ID E1AZ90_9FUNG Unreviewed; 550 AA.
AC E1AZ90;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=Malic enzyme {ECO:0000256|RuleBase:RU003426};
OS Cunninghamella echinulata.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Cunninghamellaceae; Cunninghamella.
OX NCBI_TaxID=76405 {ECO:0000313|EMBL:ADM26561.1};
RN [1] {ECO:0000313|EMBL:ADM26561.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=MIAN6 {ECO:0000313|EMBL:ADM26561.1};
RA Wan X., Wu Y., Jiang M.;
RT "Characterization of a NADP+-dependent malic enzyme from an oleaginous
RT fungus Cunninghamella echinulata.";
RL Submitted (AUG-2010) 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}.
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; HQ116563; ADM26561.1; -; mRNA.
DR AlphaFoldDB; E1AZ90; -.
DR SMR; E1AZ90; -.
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 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 2: Evidence at transcript level;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR000106-3};
KW Oxidoreductase {ECO:0000256|RuleBase:RU003426}.
FT DOMAIN 65..246
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 256..514
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT ACT_SITE 88
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT ACT_SITE 160
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT BINDING 142
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT BINDING 231
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 232
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 255
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 401
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT BINDING 445
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
SQ SEQUENCE 550 AA; 61078 MW; FFCAE025232BF256 CRC64;
MPTVLTPYWS NGVQKLKVMP NAAPPPPRGL TPPVLDRSVH RIRCLNQLRS KDKNIEKYIY
LSQLKDADPN MFYKLCIENM SEITPLIYTP TVGDACIQYS HIFRRPEGLF VSIKDKGNVG
KVLRNWPRIN EARIAVVTDG SRILGLGDLG VNGMPISIGK LSLYVAGAGI RPSSTVPICI
DVGTDNKEFL EDPLYLGLRQ PRVPEAEMHE FMEEFMHEMS VVFPELLIQF EDFATDKAFA
FLSSFRDRYP LFNDDIQGTG AVVLSGFLNA AKLSSAASGR PLTDHRILFL GAGSAGVGVG
MQLMSFFKLQ GMSEQEARER IWLVDSQGLV YDARGKLAEH KKFFSRKDYA GSPMTNLVDI
IDYVKPTALL GLSTIKGAFN QQVVEKMSEL NERPIIFPLS NPVRLSECEF DEAVQWSNGN
VIFASGSPFP EQQFAGRMLY PGQGNNMYVF PGIGLGAILS RVSSVTDSMI EAASLGLANS
LTDEERGLEL VYPRIERIRD ISAQIALSVI RAAQKANVDR SPHLRQLDDS ALVKHIMGKM
WNPQDTMSHL
//
