MAO1_RHIME
ID MAO1_RHIME Reviewed; 770 AA.
AC O30807;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=NAD-dependent malic enzyme;
DE Short=NAD-ME;
DE EC=1.1.1.39;
GN Name=dme; OrderedLocusNames=R01837; ORFNames=SMc00169;
OS Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS meliloti).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=266834;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RC STRAIN=RCR2011 / SU47;
RX PubMed=9535928; DOI=10.1074/jbc.273.15.9330;
RA Mitsch M.J., Voegele R.T., Cowie A., Oesteras M., Finan T.M.;
RT "Chimeric structure of the NAD(P)+- and NADP+-dependent malic enzymes of
RT Rhizobium (Sinorhizobium) meliloti.";
RL J. Biol. Chem. 273:9330-9336(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11481430; DOI=10.1073/pnas.161294398;
RA Capela D., Barloy-Hubler F., Gouzy J., Bothe G., Ampe F., Batut J.,
RA Boistard P., Becker A., Boutry M., Cadieu E., Dreano S., Gloux S.,
RA Godrie T., Goffeau A., Kahn D., Kiss E., Lelaure V., Masuy D., Pohl T.,
RA Portetelle D., Puehler A., Purnelle B., Ramsperger U., Renard C.,
RA Thebault P., Vandenbol M., Weidner S., Galibert F.;
RT "Analysis of the chromosome sequence of the legume symbiont Sinorhizobium
RT meliloti strain 1021.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:9877-9882(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11474104; DOI=10.1126/science.1060966;
RA Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F.,
RA Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G.,
RA Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P.,
RA Cowie A., Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S.,
RA Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I.,
RA Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S.,
RA Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C.,
RA Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R.,
RA Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H.,
RA Wong K., Yeh K.-C., Batut J.;
RT "The composite genome of the legume symbiont Sinorhizobium meliloti.";
RL Science 293:668-672(2001).
RN [4]
RP CHARACTERIZATION.
RX PubMed=10407149; DOI=10.1016/s0167-4838(99)00112-0;
RA Voegele R.T., Mitsch M.J., Finan T.M.;
RT "Characterization of two members of a novel malic enzyme class.";
RL Biochim. Biophys. Acta 1432:275-285(1999).
CC -!- FUNCTION: Required for symbiotic nitrogen fixation. Plays a key role in
CC the conversion of malate to acetyl-CoA for efficient tricarboxylic acid
CC cycle function in nitrogen-fixating bacteria.
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=1.1.1.39;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Divalent metal cations. Prefers magnesium or manganese.
CC {ECO:0000250};
CC -!- ACTIVITY REGULATION: Subject to substrate inhibition and shows
CC allosteric regulation by acetyl-CoA.
CC -!- SUBUNIT: Homooctamer.
CC -!- SIMILARITY: In the N-terminal section; belongs to the malic enzymes
CC family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the phosphate
CC acetyltransferase and butyryltransferase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF017443; AAB82459.1; -; Genomic_DNA.
DR EMBL; AL591688; CAC46416.1; -; Genomic_DNA.
DR RefSeq; NP_385943.1; NC_003047.1.
DR RefSeq; WP_003534110.1; NC_003047.1.
DR AlphaFoldDB; O30807; -.
DR SMR; O30807; -.
DR STRING; 266834.SMc00169; -.
DR EnsemblBacteria; CAC46416; CAC46416; SMc00169.
DR GeneID; 61603308; -.
DR KEGG; sme:SMc00169; -.
DR PATRIC; fig|266834.11.peg.3280; -.
DR eggNOG; COG0280; Bacteria.
DR eggNOG; COG0281; Bacteria.
DR HOGENOM; CLU_012366_0_0_5; -.
DR OMA; NIWVTDL; -.
DR Proteomes; UP000001976; Chromosome.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
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:0006108; P:malate metabolic process; IEA:InterPro.
DR CDD; cd05311; NAD_bind_2_malic_enz; 1.
DR Gene3D; 3.40.50.10380; -; 1.
DR Gene3D; 3.40.50.10750; -; 1.
DR Gene3D; 3.40.50.10950; -; 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; IPR045213; Malic_NAD-bd_bact_type.
DR InterPro; IPR012188; ME_PTA.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR042113; P_AcTrfase_dom1.
DR InterPro; IPR042112; P_AcTrfase_dom2.
DR InterPro; IPR002505; PTA_PTB.
DR Pfam; PF00390; malic; 1.
DR Pfam; PF03949; Malic_M; 1.
DR Pfam; PF01515; PTA_PTB; 1.
DR PIRSF; PIRSF036684; ME_PTA; 1.
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 Allosteric enzyme; Metal-binding; Multifunctional enzyme; NAD;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..770
FT /note="NAD-dependent malic enzyme"
FT /id="PRO_0000160245"
FT REGION 1..440
FT /note="Malic enzyme"
FT REGION 441..770
FT /note="Phosphate acetyltransferase"
FT ACT_SITE 107
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 149
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 150
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 175
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 300
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
SQ SEQUENCE 770 AA; 82865 MW; 8FF3E3DA2D923108 CRC64;
MNTGDKAKSQ AVPASGDIDQ QALFFHRYPR PGKLEIQPTK PLGNQRDLAL AYSPGVAAPC
LAIKDNPETA ADFTARANLV AVVSNGTAVL GLGNIGPLAS KPVMEGKAVL FKKFAGIDVF
DIEIDAPTVD RMVDVISALE PTFGGINLED IKAPECFEVE RRLREKMEIP VFHDDQHGTA
IIVAAAVLNG LELAGKDIAE AKIVASGAGA AALACLNLLV TLGARRENIW VHDIEGLVYK
GREALMDEWK AVYAQESDNR VLADSIGGAD VFLGLSAAGV LKPELLARMA EKPLIMALAN
PTPEIMPEVA RAARPDAMIC TGRSDFPNQV NNVLCFPHIF RGALDCGART INEEMKMAAV
RAIAGLAREE PSDVAARAYS GETPVFGPDY LIPSPFDQRL ILRIAPAVAK AAAESGVATR
PIQDFDAYLD KLNRFVFRSG FIMKPVFAAA KNAAKNRVIF AEGEDERVLR AAQVLLEEGT
AKPILIGRPQ IIETRLRRYG LRIRPDVDFE VVNPEGDPRY RDYVDDYFAL VGRLGVIPEA
ARTIVRTNTT VIGALAVKRG EADALICGVE GRYSRHLRDV SQIIGKRSGV LDFSALSLLI
SQRGATFFTD TYVSFSPSAE EIAQTTVMAA NEIRRFGITP RAALVSHSNF GSRDSESAFK
MRTALQLVRE LAPDLEVDGE MHGDSAISEV LRQRVMPDST LNGEANLLVF PNLDAANITL
GVVKTMTDSL HVGPILLGSA LPAHILSPSV TSRGVVNMAA LAVVESSHPV
