871).
CC {ECO:0000269|PubMed:16788182, ECO:0000269|PubMed:23136871}.
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:0000269|PubMed:16788182};
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 Evidence={ECO:0000269|PubMed:16788182};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P76558};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:P76558};
CC Note=Divalent metal cations. {ECO:0000250|UniProtKB:P76558};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.52 mM for malate {ECO:0000269|PubMed:16788182};
CC KM=5.5 mM for NAD {ECO:0000269|PubMed:16788182};
CC KM=7.3 mM for NADP {ECO:0000269|PubMed:16788182};
CC -!- INDUCTION: Weakly expressed in glucose or malate minimal medium.
CC {ECO:0000269|PubMed:16788182}.
CC -!- DISRUPTION PHENOTYPE: Mutant can use either a gluconeogenic carbon
CC source or glucose as efficiently as the wild-type strain
CC (PubMed:16788182). The ATP concentrations in the mutant grown in
CC minimal medium with glucose are similar to the wild-type level. ATP
CC concentrations decrease by about 10% in malate minimal medium. The
CC mleA-maeA-malS triple mutant shows a decrease in ATP concentrations by
CC about 20% and a moderate growth defect (PubMed:23136871). NADPH
CC overproduction is roughly halved in the deletion mutant
CC (PubMed:33824210). {ECO:0000269|PubMed:16788182,
CC ECO:0000269|PubMed:23136871, ECO:0000269|PubMed:33824210}.
CC -!- SIMILARITY: Belongs to the malic enzymes family. {ECO:0000305}.
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DR EMBL; AF008220; AAC00287.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14966.1; -; Genomic_DNA.
DR PIR; D69655; D69655.
DR RefSeq; NP_390866.1; NC_000964.3.
DR RefSeq; WP_003229258.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; O34389; -.
DR SMR; O34389; -.
DR IntAct; O34389; 1.
DR STRING; 224308.BSU29880; -.
DR PaxDb; O34389; -.
DR PRIDE; O34389; -.
DR EnsemblBacteria; CAB14966; CAB14966; BSU_29880.
DR GeneID; 938071; -.
DR KEGG; bsu:BSU29880; -.
DR PATRIC; fig|224308.179.peg.3246; -.
DR eggNOG; COG0281; Bacteria.
DR InParanoid; O34389; -.
DR OMA; QMWDPVY; -.
DR PhylomeDB; O34389; -.
DR BioCyc; BSUB:BSU29880-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004471; F:malate dehydrogenase (decarboxylating) (NAD+) activity; IEA:UniProtKB-EC.
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-EC.
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 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 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 Magnesium; Manganese; Metal-binding; NAD; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..566
FT /note="NAD-dependent malic enzyme 3"
FT /id="PRO_0000160210"
FT ACT_SITE 105
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P40927"
FT ACT_SITE 178
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P40927"
FT BINDING 249
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P40927"
FT BINDING 250
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P40927"
FT BINDING 273
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P40927"
FT BINDING 306..309
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P40927"
FT BINDING 423
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P40927"
FT BINDING 468
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P40927"
SQ SEQUENCE 566 AA; 62149 MW; 226C658154548270 CRC64;
MKQFRVTNEG DIQTTLRGLE VLSVPFLNKG VAFTEEERKE LGLKGFLPPK VLTIDDQAKR
AYEQYSAQPD DLSKNVYLTA LHDRNETLFY RLLNDHLGEM LPIVYTPTVG TAIQRYSHEY
RKPRGLYLSI DDPDGMKEAF KQYKDQSDTI DLIVATDAEG ILGIGDWGVG GIAISIGKLA
VYTAAAGIDP SRVLAVVLDA GTNQESLLND PLYVGNQHSR VRGERYDQFI DDYVALARET
FPNALLHWED FGAKNARSIL KRYKDKVCTF NDDIQGTGAV SLAAVLSCAK ASKVPLRDHR
VVIFGAGTAG IGIAEQLREA LVREGLSEEE SYKRFWCIDR NGLLTDDMDQ LLDFQKPYAR
SADEVKDYQR NGDGGGIDLL EVVRQAKPTI LIGTSTVSGA FTEEIVKEMA SHVKRPAILP
MSNPTTLSEA KPEDLIEWTE GRALITTGSP FPPVEYNGVT YHIGQANNAL VFPGLGLGTI
VTKSKLITDG MFEACARAIA GMVNVGVPGA PMLPKVEDLR TVSATVAVEV AKTAMKEGVA
TEEPEDIIQA VQDAMWYPVY KPIRAI
