MAO2_RHIME
ID MAO2_RHIME Reviewed; 761 AA.
AC O30808;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=NADP-dependent malic enzyme;
DE Short=NADP-ME;
DE EC=1.1.1.40;
GN Name=tme; OrderedLocusNames=R00394; ORFNames=SMc01126;
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 -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-malate + NADP(+) = CO2 + NADPH + pyruvate;
CC Xref=Rhea:RHEA:18253, ChEBI:CHEBI:15361, ChEBI:CHEBI:15589,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.40;
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=1.1.1.40;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Note=Divalent metal cations. Prefers magnesium or manganese.;
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}.
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DR EMBL; AF017444; AAB82460.1; -; Genomic_DNA.
DR EMBL; AL591688; CAC41831.1; -; Genomic_DNA.
DR RefSeq; NP_384500.1; NC_003047.1.
DR RefSeq; WP_010968547.1; NC_003047.1.
DR AlphaFoldDB; O30808; -.
DR SMR; O30808; -.
DR STRING; 266834.SMc01126; -.
DR PRIDE; O30808; -.
DR EnsemblBacteria; CAC41831; CAC41831; SMc01126.
DR GeneID; 61601873; -.
DR KEGG; sme:SMc01126; -.
DR PATRIC; fig|266834.11.peg.1767; -.
DR eggNOG; COG0280; Bacteria.
DR eggNOG; COG0281; Bacteria.
DR HOGENOM; CLU_012366_0_0_5; -.
DR OMA; VDEFINC; -.
DR Proteomes; UP000001976; Chromosome.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR GO; GO:0004471; F:malate dehydrogenase (decarboxylating) (NAD+) activity; IEA:InterPro.
DR GO; GO:0004473; F:malate dehydrogenase (decarboxylating) (NADP+) 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 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 Metal-binding; Multifunctional enzyme; NADP; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..761
FT /note="NADP-dependent malic enzyme"
FT /id="PRO_0000160246"
FT REGION 1..437
FT /note="Malic enzyme"
FT REGION 438..761
FT /note="Phosphate acetyltransferase"
FT ACT_SITE 49
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P40927"
FT ACT_SITE 104
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P40927"
FT BINDING 146
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P40927"
FT BINDING 147
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P40927"
FT BINDING 172
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P40927"
FT BINDING 205..208
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P40927"
FT BINDING 297
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P40927"
FT BINDING 329
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P40927"
FT CONFLICT 228
FT /note="L -> F (in Ref. 1; AAB82460)"
FT /evidence="ECO:0000305"
FT CONFLICT 609..636
FT /note="DMPTSEELADIAEEAAGLAKRLGYVPRV -> KHADLRGAG (in Ref.
FT 1; AAB82460)"
FT /evidence="ECO:0000305"
FT CONFLICT 761
FT /note="T -> TRRGSAESRKTAGTSSVAASPDG (in Ref. 1; AAB82460)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 761 AA; 82209 MW; A342A5F41F39DBC7 CRC64;
MPGIDKTDRA MTSVTAQEAL DFHSQGRPGK LEISPTKPMA TQRDLSLAYS PGVAVPVKAI
ADDPATAYDY TARGNMVAVI SNGTAILGLG NLGALASKPV MEGKAVLFKR FADVDSIDLE
VDTENVDEFV NCVRFLGPSF GGINLEDIKA PDCFIIEQRL REVMDIPVFH DDQHGTAIIA
AAGLVNALTL TGRDFKTAKL VCNGAGAAAI ACIELIKAMG FNPENIILCD TKGVIYKGRT
DGMNQWKSAH AVETDRRTLA EALDGADVFF GLSAKGALSA DMVRSMGARP IIFAMANPDP
EITPEEVALI RDDAIVATGR SDYPNQVNNV LGFPYIFRGA LDVRASTIND AMKIAAAEAL
ANLAKEDVPD DVAAAYQGNR PRFGPQYIIP VPFDPRLISA IPMAVAKAAM ETGVARKPIE
DLKAYGQQLS ARRDPIASTL QRIVERVRRQ PKRIVFAEGE EVQMMRSAIA YANQQLGTAL
LLGREEVMRE TAEREGIDLD RAGIQIVNAR LSKRVGAYTD FLYSRLQRKG YLFRDVQRLI
NTDRNHFAAS MVALGDADGM VTGLTRNYST ALEDVRRCID PKPGHRVIGV SIALCRGRTV
LVADTAVHDM PTSEELADIA EEAAGLAKRL GYVPRVAMLA YSTFGHPSGE RSERVREAVK
ILDRRRVDFE YDGEMAADVA LNARVMEQYP FCRLSGTANV LVMPAFHSAS ISTKMLQELG
GSTVIGPLLV GLDKSVQIAS MSAKDSDLVN LAAIAAYNAG T
