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Database: UniProt
Entry: A0A0J9WH96_FUSO4
LinkDB: A0A0J9WH96_FUSO4
Original site: A0A0J9WH96_FUSO4 
ID   A0A0J9WH96_FUSO4        Unreviewed;       716 AA.
AC   A0A0J9WH96;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=Malate dehydrogenase (Oxaloacetate-decarboxylating)(NADP+) {ECO:0008006|Google:ProtNLM};
GN   ORFNames=FOXG_01611 {ECO:0000313|EMBL:KNA96396.1};
OS   Fusarium oxysporum f. sp. lycopersici (strain 4287 / CBS 123668 / FGSC 9935
OS   / NRRL 34936) (Fusarium vascular wilt of tomato).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium oxysporum species complex.
OX   NCBI_TaxID=426428 {ECO:0000313|EMBL:KNA96396.1, ECO:0000313|Proteomes:UP000009097};
RN   [1] {ECO:0000313|EMBL:KNA96396.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=4287 {ECO:0000313|EMBL:KNA96396.1};
RG   The Broad Institute Genome Sequencing Platform;
RA   Birren B., Lander E., Galagan J., Nusbaum C., Devon K., Ma L.-J., Jaffe D.,
RA   Butler J., Alvarez P., Gnerre S., Grabherr M., Kleber M., Mauceli E.,
RA   Brockman W., MacCallum I.A., Young S., LaButti K., DeCaprio D.,
RA   Crawford M., Koehrsen M., Engels R., Montgomery P., Pearson M., Howarth C.,
RA   Larson L., White J., O'Leary S., Kodira C., Zeng Q., Yandava C.,
RA   Alvarado L., Kistler C., Shim W.-B., Kang S., Woloshuk C.;
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KNA96396.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=4287 {ECO:0000313|EMBL:KNA96396.1};
RX   PubMed=20237561; DOI=10.1038/nature08850;
RA   Ma L.J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.J.,
RA   Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA   Houterman P.M., Kang S., Shim W.B., Woloshuk C., Xie X., Xu J.R.,
RA   Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA   Butchko R.A., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.,
RA   Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA   Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA   Kumar L., Lee Y.H., Li L., Manners J.M., Miranda-Saavedra D., Mukherjee M.,
RA   Park G., Park J., Park S.Y., Proctor R.H., Regev A., Ruiz-Roldan M.C.,
RA   Sain D., Sakthikumar S., Sykes S., Schwartz D.C., Turgeon B.G.,
RA   Wapinski I., Yoder O., Young S., Zeng Q., Zhou S., Galagan J., Cuomo C.A.,
RA   Kistler H.C., Rep M.;
RT   "Comparative genomics reveals mobile pathogenicity chromosomes in
RT   Fusarium.";
RL   Nature 464:367-373(2010).
CC   -!- SIMILARITY: Belongs to the malic enzymes family.
CC       {ECO:0000256|ARBA:ARBA00008785}.
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DR   EMBL; DS231697; KNA96396.1; -; Genomic_DNA.
DR   RefSeq; XP_018234442.1; XM_018378507.1.
DR   AlphaFoldDB; A0A0J9WH96; -.
DR   SMR; A0A0J9WH96; -.
DR   GeneID; 28943854; -.
DR   KEGG; fox:FOXG_01611; -.
DR   VEuPathDB; FungiDB:FOXG_01611; -.
DR   OrthoDB; 1069499at2759; -.
DR   Proteomes; UP000009097; Unassembled WGS sequence.
DR   GO; GO:0004470; F:malic enzyme activity; IEA:InterPro.
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; 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   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   Reference proteome {ECO:0000313|Proteomes:UP000009097}.
FT   DOMAIN          230..395
FT                   /note="Malic enzyme N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01274"
FT   DOMAIN          405..672
FT                   /note="Malic enzyme NAD-binding"
FT                   /evidence="ECO:0000259|SMART:SM00919"
FT   REGION          36..76
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          89..129
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   716 AA;  79618 MW;  E5C12F0A063C77A2 CRC64;
     MGQTLSTMTV ASPSGPGSAQ NVLNRLFFAS GPLRSATSST LTRASTRSST VPPAVVLTAT
     TNNRRPRPSN PRLSYSSFFP FSSPHLPLSM SMASSSPHST ASSEIATPRS RSSTTSSPRR
     LTDSNPMSPV DLSKIEQEIK MAALDQHRGY VQDHYAEVKQ DRTPEYVDES NAAGYQIVRE
     PLWNKGLAFT PEERASKNLT GLLPHTMESF ETQCARAMKM IQTRQTPIDK DQNTDLFYRL
     LIDNIRELMP LVYTPTIGDV CLQYSSIYTR PEALYISIKQ RKSIRAMLRN WPCQDPEICV
     VTMALASLVW IGKPALYTGA AGIHPSKTLP IVLDCGTQQR GEPERPLLPW RPSYPEQQAF
     MDEFMEAARE VFPSMVVQFE DFDSEKAFGY LDRYRDQYRC FNDDIQGTGA VVLGGYIGAV
     EQSGVPIEEQ RLVFMGAGSA GVGVAKQLVE YYTRRGLSEA AARDKFWLVD TKGLVTKDRG
     DRLAEHKKYF ARTDNNGQQY RTLEEVIEYV KPSALVGLTA TFGVFTEPVV RALKHSVQEG
     GLERRPILFP LSNPLTKAEC TFEQAIEWTE GTVLFASGSP FNPVKAKFGD ETHHTVYHPN
     QGNNVYIFPG LGLGAILAKA SRVTDEMVYT SAAALAGSLN ADEVHKGLIY PRIERVRDAS
     VIVAREVMKA ARRGGVSELP ESQWAEWEEW GDVALTTYIK QRIYNPLCFA DAKTHL
//
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