ID A0A1Y2F1B2_9BASI Unreviewed; 549 AA.
AC A0A1Y2F1B2;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Malic enzyme {ECO:0000256|RuleBase:RU003426};
GN ORFNames=BCR35DRAFT_305399 {ECO:0000313|EMBL:ORY77633.1};
OS Leucosporidium creatinivorum.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Leucosporidiales; Leucosporidium.
OX NCBI_TaxID=106004 {ECO:0000313|EMBL:ORY77633.1, ECO:0000313|Proteomes:UP000193467};
RN [1] {ECO:0000313|EMBL:ORY77633.1, ECO:0000313|Proteomes:UP000193467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=62-1032 {ECO:0000313|EMBL:ORY77633.1,
RC ECO:0000313|Proteomes:UP000193467};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (JUL-2016) 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 -!- 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:ORY77633.1}.
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DR EMBL; MCGR01000031; ORY77633.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2F1B2; -.
DR STRING; 106004.A0A1Y2F1B2; -.
DR InParanoid; A0A1Y2F1B2; -.
DR OrthoDB; 1069499at2759; -.
DR Proteomes; UP000193467; 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 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:UP000193467}.
FT DOMAIN 60..255
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 261..516
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT ACT_SITE 83
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT ACT_SITE 165
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT BINDING 147
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT BINDING 236
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 237
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 260
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 403
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT BINDING 447
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
SQ SEQUENCE 549 AA; 59902 MW; 50F852122E906132 CRC64;
MSTNSNGIAQ QTKFAPSVGL PGGTEPTLVG SKEVLVGRAL ARLRSIPGDL EKYTFLASLK
SRNENIFYSL VGSHMKECTP LIYTPVIGLA CQNWSLIHPP PSTYQTPASA LYLSINDLPN
IGQILADLKT RVPKDEMEIS VVTDGSRVLG LGDLGVGGMG ISMGKLSLYV AAGGVNPKAT
LPIVLDFGTD NEKLLADPLY VGLRQRRLPD AECEAFVDVF MAEMHKTFPN MIIQFEDFHT
TLAFPLLFNN REKYPCFNDD IQGTGAVVLA GAIRAFALSE IPLKDQRILF FGAGSSGVGV
AETICKYFEK QGMTEEEAKA KFWLVDSRGL VAHNRGDTLP EHKRYLARSE SDAPKLKTLS
EVVEHVKPTA LLGLSTVGGT FTKEILQYMG KINKKPIVFA LSNPVKQAEC TFEQAVEGTG
GRVMYASGSP FDPVQFEGQK YEPGQGNNMY IFPGLGLGAI LAKVKSIPED LVHASAQALA
DSLTVEEKER NLLYPDVERI REVSMTIAVG VIRAAQKLNV DRNEELRGMN DAQLLAFVQN
QMYHPLLDL
//
