ID A0A094GRB5_9PEZI Unreviewed; 492 AA.
AC A0A094GRB5;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Ketopantoate reductase C-terminal domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=V501_08425 {ECO:0000313|EMBL:KFZ05362.1};
OS Pseudogymnoascus sp. VKM F-4519 (FW-2642).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420914 {ECO:0000313|EMBL:KFZ05362.1, ECO:0000313|Proteomes:UP000029315};
RN [1] {ECO:0000313|EMBL:KFZ05362.1, ECO:0000313|Proteomes:UP000029315}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4519 (FW-2642) {ECO:0000313|Proteomes:UP000029315};
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:KFZ05362.1}.
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DR EMBL; JPKD01002315; KFZ05362.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094GRB5; -.
DR STRING; 1420914.A0A094GRB5; -.
DR HOGENOM; CLU_031468_10_1_1; -.
DR Proteomes; UP000029315; 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:UP000029315}.
FT DOMAIN 123..300
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 345..472
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
FT REGION 38..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..56
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..87
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..118
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 492 AA; 55074 MW; 92193014A1BF2AEB CRC64;
MGNTFVQIEG RGARRLISIQ YGRRYSSQKV HWNSEFAHVE PSGEEGGREE AGRGYEQRIP
RTSSRNISTP RNNIPTPRTL ESEASINASD PQHREIREEE EMEMDRGEKE EVSTHTHSKP
SRIHILGTGK EGKFVAHSLA SLGGRPPISL LLQRPSLVNQ WHSEGQILEL LEAKKSMVQI
GFDIENPNLT QAEYTQGRML STKNVLFGQD GWNIDQLIVT TEAPVTVRSL LPIKDRLHST
STILFLQNGM GVIDEVNENV FPNPATRPRY IEGMTSHSLR NHPARTFTTL HSGEGEIFLA
AQKGDETSSD AVDMIDSTRS LLRSLARSPA LNAKGVSPAE LLVLKLERLA VEAVIGPLAV
MFDCKNGDLL SNYMVTLLLR EVLNEISTVA SELPELKGET GLSYRLHPRK IERTFVQVAT
MTSSEIHDMV RSVRLGKKSE VGYFTGYILK RAAELGIDCP NNTLMERMVK AKTAMRSQEA
NSYIPYKKDR RF
//
