ID A0A0A2VHU8_BEABA Unreviewed; 707 AA.
AC A0A0A2VHU8;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=NADP-dependent malic enzyme {ECO:0000313|EMBL:KGQ05907.1};
GN ORFNames=BBAD15_g8835 {ECO:0000313|EMBL:KGQ05907.1};
OS Beauveria bassiana D1-5.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX NCBI_TaxID=1245745 {ECO:0000313|EMBL:KGQ05907.1, ECO:0000313|Proteomes:UP000030106};
RN [1] {ECO:0000313|EMBL:KGQ05907.1, ECO:0000313|Proteomes:UP000030106}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D1-5 {ECO:0000313|EMBL:KGQ05907.1,
RC ECO:0000313|Proteomes:UP000030106};
RA Li Q., Wang L., Zhang Z., Wang Q., Ren J., Wang M., Xu W., Wang J., Lu Y.,
RA Du Q., Sun Z.;
RT "Genome sequencing and analysis of entomopathogenic fungi Beauveria
RT bassiana D1-5.";
RL Submitted (OCT-2012) 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}.
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:KGQ05907.1}.
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DR EMBL; ANFO01000905; KGQ05907.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A2VHU8; -.
DR STRING; 1245745.A0A0A2VHU8; -.
DR EnsemblFungi; BB8028_0005g04070.1; BB8028_0005g04070.1; BB8028_0005g04070.
DR eggNOG; KOG1257; Eukaryota.
DR HOGENOM; CLU_011405_2_1_1; -.
DR Proteomes; UP000030106; 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; 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.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|PIRSR:PIRSR000106-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000030106}.
FT DOMAIN 206..386
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 396..662
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT REGION 34..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 229
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT ACT_SITE 300
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT BINDING 282
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT BINDING 371
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 372
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 395
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 544
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT BINDING 593
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
SQ SEQUENCE 707 AA; 78423 MW; B4182AB665DDC0B0 CRC64;
MSSPRFSALA TALANSPIAR RSSFPSRASA LPMASSYPLS TDTSDIATPR SASLSSIDSR
KSGRSISRFS VRSASQTSTS RLSFSAQRLT QRNTMSAVDI SAIQEAMKMT ALDQHRGYTQ
DRFAEVKQTQ PTQYISEAAA AGYQIIREPH WNKGLSFTPE ERVAKNLTGL IPHTMESLET
QSIRAMKMIQ TRQTSIDKYL YLSNLKAQNI DLFYRLLMDN IRELMPLVYT PTIGDVCLQY
STLYTRPEAL YISIKQRRSI KTMLRNWPCT DPEICVVTDG SRILGLGDLG VNGVGISIGK
LSLYTAAAGI SPEKTLPIVL DTGTDNESNL KDPLYLGLRQ KRVSKAAQQE FMDEFMDAVK
EVYPSMVVQF EDFESEKAFN YLDRYRNTHR CFNDDVQGTG AVVLGGYIGA VNLSGVPLED
QRLVFMGAGS AGVGVAKQLV EYYTKRGLSQ SEARDRFWLV DTKGLVTKDR GDHLAEHKQY
FARTDNQGQQ FRTLEEVIEY VRPSALVGLA ATYGVFTESC IRALKHSVDG GGPNRRPILF
PLSNPHTKAE CTFEQAVEWT DGSVIFASGS PFPSLTVAGP NGNEITYHPN QGNNVYVFPG
LGLGAILAQA TRITDEMVYT SASALANCLN ADELAKGLIY PRIERVREAS VIIAREVMKA
ARREGVSTLP EELWNEWEEW GDVALTSYIR QRVYEPKSFN DANSSRL
//
