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Database: UniProt
Entry: A0A080WI34_TRIRC
LinkDB: A0A080WI34_TRIRC
Original site: A0A080WI34_TRIRC 
ID   A0A080WI34_TRIRC        Unreviewed;       474 AA.
AC   A0A080WI34;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=Malic enzyme {ECO:0000256|RuleBase:RU003426};
GN   ORFNames=TERG_03065 {ECO:0000313|EMBL:KFL61059.1};
OS   Trichophyton rubrum (strain ATCC MYA-4607 / CBS 118892) (Athlete's foot
OS   fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=559305 {ECO:0000313|EMBL:KFL61059.1, ECO:0000313|Proteomes:UP000008864};
RN   [1] {ECO:0000313|Proteomes:UP000008864}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4607 / CBS 118892 {ECO:0000313|Proteomes:UP000008864};
RX   PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA   Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA   Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA   Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA   Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA   Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT   "Comparative genome analysis of Trichophyton rubrum and related
RT   dermatophytes reveals candidate genes involved in infection.";
RL   MBio 3:E259-E259(2012).
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; GG700650; KFL61059.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A080WI34; -.
DR   VEuPathDB; FungiDB:TERG_03065; -.
DR   HOGENOM; CLU_011405_5_0_1; -.
DR   OMA; ANYDTAN; -.
DR   OrthoDB; 1069499at2759; -.
DR   Proteomes; UP000008864; 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; 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; 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.
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:UP000008864}.
FT   DOMAIN          1..135
FT                   /note="Malic enzyme N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01274"
FT   DOMAIN          145..405
FT                   /note="Malic enzyme NAD-binding"
FT                   /evidence="ECO:0000259|SMART:SM00919"
FT   BINDING         33
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT   BINDING         122
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT   BINDING         123
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT   BINDING         144
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT   BINDING         287
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT   BINDING         336
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
SQ   SEQUENCE   474 AA;  51568 MW;  F57CF041180965B9 CRC64;
     MYLSYEDRGN IAAVIQNWPQ PNVDITVITD GSRILGLGDL GINGMGIPIG KLALYTACAG
     IRPEATLPLT LDLGTSNKAL REDPLYMGSR RGKVTQEQEL EFMDELMAAL TERWPGIVIQ
     FEDFKNPFPA LEKYRHNYTC FNDDIQGTGA VILGGVINAV KRSGVPPKDH RAVFLGAGSA
     GVGVAKQIVD FFVKEGMTED EAKACFYLVD TKGLVTADRG DRLAAHKVYF ARHDNNGQQF
     KTLEEVVDHV KPTMLMGLST LGGVFTPEIL KKMADNNKQP IIFPLSNPSA NSECDFKSAI
     THTDGRALFA SGSPFPSFSF KNSAGETSTY YPGQGNNMYV FPGIGLGTIL SKAVEVTDSM
     IYAAADALST SLTTEELDRG LLYPEITRIR EVSVAVARGV IRAAQEAKVD RETAIRTFTD
     SDLDSWIKSK MYNPHSEVNS LEREVGILLS SIGRMNGTSN GDISPRGEDQ GSKL
//
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