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Database: UniProt
Entry: Q0CGJ8_ASPTN
LinkDB: Q0CGJ8_ASPTN
Original site: Q0CGJ8_ASPTN 
ID   Q0CGJ8_ASPTN            Unreviewed;       746 AA.
AC   Q0CGJ8;
DT   17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   17-OCT-2006, sequence version 1.
DT   13-SEP-2023, entry version 77.
DE   RecName: Full=2-dehydropantoate 2-reductase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=ATEG_07194 {ECO:0000313|EMBL:EAU32578.1};
OS   Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=341663 {ECO:0000313|EMBL:EAU32578.1, ECO:0000313|Proteomes:UP000007963};
RN   [1] {ECO:0000313|Proteomes:UP000007963}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIH 2624 / FGSC A1156 {ECO:0000313|Proteomes:UP000007963};
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA   Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA   Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA   Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA   Nierman W.C., Milne T., Madden K.;
RT   "Annotation of the Aspergillus terreus NIH2624 genome.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CH476603; EAU32578.1; -; Genomic_DNA.
DR   RefSeq; XP_001209880.1; XM_001209880.1.
DR   AlphaFoldDB; Q0CGJ8; -.
DR   STRING; 341663.Q0CGJ8; -.
DR   EnsemblFungi; EAU32578; EAU32578; ATEG_07194.
DR   GeneID; 4319207; -.
DR   VEuPathDB; FungiDB:ATEG_07194; -.
DR   eggNOG; ENOG502QT3Z; Eukaryota.
DR   HOGENOM; CLU_021479_0_0_1; -.
DR   OMA; RENAYDY; -.
DR   OrthoDB; 2727909at2759; -.
DR   Proteomes; UP000007963; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR   InterPro; IPR013328; 6PGD_dom2.
DR   InterPro; IPR013752; KPA_reductase.
DR   InterPro; IPR013332; KPR_N.
DR   PANTHER; PTHR21708; PROBABLE 2-DEHYDROPANTOATE 2-REDUCTASE; 1.
DR   PANTHER; PTHR21708:SF25; PROTEIN PAM1-RELATED; 1.
DR   Pfam; PF02558; ApbA; 1.
DR   Pfam; PF08546; ApbA_C; 1.
DR   SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000007963}.
FT   DOMAIN          9..165
FT                   /note="Ketopantoate reductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02558"
FT   DOMAIN          198..320
FT                   /note="Ketopantoate reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08546"
FT   REGION          324..397
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          466..485
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          518..545
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          594..746
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        334..360
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        626..667
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        678..739
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   746 AA;  80611 MW;  D20B394C973D6CCD CRC64;
     MAPPPRLRIL SVGSNAISAF LSWRLQATTS CDVTLVWKSG YEAVSQYGVS FKSKAFGNER
     FKPRHVVRAP EDAASRENAY DYVILCVKAL PDVYDLAAVI ESVVTPQHTC ILVNTTNTIG
     VESHLEQRFP TNVVLSLVSG VEISQIGASE FEHLNSSEIW VGATNKKSNI PSSIQNDMAA
     ALAMTLGSGQ VDCKVSPNIR QEQFERMIGP IAFYPSSVMF ETSNHSQLLE KVGVRQLVTD
     IIEELMELAK ANGCSFPDDF AQKTIEKMTA SGAPSSMYQD FQARRPMEIE TYLGSPIKLA
     AESGVRVPRI ETLYAVLHHV NTTNLNKPRT NESPPPTLAN PPPRMSSAPP RGPPMNGPMR
     PGPAGRTSSG MAMPPRRGPP MPGMARPPSA QPASARIPRE PSLEGLEEFS HLVLYDDAPD
     AVMPQNGANG VHDMPPGPPA AADLALRERE LALRQRELQI REQEMGMRRG PPRRGPPPRA
     AFDEEDEDDF FDPMESMPVP HIDPDSVDMM SITSRRAKKA PSASQFRKNP EIHINGNGGS
     RPGSAFSRYF GGRKRASDRI MQEIPGLHDS LMDNPMMAYS SNRYGAVDRN QMHAGSRANS
     LTASRMGDFP PHPYPQSRRN SQSPATPFGP PGPRMGRPAN PQDPSLGPPN GPPSGHPSPP
     GQMRAPVPRY PPGQGNAVGP QQVEQQYGVS NSFSAKGTPK HRSLTGSASA SAESGDSGAS
     ANLESETSAH SSQISLGAQQ AAMPVR
//
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