MAO2_SALTY
ID MAO2_SALTY Reviewed; 759 AA.
AC Q9ZFV8;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 13-DEC-2001, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=NADP-dependent malic enzyme;
DE Short=NADP-ME;
DE EC=1.1.1.40;
GN Name=maeB; OrderedLocusNames=STM2472;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 610-759.
RC STRAIN=LT2;
RX PubMed=10464203; DOI=10.1128/jb.181.17.5317-5329.1999;
RA Kofoid E.C., Rappleye C.A., Stojiljkovic I., Roth J.R.;
RT "The 17-gene ethanolamine (eut) operon of Salmonella typhimurium encodes
RT five homologues of carboxysome shell proteins.";
RL J. Bacteriol. 181:5317-5329(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; 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; AE006468; AAL21366.1; -; Genomic_DNA.
DR EMBL; AF093749; AAC78109.1; -; Genomic_DNA.
DR RefSeq; NP_461407.1; NC_003197.2.
DR RefSeq; WP_000344297.1; NC_003197.2.
DR AlphaFoldDB; Q9ZFV8; -.
DR SMR; Q9ZFV8; -.
DR STRING; 99287.STM2472; -.
DR PaxDb; Q9ZFV8; -.
DR EnsemblBacteria; AAL21366; AAL21366; STM2472.
DR GeneID; 1253994; -.
DR KEGG; stm:STM2472; -.
DR PATRIC; fig|99287.12.peg.2610; -.
DR HOGENOM; CLU_012366_0_0_6; -.
DR OMA; NIWVTDL; -.
DR PhylomeDB; Q9ZFV8; -.
DR BioCyc; SENT99287:STM2472-MON; -.
DR Proteomes; UP000001014; 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 3: Inferred from homology;
KW Metal-binding; Multifunctional enzyme; NADP; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..759
FT /note="NADP-dependent malic enzyme"
FT /id="PRO_0000160244"
FT REGION 1..428
FT /note="Malic enzyme"
FT REGION 429..759
FT /note="Phosphate acetyltransferase"
FT ACT_SITE 39
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P40927"
FT ACT_SITE 94
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P40927"
FT BINDING 136
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P40927"
FT BINDING 137
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P40927"
FT BINDING 162
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P40927"
FT BINDING 195..198
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P40927"
FT BINDING 288
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P40927"
FT BINDING 320
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P40927"
FT CONFLICT 610
FT /note="A -> G (in Ref. 2; AAC78109)"
FT /evidence="ECO:0000305"
FT CONFLICT 613
FT /note="A -> P (in Ref. 2; AAC78109)"
FT /evidence="ECO:0000305"
FT CONFLICT 621
FT /note="R -> H (in Ref. 2; AAC78109)"
FT /evidence="ECO:0000305"
FT CONFLICT 626
FT /note="E -> G (in Ref. 2; AAC78109)"
FT /evidence="ECO:0000305"
FT CONFLICT 635
FT /note="S -> C (in Ref. 2; AAC78109)"
FT /evidence="ECO:0000305"
FT CONFLICT 643
FT /note="L -> P (in Ref. 2; AAC78109)"
FT /evidence="ECO:0000305"
FT CONFLICT 679
FT /note="R -> C (in Ref. 2; AAC78109)"
FT /evidence="ECO:0000305"
FT CONFLICT 754
FT /note="A -> G (in Ref. 2; AAC78109)"
FT /evidence="ECO:0000305"
FT CONFLICT 757
FT /note="T -> Q (in Ref. 2; AAC78109)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 759 AA; 82322 MW; D5120B020158EF18 CRC64;
MDEQLKQSAL DFHEFPVPGK IQVSPTKPLA TQRDLALAYS PGVAAPCLEI EKDPLAAYKY
TARGNLVAVI SNGTAVLGLG NIGALAGKPV MEGKGVLFKK FAGIDVFDIE VDELDPDKFI
NVVAALEPTF GGINLEDIKA PECFYIEQKL RERMNIPVFH DDQHGTAIIS TAAILNGLRV
VEKNISDVRM VVSGAGAAAI ACMNLLVALG MQKHNIVVCD SKGVIYKGRE PNMAETKAAY
AVDDSGKRTL DEVIDGADIF LGCSGPKVLT QEMVKKMARA PMILALANPE PEILPPLAKE
VRPDAIICTG RSDYPNQVNN VLCFPFIFRG ALDVGATAIN EEMKLAAVRA IAELAHAEQS
EVVASAYGDQ DLSFGPEYII PKPFDPRLIV KIAPAVAKAA MDSGVATRPI ADFDAYIDKL
TEFVYKTNLF MKPIFSQARK DPKRVVLPEG EEARVLHATQ ELITLGLAKP ILIGRPSVIE
MRIQKLGLQI KAGVDFEIVN NESDPRFKEY WSEYYQIMKR RGITQEQAQR AMIGNHTAIG
AIMVQRGEAD AMICGTIGDY HEHFSVVKAV FGYRDGVHTA GAMNALLLPS GNTFIADTYV
NEDPTPEQLA EIAVMAAETV RRFGIEPKVA LLSHSNFGSS NSLSASKMRE TLERVRERAP
DLMIDGEMHG DAALVESIRN DRMPDSPLKG AANILVMPNM EAARISYNLL RVSSSEGVTV
GPVLMGVSKP VHVLTPIASV RRIVNMVALA VVEAQTTPL
