ID A0A093ZAE8_9PEZI Unreviewed; 598 AA.
AC A0A093ZAE8;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=2-dehydropantoate 2-reductase {ECO:0008006|Google:ProtNLM};
GN ORFNames=V492_04177 {ECO:0000313|EMBL:KFY11943.1};
OS Pseudogymnoascus sp. VKM F-4246.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420902 {ECO:0000313|EMBL:KFY11943.1, ECO:0000313|Proteomes:UP000029299};
RN [1] {ECO:0000313|EMBL:KFY11943.1, ECO:0000313|Proteomes:UP000029299}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4246 {ECO:0000313|EMBL:KFY11943.1,
RC ECO:0000313|Proteomes:UP000029299};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the PDCD5 family.
CC {ECO:0000256|ARBA:ARBA00010490}.
CC -!- SIMILARITY: Belongs to the ketopantoate reductase family.
CC {ECO:0000256|ARBA:ARBA00007870}.
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:KFY11943.1}.
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DR EMBL; JPJU01001370; KFY11943.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093ZAE8; -.
DR STRING; 1420902.A0A093ZAE8; -.
DR HOGENOM; CLU_031468_10_1_1; -.
DR Proteomes; UP000029299; Unassembled WGS sequence.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 1.10.8.140; PDCD5-like; 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 InterPro; IPR002836; PDCD5-like.
DR InterPro; IPR036883; PDCD5-like_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 Pfam; PF01984; dsDNA_bind; 1.
DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF46950; Double-stranded DNA-binding domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000029299}.
FT DOMAIN 101..277
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 323..424
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
FT REGION 1..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 480..512
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..36
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..70
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 484..512
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 598 AA; 65777 MW; 00C9277CB3F47537 CRC64;
MELRKYSSQR VHWNPEFAHV EPSGEEGGRE EAGRGYGEAI PRTSSRNISK SRNSIPTLQT
LESAAAISPS DPQHSERREG EMSPGEQEGA STHTHSKPSR IHILGTGKEG KFVAHSLASL
GGRPPISLLL QRPSLVHQWH EEGQILELLE AKKSTVQIGF DVENPNLTQA EYTQGRMLST
KNVLFGQDGW NIDQLIVTTE APVTVRSLLP IKDRLTSTST ILFLQNGMGV IDEVNEKVFP
NPAARPRYIE GMTSHSLRNH PARTFTTLHS GQGQIFLAAQ KADQMPPDTL DMIDSTRSLL
RSLARSPALN AKGVSPTELL VLKLERLAVE AVIGPLSVMF DCKNGDLLSN YMVTLLLREV
LNEISAVASE LPELKGQGGL SYRLHPRKIE RTFVQVATMT SSEIHDMVRS VRLGKKSEVG
YFTGLEILPP WSDKASSPHS HTSASTTIQI KLRLAQNTTT TNKMADADLE EIRKARLAQL
KSQGGGGGAS SSGGGGGGQD EQRQQQESEA RQSVLNQILE PAAAERLGRI RLVKESRADD
VENRLITLAR SGQLRQKVTE EQLKELLNAV AETKEEEKIV ISRRKGGWDD DDDDLFNM
//