ID A0A178EN67_9PLEO Unreviewed; 493 AA.
AC A0A178EN67;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=2-dehydropantoate 2-reductase {ECO:0008006|Google:ProtNLM};
GN ORFNames=IQ07DRAFT_527750 {ECO:0000313|EMBL:OAL57112.1};
OS Pyrenochaeta sp. DS3sAY3a.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Cucurbitariaceae;
OC Pyrenochaeta.
OX NCBI_TaxID=765867 {ECO:0000313|EMBL:OAL57112.1, ECO:0000313|Proteomes:UP000077535};
RN [1] {ECO:0000313|EMBL:OAL57112.1, ECO:0000313|Proteomes:UP000077535}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS3sAY3a {ECO:0000313|EMBL:OAL57112.1,
RC ECO:0000313|Proteomes:UP000077535};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the ketopantoate reductase family.
CC {ECO:0000256|ARBA:ARBA00007870}.
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DR EMBL; KV441636; OAL57112.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A178EN67; -.
DR STRING; 765867.A0A178EN67; -.
DR InParanoid; A0A178EN67; -.
DR OrthoDB; 1354873at2759; -.
DR Proteomes; UP000077535; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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 InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43765; 2-DEHYDROPANTOATE 2-REDUCTASE-RELATED; 1.
DR PANTHER; PTHR43765:SF2; 2-DEHYDROPANTOATE 2-REDUCTASE-RELATED; 1.
DR Pfam; PF02558; ApbA; 1.
DR Pfam; PF08546; ApbA_C; 1.
DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000077535}.
FT DOMAIN 49..245
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 320..452
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 128..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 462..493
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 463..486
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 493 AA; 54738 MW; 74F5B30C958AEE42 CRC64;
MTSWKNEQTM QPEDGTAQSK ESYDEPAPPN ISNDAADFYR VKPTSDRRIH VMGVGNVGKF
VAHAIRGIPN PPPVTLIFSR WDKLKEWNVS EKKITVITDG DAEAREGFEA EIAIPRIRYH
GKEVGLNIGS SQSNAESENT EPGPPQTLPG ESTEPISSLI VCSKAPYVLQ GLSAVKHRLN
KDSVVMFLLN GMGTVEEVNR EIFPDPATRP YYMLGINSHG MHSTPDDPFA TVHAGFGTMS
VGYSPQERDR NTTAYQSPDV RFTANPNKPP TYYDYTSQEQ SNDTTAATGT KIRFTSNQRY
LLRTILRTPV LGAAAFSPLD LLQMQLEKLA VNCIVNPLTV LLDARNGSIL YNFALTRTMR
LLLAEISLVI RSIPELRHIP NVDQRFDAAR LETRVVAIAR ATKDNISSML ADVRAGHQTE
INYINGWIVN KGEELGIRCT MNYMLLNLVK GKASLISNEA KEDVPLVSER GPENEEKDDG
LKIKNRQARK GNL
//
