MAOX_DICDI
ID MAOX_DICDI Reviewed; 544 AA.
AC Q6TU48; Q559J5; Q7KWU9;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=NADP-dependent malic enzyme;
DE Short=NADP-ME;
DE EC=1.1.1.40;
DE AltName: Full=SrfA-induced gene A protein;
GN Name=malA; Synonyms=sigA; ORFNames=DDB_G0272524;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND INDUCTION.
RC STRAIN=AX4;
RX PubMed=14665466; DOI=10.1128/ec.2.6.1327-1335.2003;
RA Escalante R., Moreno N., Sastre L.;
RT "Dictyostelium discoideum developmentally regulated genes whose expression
RT is dependent on MADS box transcription factor SrfA.";
RL Eukaryot. Cell 2:1327-1335(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=12097910; DOI=10.1038/nature00847;
RA Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA Noegel A.A.;
RT "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL Nature 418:79-85(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [4]
RP DEVELOPMENTAL STAGE, AND INDUCTION BY SRFA.
RX PubMed=15075287; DOI=10.1128/ec.3.2.564-566.2004;
RA Escalante R., Iranfar N., Sastre L., Loomis W.F.;
RT "Identification of genes dependent on the MADS box transcription factor
RT SrfA in Dictyostelium discoideum development.";
RL Eukaryot. Cell 3:564-566(2004).
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 -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in the fruiting body.
CC {ECO:0000269|PubMed:14665466}.
CC -!- DEVELOPMENTAL STAGE: Expressed at late stage of development (20 to 24
CC hours). {ECO:0000269|PubMed:14665466, ECO:0000269|PubMed:15075287}.
CC -!- INDUCTION: By cAMP and the MADS-box protein srfA.
CC {ECO:0000269|PubMed:14665466, ECO:0000269|PubMed:15075287}.
CC -!- SIMILARITY: Belongs to the malic enzymes 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; AY387644; AAQ95658.1; -; Genomic_DNA.
DR EMBL; AAFI02000008; EAL71186.1; -; Genomic_DNA.
DR RefSeq; XP_645111.1; XM_640019.1.
DR AlphaFoldDB; Q6TU48; -.
DR SMR; Q6TU48; -.
DR STRING; 44689.DDB0191268; -.
DR PaxDb; Q6TU48; -.
DR EnsemblProtists; EAL71186; EAL71186; DDB_G0272524.
DR GeneID; 8618505; -.
DR KEGG; ddi:DDB_G0272524; -.
DR dictyBase; DDB_G0272524; malA.
DR eggNOG; KOG1257; Eukaryota.
DR HOGENOM; CLU_011405_5_0_1; -.
DR InParanoid; Q6TU48; -.
DR OMA; GDACLQY; -.
DR PhylomeDB; Q6TU48; -.
DR Reactome; R-DDI-70268; Pyruvate metabolism.
DR Reactome; R-DDI-71403; Citric acid cycle (TCA cycle).
DR PRO; PR:Q6TU48; -.
DR Proteomes; UP000002195; Chromosome 2.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004471; F:malate dehydrogenase (decarboxylating) (NAD+) activity; IEA:InterPro.
DR GO; GO:0004473; F:malate dehydrogenase (decarboxylating) (NADP+) activity; ISS:dictyBase.
DR GO; GO:0004470; F:malic enzyme activity; ISS:dictyBase.
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; IBA:GO_Central.
DR GO; GO:0006090; P:pyruvate metabolic process; IBA:GO_Central.
DR Gene3D; 3.40.50.10380; -; 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; IPR001891; Malic_OxRdtase.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF00390; malic; 1.
DR Pfam; PF03949; Malic_M; 1.
DR PIRSF; PIRSF000106; ME; 1.
DR PRINTS; PR00072; MALOXRDTASE.
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 2: Evidence at transcript level;
KW Cytoplasm; Metal-binding; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..544
FT /note="NADP-dependent malic enzyme"
FT /id="PRO_0000328379"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 92
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 163
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 145
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 234
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 235
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 258
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 258
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 287..303
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 400
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT SITE 258
FT /note="Important for activity"
FT /evidence="ECO:0000250"
SQ SEQUENCE 544 AA; 60652 MW; EE9938C161E7198E CRC64;
MQNKPSFILR NPSANKGTGF NNEEREKLGL KGLLPPKVES LQEQSDRALS QFTSFNTNLE
RYIFLNCLRD RNETLFYYLL SNNLELMMPI IYTPTVGEAC QKFGNEFRFA QGMYFASQDK
GNIRAMMDNW PAEGVDIIVV SDGSRILGLG DLGTNGMGIP VGKLQLYVAG AGFCPTRTLP
VIIDSGTNTK KYLEDKYYLG ERHPRIPDSE YYPLVDEFLA AAFNKWPKVI VQFEDISNDH
CFNLLDEYRN KYLCFNDDIQ GTGSVILSGF INAVRSVQKP IKEHRMVFLG AGSAGIGVAD
CIMSLFDEAG VSKEEARKSF WFVDSKGLIT TTRGDELTSQ KKQYAREDYT YQLKSLLEVV
RDVKPTAIIG LSGIGGSFSQ EVIEEMAKHV EKPIVFALSN PTTNAECTAE QAYQWTDGRC
IFASGSPFKP VEYKGKTFVP GQGNNMYIFP GLGLAASVCE AKHVTDAMII TAAKTLASFV
EDSEVLTGKI YPGLQHIREI STRIAVKVIE KAYEEGMAQL PRPDNIEALV KSRQYVPSYD
KSKN
