MAOX_SCHPO
ID MAOX_SCHPO Reviewed; 565 AA.
AC P40375; A1EGU1;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=NAD-dependent malic enzyme;
DE Short=NAD-ME;
DE EC=1.1.1.38;
GN Name=mae2; ORFNames=SPCC794.12c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=7941746; DOI=10.1002/yea.320100506;
RA Viljoen M., Subden R.E., Krizus A., van Vuuren H.J.J.;
RT "Molecular analysis of the malic enzyme gene (mae2) of Schizosaccharomyces
RT pombe.";
RL Yeast 10:613-624(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Li A., Su X., Zhang W.;
RT "Sequencing and analysis of malate degradation related enzyme gene from
RT Schizosaccharomyces pombe.";
RL Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-445, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
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=1.1.1.38;
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=1.1.1.38;
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: Belongs to the malic enzymes family. {ECO:0000305}.
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DR EMBL; U00621; AAA18985.1; -; Genomic_DNA.
DR EMBL; EF125016; ABL67725.1; -; Genomic_DNA.
DR EMBL; CU329672; CAA19139.1; -; Genomic_DNA.
DR PIR; S44330; S44330.
DR RefSeq; NP_587760.1; NM_001022753.2.
DR AlphaFoldDB; P40375; -.
DR SMR; P40375; -.
DR BioGRID; 276150; 7.
DR STRING; 4896.SPCC794.12c.1; -.
DR iPTMnet; P40375; -.
DR MaxQB; P40375; -.
DR PaxDb; P40375; -.
DR PRIDE; P40375; -.
DR EnsemblFungi; SPCC794.12c.1; SPCC794.12c.1:pep; SPCC794.12c.
DR GeneID; 2539592; -.
DR KEGG; spo:SPCC794.12c; -.
DR PomBase; SPCC794.12c; mae2.
DR VEuPathDB; FungiDB:SPCC794.12c; -.
DR eggNOG; KOG1257; Eukaryota.
DR HOGENOM; CLU_011405_5_2_1; -.
DR InParanoid; P40375; -.
DR OMA; QMWDPVY; -.
DR PhylomeDB; P40375; -.
DR PRO; PR:P40375; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005739; C:mitochondrion; ISS:PomBase.
DR GO; GO:0004471; F:malate dehydrogenase (decarboxylating) (NAD+) activity; IDA:PomBase.
DR GO; GO:0004470; F:malic enzyme activity; IBA:GO_Central.
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; IMP:PomBase.
DR GO; GO:0006090; P:pyruvate metabolic process; IMP:PomBase.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IC:PomBase.
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 1: Evidence at protein level;
KW Metal-binding; NAD; Oxidoreductase; Phosphoprotein; Reference proteome.
FT CHAIN 1..565
FT /note="NAD-dependent malic enzyme"
FT /id="PRO_0000160205"
FT ACT_SITE 103
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 177
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 248
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 249
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 272
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 272
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 419
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT SITE 272
FT /note="Important for activity"
FT /evidence="ECO:0000250"
FT MOD_RES 445
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 565 AA; 62535 MW; AF22D98E1BB72CA8 CRC64;
MPAGTKEQIE CPLKGVTLLN SPRYNKDTAF TPEERQKFEI SSRLPPIVET LQQQVDRCYD
QYKAIGDEPL QKNLYLSQLS VTNQTLFYAL ISQHLIEMIP IIYTPTEGDA IKQFSDIYRY
PEGCYLDIDH NDLSYIKQQL SEFGKSDSVE YIIITDSEGI LGIGDQGVGG VLISVAKGHL
MTLCAGLDPN RFLPIVLDVG TNNETHRKNH QYMGLRKDRV RGEQYDSFLD NVIKAIREVF
PEAFIHFEDF GLANAKRILD HYRPDIACFN DDIQGTGAVA LAAIIGALHV TKSPLTEQRI
MIFGAGTAGV GIANQIVAGM VTDGLSLDKA RGNLFMIDRC GLLLERHAKI ATDGQKPFLK
KDSDFKEVPS GDINLESAIA LVKPTILLGC SGQPGKFTEK AIREMSKHVE RPIIFPISNP
TTLMEAKPDQ IDKWSDGKAL IATGSPLPPL NRNGKKYVIS QCNNALLYPA LGVACVLSRC
KLLSDGMLKA ASDALATVPR SLFAADEALL PDLNNAREIS RHIVFAVLKQ AVSEGMSTVD
LPKDDAKLKE WIIEREWNPE YKPFV
