ID A0A060SSC4_PYCCI Unreviewed; 480 AA.
AC A0A060SSC4;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Malic enzyme {ECO:0000256|RuleBase:RU003426};
GN ORFNames=BN946_scf184753.g20 {ECO:0000313|EMBL:CDO77270.1};
OS Pycnoporus cinnabarinus (Cinnabar-red polypore) (Trametes cinnabarina).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Polyporaceae; Trametes.
OX NCBI_TaxID=5643 {ECO:0000313|EMBL:CDO77270.1, ECO:0000313|Proteomes:UP000029665};
RN [1] {ECO:0000313|EMBL:CDO77270.1, ECO:0000313|Proteomes:UP000029665}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRFM137 {ECO:0000313|EMBL:CDO77270.1,
RC ECO:0000313|Proteomes:UP000029665};
RA Levasseur A., Lomascolo A., Ruiz-Duenas F.J., Uzan E., Piumi F., Kues U.,
RA Ram A.F.J., Murat C., Haon M., Benoit I., Arfi Y., Chevret D., Drula E.,
RA Kwon M.J., Gouret P., Lesage-Meessen L., Lombard V., Mariette J.,
RA Noirot C., Park J., Patyshakuliyeva A., Wieneger R.A.B., Wosten H.A.B.,
RA Martin F., Coutinho P.M., de Vries R., Martinez A.T., Klopp C.,
RA Pontarotti P., Henrissat B., Record E.;
RT "The genome of the white-rot fungus Pycnoporus cinnabarinus: a
RT basidiomycete model with a versatile arsenal for lignocellulosic biomass
RT breakdown.";
RL Submitted (JAN-2014) 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:CDO77270.1}.
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DR EMBL; CCBP010000447; CDO77270.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A060SSC4; -.
DR STRING; 5643.A0A060SSC4; -.
DR HOGENOM; CLU_011405_5_2_1; -.
DR OMA; QIVNHMV; -.
DR OrthoDB; 1069499at2759; -.
DR Proteomes; UP000029665; 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:0008152; P:metabolic process; IEA:UniProt.
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:UP000029665}.
FT DOMAIN 79..257
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 267..479
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT ACT_SITE 102
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT ACT_SITE 171
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT BINDING 152
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT BINDING 242
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 243
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 266
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 418
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT BINDING 463
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
SQ SEQUENCE 480 AA; 53579 MW; 3F381EC77B3A81E6 CRC64;
MSTAKNHVLR VALRGDSILT HPRFNKGTAF TLSERKAFGL TGRLPHRVNT LEEQCLRAYD
QLSTRPEPLR KNTFMQSLKD QNWVLYYGLL SRHVKELIPI IYTPTQGDAI ANYSHLFRRS
EGLYLTFPEQ DAMEEDFLNS PRDATSSSLS SRTLKQSWAS ATKGIGIATA KSAIYTLLGG
MDPSKTLPVV LDVGTDNQQL LDDPLYVGWP NKRIRGRAYD RFVDQFVQLV RKHYPHSLLH
FEDFGVGNAQ RLLDMYRNKH AVFNDDVQGT GAVTLAAMMS AVGVTKSRLS EQRYVVYGAG
TAGLGITKQL RDGIMSIDKL SREDANKRFF LLDRYGLIKE SLGPAKIRDA VREFVRPDAE
WEGVPTNAQG EVGLLEVVKK VKPTVLIGCS THAGAFSEEV VREMAKGVDR PIIFPLSNPS
RLVEVDPKDA NDWTDGKALM ATGSPFPPCQ MPNGKFYDIA ECNSAFPSAR RLLMSHKLIL
//
