ID A0A2S7NW18_9HELO Unreviewed; 610 AA.
AC A0A2S7NW18;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 02-APR-2025, entry version 20.
DE SubName: Full=2-dehydropantoate 2-reductase protein {ECO:0000313|EMBL:PQE06192.1};
GN ORFNames=CJF30_00005138 {ECO:0000313|EMBL:PQE06192.1};
OS Rutstroemia sp. NJR-2017a BBW.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Rutstroemiaceae; Rutstroemia.
OX NCBI_TaxID=2070414 {ECO:0000313|EMBL:PQE06192.1, ECO:0000313|Proteomes:UP000238072};
RN [1] {ECO:0000313|EMBL:PQE06192.1, ECO:0000313|Proteomes:UP000238072}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NJR-2017a BBW {ECO:0000313|EMBL:PQE06192.1,
RC ECO:0000313|Proteomes:UP000238072};
RA Gaut B.S., Morton B.R., Clegg M.T., Duvall M.R.;
RL Submitted (JAN-2018) 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:PQE06192.1}.
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; NJPT01000082; PQE06192.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S7NW18; -.
DR STRING; 2070414.A0A2S7NW18; -.
DR OrthoDB; 73846at2759; -.
DR Proteomes; UP000238072; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:TreeGrafter.
DR GO; GO:0008677; F:2-dehydropantoate 2-reductase activity; IEA:TreeGrafter.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:TreeGrafter.
DR Gene3D; 1.10.1040.10; N-(1-d-carboxylethyl)-l-norvaline Dehydrogenase, domain 2; 1.
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; IPR050838; Ketopantoate_reductase.
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:SF2; 2-DEHYDROPANTOATE 2-REDUCTASE; 1.
DR PANTHER; PTHR43765; 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:UP000238072}.
FT DOMAIN 127..293
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 351..475
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
FT REGION 1..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 492..521
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..18
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 495..510
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 511..521
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 610 AA; 67415 MW; 8D044EE1E5A0308A CRC64;
MQSGAKPADA EEVAKNRSLE LGPLATPSRS ENVEDPAEEA QYALADEGTQ STMLDQPFDL
ERESPSISRD ETFQDTQQYA EVAQTGFVEN LQPESAQQQM EDYGTTSEEV SITEDTIVDT
QEVSRTIHIL GTDPVGQFVA HGLAGLDFAP PITLLMDRPI QIKHWRAAGG AVKVRNQGLT
SERSGFDVEL TKDFGVQSKQ AFKSSDEVIN NLIITTKGAK TVAALTSIKH RLRSSSTICF
IQHGAGVIDE INALVFPDPT TRPHYMLGNA SHGVFPSDQP WTVSQVSHGQ LKLTILPRDT
DKSTGRGSVR RLDPGWAPSS RYMLMMLCRD PELRATGLLY PEYLKAHFEF VAVNSVISPL
SVVFDCSCNQ LLYNYPASQT MKSLLQEISG VLTILPEFEN TPNITKHFGL DRLESLVLSV
IARTGENLTT MLRNVRAGKR TDIDYYNGYI VKRAKELGVP FSVNEMVVNM VKAKQAMDDD
LAQIRRARLE QLKSQGGGGR AAGPSSGGGQ DENRQQQEEA ARQSILNQIL EPEAADRLGR
IRLVKESRAA DVENRLIMLA RSGQLRQKIT EDQLKELLGS VAESKKDEEK IVVSRRKGGW
DDEDDDLLDL
//
