ID A0A059LRH3_9CHLO Unreviewed; 601 AA.
AC A0A059LRH3;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Malic enzyme {ECO:0000256|RuleBase:RU003426};
GN ORFNames=H632_c101p1 {ECO:0000313|EMBL:KDD76796.1};
OS Helicosporidium sp. ATCC 50920.
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC Chlorellales; Chlorellaceae; Helicosporidium.
OX NCBI_TaxID=1291522 {ECO:0000313|EMBL:KDD76796.1, ECO:0000313|Proteomes:UP000026042};
RN [1] {ECO:0000313|EMBL:KDD76796.1, ECO:0000313|Proteomes:UP000026042}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 50920 {ECO:0000313|EMBL:KDD76796.1,
RC ECO:0000313|Proteomes:UP000026042};
RX PubMed=24809511;
RA Pombert J.F., Blouin N.A., Lane C., Boucias D., Keeling P.J.;
RT "A lack of parasitic reduction in the obligate parasitic green alga
RT helicosporidium.";
RL PLoS Genet. 10:E1004355-E1004355(2014).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|PIRSR:PIRSR000106-3};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|PIRSR:PIRSR000106-3};
CC Note=Divalent metal cations. Prefers magnesium or manganese.
CC {ECO:0000256|PIRSR:PIRSR000106-3};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SIMILARITY: Belongs to the malic enzymes family.
CC {ECO:0000256|ARBA:ARBA00008785, ECO:0000256|RuleBase:RU003426}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KDD76796.1}.
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DR EMBL; AYPS01000101; KDD76796.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A059LRH3; -.
DR STRING; 1291522.A0A059LRH3; -.
DR OrthoDB; 1069499at2759; -.
DR Proteomes; UP000026042; Unassembled WGS sequence.
DR GO; GO:0004470; F:malic enzyme activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0006108; P:malate metabolic process; IEA:UniProt.
DR CDD; cd05312; NAD_bind_1_malic_enz; 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; 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 PANTHER; PTHR23406; MALIC ENZYME-RELATED; 1.
DR PANTHER; PTHR23406:SF32; NAD-DEPENDENT MALIC ENZYME, MITOCHONDRIAL; 1.
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; SSF53223; Aminoacid dehydrogenase-like, N-terminal domain; 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 {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR000106-3};
KW Oxidoreductase {ECO:0000256|RuleBase:RU003426};
KW Reference proteome {ECO:0000313|Proteomes:UP000026042}.
FT DOMAIN 108..288
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 298..558
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT ACT_SITE 131
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT ACT_SITE 202
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT BINDING 184
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT BINDING 273
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 274
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 297
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 445
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT BINDING 489
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
SQ SEQUENCE 601 AA; 66461 MW; 2436D5168B9E4237 CRC64;
MRSKSFADLP SFPYTQREHT DVTSVRLRGS EILHNPVYNK GTAHSMMERE RLGLRGLLPP
RIMTLEQQMD KVMDQYWHGS DFIDPSQVSE GGITHEHTRK WTALTELQDR NETLFYRVLM
DNFVEMAPII YTPTVGWACM NFHKLYRRAR GMYFSALDRG MMGSMVHSWP QEDVDAIVIT
DGSRILGLGD LGCNGLGISV GKLDLYVAAG GFHPGRVLPC VVDVGTDNER LRQDPWYFGL
KQERLTGDAY YEIVDEAVRA LMHRWPRAVL QFEDFAMPHA GPLLERYRSQ HCVFNDDIQG
TACVAVAGLY GALRVQGQPP AALTQQRFVV VGAGSAGMGV AGMIAEAMVK QGLSLQQARE
RFYIVDHRGL VTQARPDLPP HVVPFARPPL PSDELGEGAQ LLSVVDAAKP TVLIGLAGAG
RLFSKDVLQS MARHNDRPIV FPMSNPTSKM ECTHEDAVTA TGGRAIFASG SPQPRVQLEG
RTHIPSQANN MYVFPGLALG AHLARSNRVT NDMLMSAAEA VPAFLSDHEL GLGLVYPNLN
AIREISVGVA ATVIKSAAEE GLLRNRKAAK ALDKGDEELQ TYIQSTMYYP EYSNLVYQKN
H
//
