ID MAO2_RICPR Reviewed; 767 AA.
AC Q9ZDF6;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 27-NOV-2024, entry version 121.
DE RecName: Full=Probable NADP-dependent malic enzyme;
DE Short=NADP-ME;
DE EC=1.1.1.40;
GN OrderedLocusNames=RP373;
OS Rickettsia prowazekii (strain Madrid E).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX NCBI_TaxID=272947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Madrid E;
RX PubMed=9823893; DOI=10.1038/24094;
RA Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T.,
RA Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H.,
RA Kurland C.G.;
RT "The genome sequence of Rickettsia prowazekii and the origin of
RT mitochondria.";
RL Nature 396:133-140(1998).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-malate + NADP(+) = pyruvate + CO2 + NADPH;
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=oxaloacetate + H(+) = pyruvate + CO2; 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; 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 -!- 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; AJ235271; CAA14832.1; -; Genomic_DNA.
DR PIR; F71694; F71694.
DR RefSeq; NP_220756.1; NC_000963.1.
DR RefSeq; WP_004597525.1; NC_000963.1.
DR AlphaFoldDB; Q9ZDF6; -.
DR SMR; Q9ZDF6; -.
DR STRING; 272947.gene:17555453; -.
DR EnsemblBacteria; CAA14832; CAA14832; CAA14832.
DR KEGG; rpr:RP373; -.
DR PATRIC; fig|272947.5.peg.384; -.
DR eggNOG; COG0280; Bacteria.
DR eggNOG; COG0281; Bacteria.
DR HOGENOM; CLU_012366_0_0_5; -.
DR OrthoDB; 9805787at2; -.
DR Proteomes; UP000002480; Chromosome.
DR GO; GO:0016746; F:acyltransferase 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 FunFam; 3.40.50.10380:FF:000003; NADP-dependent malic enzyme; 1.
DR FunFam; 3.40.50.720:FF:000095; NADP-dependent malic enzyme; 1.
DR Gene3D; 3.40.50.10950; -; 1.
DR Gene3D; 3.40.50.10750; Isocitrate/Isopropylmalate dehydrogenase-like; 1.
DR Gene3D; 3.40.50.10380; Malic enzyme, N-terminal domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR046346; Aminoacid_DH-like_N_sf.
DR InterPro; IPR051674; Malate_Decarboxylase.
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 PANTHER; PTHR43237; NADP-DEPENDENT MALIC ENZYME; 1.
DR PANTHER; PTHR43237:SF4; NADP-DEPENDENT MALIC ENZYME; 1.
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; SSF53223; Aminoacid dehydrogenase-like, N-terminal domain; 1.
DR SUPFAM; SSF53659; Isocitrate/Isopropylmalate dehydrogenase-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00331; MALIC_ENZYMES; 1.
PE 3: Inferred from homology;
KW Metal-binding; Multifunctional enzyme; NADP; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..767
FT /note="Probable NADP-dependent malic enzyme"
FT /id="PRO_0000160247"
FT REGION 1..430
FT /note="Malic enzyme"
FT REGION 431..767
FT /note="Phosphate acetyltransferase"
FT ACT_SITE 42
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P40927"
FT ACT_SITE 97
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P40927"
FT BINDING 139
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P40927"
FT BINDING 140
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P40927"
FT BINDING 165
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P40927"
FT BINDING 198..201
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P40927"
FT BINDING 290
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P40927"
FT BINDING 322
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P40927"
SQ SEQUENCE 767 AA; 84253 MW; 6782D33C85E30A5E CRC64;
MDEMNKINYT EALEYHEKDK PGKIAITTTK SLVTQQDLSL AYSPGVAAPC LEISKNLEAV
YKYTSRSNLV AVISNGTAVL GLGNLGAAAS KPVMEGKAVL FKKFADIDAI DLEVNTEDPI
EFINAVKYLG YSFGGINLED IKAPECFLIE EKLKSLMDIP VFHDDQHGTA IITAAGLINA
AYLTNRTLKD LKIVINGAGA AAIACIDLLI ALGVDKSKII LCDTKGVIYK GRTSGMNKWK
ERYASDTKIR TLTESLNNAD VFIGLSVKGA VTKDMISKMA HKPIIFAMAN PDPEITPEDI
KFVRDDAIIA TGRSDYNNQV NNVMGFPYIF RGALDVRAST INTEMKIAAA RAIADLARRP
VPEEVYKAYS GRKMVFGNEY IIPVPFDPRL ITVVATAVAV AAIESGVARV KDFSIDKYKQ
QLGSRLNPTA NYMNFLAEKI HNVPLKRIVF AEGEEEEVIS AALMMRDEKY GNPIIIGRVE
RIEVTLKKIG KDISLAGIQI MNAALSDRLE QYTDYLYKRL QRKGYLYRDC AKLVKTDKNI
FAACMVACGD GDALLTGVTK SYIDSLEDII KVISPKQNRR ILGYSIMIAK DHNIIIADNC
ITEYPNSLEL AQIATQTAEI AKNMGITPRV ALIAFSTFGN SSQEKTVRIR EAVNILDNFS
KDKKKLNGIK VDFEYDGEMS VKVALDHDLR KLYQFCRLSG SANVLIMPGL NSAAISTELL
QKFSSNSFIG PITNGFAKPV QILPTTATAN EILKIATFAC VEAIKEV
//
