MAO1_BACSU
ID MAO1_BACSU Reviewed; 439 AA.
AC P54572;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=NAD-dependent malic enzyme 1 {ECO:0000305};
DE Short=NAD-ME 1;
DE EC=1.1.1.38 {ECO:0000269|PubMed:16788182};
DE AltName: Full=Malate dehydrogenase MleA {ECO:0000305};
GN Name=mleA {ECO:0000303|PubMed:16788182}; Synonyms=yqkJ;
GN OrderedLocusNames=BSU23550;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / JH642;
RX PubMed=8969508; DOI=10.1099/13500872-142-11-3103;
RA Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M.,
RA Kobayashi Y.;
RT "Systematic sequencing of the 283 kb 210 degrees-232 degrees region of the
RT Bacillus subtilis genome containing the skin element and many sporulation
RT genes.";
RL Microbiology 142:3103-3111(1996).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 432-439.
RX PubMed=8501064; DOI=10.1128/jb.175.11.3607-3617.1993;
RA Smith K., Bayer M.E., Youngman P.;
RT "Physical and functional characterization of the Bacillus subtilis spoIIM
RT gene.";
RL J. Bacteriol. 175:3607-3617(1993).
RN [4]
RP DISCUSSION OF FUNCTION.
RX PubMed=10903309; DOI=10.1074/jbc.m001112200;
RA Wei Y., Guffanti A.A., Ito M., Krulwich T.A.;
RT "Bacillus subtilis YqkI is a novel malic/Na+-lactate antiporter that
RT enhances growth on malate at low protonmotive force.";
RL J. Biol. Chem. 275:30287-30292(2000).
RN [5]
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 [6]
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 [7]
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. Is
CC specific for NAD, cannot use NADP. Can also catalyze the
CC decarboxylation of oxaloacetate (PubMed:16788182). Involved in keeping
CC the ATP levels high (PubMed:23136871). {ECO:0000269|PubMed:16788182,
CC 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=1.56 mM for malate {ECO:0000269|PubMed:16788182};
CC KM=1 mM for NAD {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 slightly decrease in malate minimal medium. The mleA-
CC maeA-malS triple mutant shows a decrease in ATP concentrations by about
CC 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; D84432; BAA12645.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14287.1; -; Genomic_DNA.
DR EMBL; L06664; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; C69967; C69967.
DR RefSeq; NP_390236.1; NC_000964.3.
DR RefSeq; WP_004398731.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; P54572; -.
DR SMR; P54572; -.
DR STRING; 224308.BSU23550; -.
DR jPOST; P54572; -.
DR PaxDb; P54572; -.
DR PRIDE; P54572; -.
DR EnsemblBacteria; CAB14287; CAB14287; BSU_23550.
DR GeneID; 938725; -.
DR KEGG; bsu:BSU23550; -.
DR PATRIC; fig|224308.179.peg.2567; -.
DR eggNOG; COG0281; Bacteria.
DR InParanoid; P54572; -.
DR OMA; FMAYGVK; -.
DR PhylomeDB; P54572; -.
DR BioCyc; BSUB:BSU23550-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0004471; F:malate dehydrogenase (decarboxylating) (NAD+) activity; IEA:UniProtKB-EC.
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 Gene3D; 3.40.50.10380; -; 1.
DR InterPro; IPR002912; ACT_dom.
DR InterPro; IPR046346; Aminiacid_DH-like_N_sf.
DR InterPro; IPR006140; D-isomer_DH_NAD-bd.
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; PF02826; 2-Hacid_dh_C; 1.
DR Pfam; PF00390; malic; 1.
DR Pfam; PF03949; Malic_M; 1.
DR PIRSF; PIRSF000106; ME; 1.
DR SMART; SM01274; malic; 1.
DR SMART; SM00919; Malic_M; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF53223; SSF53223; 1.
DR PROSITE; PS51671; ACT; 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..439
FT /note="NAD-dependent malic enzyme 1"
FT /id="PRO_0000160208"
FT DOMAIN 9..84
FT /note="ACT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
FT ACT_SITE 112
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P40927"
FT ACT_SITE 167
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P40927"
FT BINDING 209
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P40927"
FT BINDING 210
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P40927"
FT BINDING 235
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P40927"
FT BINDING 268..271
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P40927"
FT BINDING 347
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P40927"
FT BINDING 373
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P40927"
SQ SEQUENCE 439 AA; 45890 MW; 2C6863E83CA86939 CRC64;
MIAKHMIRTL MIETPSVPGN LGRVATAIGL LGGDIGEVET VKVGPNYTMR NITVQVENEE
QLQEVIAAVQ ALGEGIRLHT VSDEVLSAHE GGKIQMKSKM PIRSLAELGR VYTPGVADVC
RLIEKEPEKA SIYTTISNSV AIVTDGTAIL GLGNIGSVAG MPVMEGKAAL FDQLAGISGI
PILLDTSDPE EIIKTVKHIS PGFSGILLED IGSPHCFEIE DRLKEELNIP VMHDDQHGTA
VVTLAAAISA CRSAGVDLKE AKVGQIGLGA AGVAICRMFM AYGVNAVYGT DKSESAMNRL
EQYGGQAVSS IEELMETCDI VIATTGVPGL IKPAFVRSGQ VILALSNPKP EIEPEAALQA
GAAYAADGRS VNNVLGFPGI FRGALNAKST EINHDMLVAA AEAIAACTKQ GDVVPQPLDS
KVHHAVAAAV EHAALTAVK
