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Database: UniProt
Entry: A0A1J7IRH4_9PEZI
LinkDB: A0A1J7IRH4_9PEZI
Original site: A0A1J7IRH4_9PEZI 
ID   A0A1J7IRH4_9PEZI        Unreviewed;       655 AA.
AC   A0A1J7IRH4;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=Malic enzyme {ECO:0008006|Google:ProtNLM};
GN   ORFNames=CONLIGDRAFT_575725 {ECO:0000313|EMBL:OIW30263.1};
OS   Coniochaeta ligniaria NRRL 30616.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Coniochaetales; Coniochaetaceae; Coniochaeta.
OX   NCBI_TaxID=1408157 {ECO:0000313|EMBL:OIW30263.1, ECO:0000313|Proteomes:UP000182658};
RN   [1] {ECO:0000313|EMBL:OIW30263.1, ECO:0000313|Proteomes:UP000182658}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 30616 {ECO:0000313|EMBL:OIW30263.1,
RC   ECO:0000313|Proteomes:UP000182658};
RG   DOE Joint Genome Institute;
RA   Jimenez D.J., Hector R.E., Riley R., Sun H., Grigoriev I.V.,
RA   Van Elsas J.D., Nichols N.N.;
RT   "Draft genome sequence of Coniochaeta ligniaria NRRL30616, a
RT   lignocellulolytic fungus for bioabatement of inhibitors in plant biomass
RT   hydrolysates.";
RL   Submitted (OCT-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   -!- SIMILARITY: Belongs to the malic enzymes family.
CC       {ECO:0000256|ARBA:ARBA00008785}.
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DR   EMBL; KV875097; OIW30263.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1J7IRH4; -.
DR   STRING; 1408157.A0A1J7IRH4; -.
DR   InParanoid; A0A1J7IRH4; -.
DR   OrthoDB; 1069499at2759; -.
DR   Proteomes; UP000182658; Unassembled WGS sequence.
DR   GO; GO:0004471; F:malate dehydrogenase (decarboxylating) (NAD+) activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0051287; F:NAD binding; 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; 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; NADP-DEPENDENT MALIC ENZYME; 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.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000106-3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000182658}.
FT   DOMAIN          164..344
FT                   /note="Malic enzyme N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01274"
FT   DOMAIN          354..619
FT                   /note="Malic enzyme NAD-binding"
FT                   /evidence="ECO:0000259|SMART:SM00919"
FT   REGION          1..48
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        187
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT   ACT_SITE        258
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT   BINDING         240
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT   BINDING         329
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT   BINDING         330
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT   BINDING         353
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT   BINDING         502
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT   BINDING         550
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
SQ   SEQUENCE   655 AA;  72871 MW;  298D09F72E2D4A07 CRC64;
     MAAYAYSTSS SDIPTPRSIS PSASVISGRS SQSSISNKRM SISSRRISAS NPMSSVDISA
     IEEAMKMATL DTHRGYAQNH YGQVQQYAKT EYISQNQAAG YQILREPLWN KGLSFTPEQR
     VARNLTGLLP HVMENLDKQC ERALRMIRSR QTNIDRYLYL STIKDQNVDL FYRLLIDNAK
     EMMPLVYTPT IGDVCLQYST LYTRPEALYI SIKQRKSIKT ILQNWPYPNP EICVVTDGSR
     ILGLGDLGVN GVGIPIGKLA LYTAAAGIHP EKTLPIVLDC GTANETNLKD PLYLGMRSKR
     IPVEEQQEFM DEFMEAAREV YPEMVVQFED FESEKAFNYL DRYRHTHKCF NDDIQGTGAV
     VLAGYIGAVN LSGVPLEEQR LVFMGAGSAG VGVAKQLVEY YTKRGLSEAA ARDKFWLVDT
     KGLVTKDRGD KLADHKKYFA RTDNNGHQFR TLEEVIEYVK PSALVGLTAT FGVFTESVVR
     ALKASVDAGG LGRRPILFPL SNPLTKAECT FEQAVQWTEG TVLFASGSPF SSFSVKTGDH
     IVTHHPNQGN NVYVFPGIGL GAILSKASKV TDNMIYTSAA SLAASLNADE IHKGLIYPRI
     ERVREASIIV AREVMKAARL DGVSTLPEEQ WIEWEEWGDV ALTKYIKERI YDPVI
//
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