ID A0A0D2A7B6_9EURO Unreviewed; 760 AA.
AC A0A0D2A7B6;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=2-dehydropantoate 2-reductase {ECO:0008006|Google:ProtNLM};
GN ORFNames=PV08_01244 {ECO:0000313|EMBL:KIW20667.1};
OS Exophiala spinifera.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=91928 {ECO:0000313|EMBL:KIW20667.1, ECO:0000313|Proteomes:UP000053328};
RN [1] {ECO:0000313|EMBL:KIW20667.1, ECO:0000313|Proteomes:UP000053328}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 89968 {ECO:0000313|EMBL:KIW20667.1,
RC ECO:0000313|Proteomes:UP000053328};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala spinifera CBS89968.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KN847492; KIW20667.1; -; Genomic_DNA.
DR RefSeq; XP_016240883.1; XM_016375607.1.
DR AlphaFoldDB; A0A0D2A7B6; -.
DR STRING; 91928.A0A0D2A7B6; -.
DR GeneID; 27328327; -.
DR VEuPathDB; FungiDB:PV08_01244; -.
DR HOGENOM; CLU_021479_0_0_1; -.
DR OrthoDB; 2727909at2759; -.
DR Proteomes; UP000053328; 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:UP000053328}.
FT DOMAIN 9..163
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 197..320
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
FT REGION 328..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 473..557
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 617..760
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 335..350
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..405
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 518..540
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 647..692
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 720..760
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 760 AA; 82182 MW; 6350A7D55475A57A CRC64;
MNRELRHCCL VGGNAVSAFL SWRLQATNAC DVTLVWKANY QSVAQYGVSF KSQMFGNERF
KPRYVVQTPE DAGGRQAAFD YVILCVKALP DVYNLADIIQ SVVTPQHTCI LVNTTNTLGV
EKQLEERFPT NVVLSLVSGA DLVQLGTSEF EHRGSTEIWV GPSSQNSTIP EAIQRDMSEA
LAMTLTTAQV DCKVSSNIKQ QQYERMIGPI AFHPTSVVFE TANLADLVRM PGVHDLISDV
IEELLSVARA QNCVFPADFK ETTISNMIDS SQEASTMYQD FSARRPMEVE TYLGAPVQLA
KAAGVKVPRI ETLYALLRHV NTVNKDRPVA SAAPPASLQS PTAAVQPPPR TISLSNPPPP
RQPNGSFNGP PRPMRGPPPM GPPGRRGPPP VNGFRGPPNS FPQRPGPMQR RPSYDENNLD
EFSHVVLYDE MADGDGAPAG FAENGVGPSL RERELMLRER ELQIKQQEMA MRRGVGGGGR
RTSHNRHQEF DDDDDDDDFF DPMMARGPPP PSIDPDNFDM MSVTSRRTKR APSQSQLRKD
GYVNGGPMRP GSYGRPNMGM GRHRTSASIL SDMPVLGSNI LDNPMMGFSS NRYGNVDRKE
MADESRANSL TASRLQEIGM NGGPGMSGGP YPGPPSRRTS RSPGNPFGPP GRIPGGRPSP
PNDPYMQPGP SRNGRPSPPG GMPAPIPRYP PGQNGMIPGQ VEQAGNNKPF PPPKAPVKSL
TGSASASAGS GDSGSANIES EPSAHSSTSS FAQRQMLGAH
//