MAOH_NEOFR
ID MAOH_NEOFR Reviewed; 592 AA.
AC P78715;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Malic enzyme, hydrogenosomal;
DE Short=ME;
DE EC=1.1.1.40;
DE Flags: Precursor;
OS Neocallimastix frontalis (Rumen fungus).
OC Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC Chytridiomycota incertae sedis; Neocallimastigomycetes; Neocallimastigales;
OC Neocallimastigaceae; Neocallimastix.
OX NCBI_TaxID=4757;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=L2;
RX PubMed=9004216; DOI=10.1046/j.1365-2958.1997.1891553.x;
RA van der Giezen M., Rechinger K.B., Svendsen I., Durand R., Hirt R.P.,
RA Fevre M., Embley T.M., Prins R.A.;
RT "A mitochondrial-like targeting signal on the hydrogenosomal malic enzyme
RT from the anaerobic fungus Neocallimastix frontalis: support for the
RT hypothesis that hydrogenosomes are modified mitochondria.";
RL Mol. Microbiol. 23:11-21(1997).
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 -!- SUBCELLULAR LOCATION: Hydrogenosome.
CC -!- SIMILARITY: Belongs to the malic enzymes family. {ECO:0000305}.
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DR EMBL; U62041; AAC49572.1; -; mRNA.
DR AlphaFoldDB; P78715; -.
DR SMR; P78715; -.
DR PRIDE; P78715; -.
DR GO; GO:0042566; C:hydrogenosome; 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; 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 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 Direct protein sequencing; Hydrogenosome; Metal-binding; NADP;
KW Oxidoreductase; Transit peptide.
FT TRANSIT 1..27
FT /note="Hydrogenosome"
FT CHAIN 28..592
FT /note="Malic enzyme, hydrogenosomal"
FT /id="PRO_0000018549"
FT ACT_SITE 134
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 205
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 182..205
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 187
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 276
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 277
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 300
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 300
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 335..352
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 443
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT SITE 300
FT /note="Important for activity"
FT /evidence="ECO:0000250"
SQ SEQUENCE 592 AA; 65546 MW; 5BB891C4FDA127BF CRC64;
MLAPIQTIAR PVSSILPATG ALAAKRTFFA PSEVYNKKQV IVTKKTGLDI LNDPKLNKGS
AFTADEKDRL GIRGLVPPRP QSLEAQYKRC KTNLDKISDP LEKFIYLNHL QNRNETLYYK
MILENFVELA PIIYTPVVGE ACQKFHKIFT QTRGMYFSTA DRGQMSAVAA NWPYDDVDVI
VVTDGSRILG LGDLGAGGMQ IPIGKLTLYV CGGGINPRNV LPIVLDVGTN NKELLNDPLY
LGMQHPRLQG EEFHAFVDEW VSAITDRFPK AVIQFEDFMM PNALDLLLKY KDQICMFNDD
IQSTGAITLA SVLATMRARG GTFADIKKET FLCLGAGSSG VGVCETIVDC IVAEGATREE
AYAQFYMFDH KGLLGKGRDD LLPSQQVFMR KEIEGGKTPA ELLKKIKPTC LLGLSTCPKL
FNKEMLSYVA SYCEKPGIFP LSNPTSRSEC TAEEAVEFTD GNLIFASGSP FDPVEWKGKT
IQTNQCNNSY SFPGIGLGLV SSRATRVPFE TFQVCARVIA SLGTPEMLAT GKIFPDLDNL
RAVSLEVGIE VAKMAERMNI ATQFPPKGMD WREWLKHNMW QPEYPHIVVK NL
