ID A0A093XPJ4_9PEZI Unreviewed; 469 AA.
AC A0A093XPJ4;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=2-dehydropantoate 2-reductase {ECO:0008006|Google:ProtNLM};
GN ORFNames=O988_08940 {ECO:0000313|EMBL:KFX88674.1};
OS Pseudogymnoascus sp. VKM F-3808.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1391699 {ECO:0000313|EMBL:KFX88674.1, ECO:0000313|Proteomes:UP000029329};
RN [1] {ECO:0000313|EMBL:KFX88674.1, ECO:0000313|Proteomes:UP000029329}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-3808 {ECO:0000313|EMBL:KFX88674.1,
RC ECO:0000313|Proteomes:UP000029329};
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 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:KFX88674.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JPJR01002407; KFX88674.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093XPJ4; -.
DR HOGENOM; CLU_031468_10_1_1; -.
DR Proteomes; UP000029329; 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:UP000029329}.
FT DOMAIN 100..279
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 322..449
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
FT REGION 20..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..42
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..72
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 469 AA; 51969 MW; 3C6D2DB86F62B305 CRC64;
MELRRSYSSQ RVQWNSEFAH VEPSVEEGGA EEARRGYEHG IPRKSSRNIY TPRNNTPRTL
DSAAATSASD LQHSETREGE VGSGVQEGAS IHTHSKPSRI HILGTGKEGK FVAHSLASLG
GRPPISLLLQ RPSLVSQWHQ EGQILELLEA KESMVQIGFD IENPNLTQAE YTQGRMLSTK
NVLFGQDGWN IDQLIVTTEA PVTVRSLLPI KDRLHSTSTI LFLQNGMGVI DEVNEKVFPN
PATRPRYIEG MSSHSLRNHP ARTFTTLHSG QGEIFLTAHE GDQMSPDAVD MIDSTRNLLR
SLARSPALNA KGVPPDELLV LKLERLAVEA VIGPLAVMFD CKNGDLLNNY NVSLLLRGVL
NEISTVASAL PELKGQSGLS YRLHPRKIER TFVQVATKTR TEIHDMVRSV RLGKKSEVAY
FTGYILKRAA ELGIDCPNNA LMETMVKAKT AMRSQEASGH IPYKNDRRF
//
