ID Q875H8_MUCCI Unreviewed; 617 AA.
AC Q875H8;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 87.
DE RecName: Full=Malic enzyme {ECO:0000256|RuleBase:RU003426};
GN Name=mce {ECO:0000313|EMBL:AAO26053.1};
OS Mucor circinelloides (Mucor griseo-roseus).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Mucor.
OX NCBI_TaxID=36080 {ECO:0000313|EMBL:AAO26053.1};
RN [1] {ECO:0000313|EMBL:AAO26053.1}
RP NUCLEOTIDE SEQUENCE.
RA Li Y., Wynn J.P., Adams I.P., Ratledge C.;
RT "Cloning of a gene encoding malic enzyme from the oleaginous fungus, Mucor
RT circinelloides.";
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; AY209191; AAO26053.1; -; Genomic_DNA.
DR VEuPathDB; FungiDB:HMPREF1544_09848; -.
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 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}.
FT DOMAIN 114..294
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 304..581
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT ACT_SITE 137
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT ACT_SITE 208
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT BINDING 190
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT BINDING 279
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 280
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 303
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 465
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT BINDING 510
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
SQ SEQUENCE 617 AA; 68949 MW; 9071EB5B0571A73C CRC64;
MLSLKRIATT TKSNIFHRAL LAQRSYSYIN ANEYSDPRHD KNVHVMHSRG VNLLHDPLLS
KGTAFSIAER ERLSIRGLVP PRCQEMDKQL LRIKRNLDAC ETPLAKFVFL AALHDRNETL
YYKIIMEHLE ELAGIIYTPT VGLASQMSHS IYRRSRGMYF SSQDRGQMSA MVYNWPHDKV
DVIVVTDGSR VLGLGDLGAN GMEIPIGKLS LYVAAGGIRP RAVLPVVLDV GTNNQDLLND
PLYLGMSHPR LEGEEYYSFI DEWVTAITSR WPDTLIQFED FKYPHAYNLL AKYRNRITCF
NDDIQSTSSI TLAGILASLK SRGMSQEDLS NERIICVGAG SAGVGVCEGI IDCMVAQGRV
KSREEAYSKI YMLDQYGLLG NPGVHLPSDE EHGHPYQPRT TKLDDRQYCY VKHDLRDQMG
LEELVRKVKP TVLLGLTGIQ GVXSEEAVRE MAKHHERPVI FPLSNPDTHA ECTAEEAFKW
TDGRAIFASG SPFKDVELPN GKIGRTNQCN NSYSFPVSGL GXGITVSRAS RVTPNMFLET
ARTIADMATP SQLKEGILFP GVSQLREVAL NVGTRVCEVA FEEGYATAKL EEGEILSEVV
RSSAYQPEYV PLVYRDH
//
