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Database: UniProt
Entry: X0BQR5_FUSOX
LinkDB: X0BQR5_FUSOX
Original site: X0BQR5_FUSOX 
ID   X0BQR5_FUSOX            Unreviewed;       653 AA.
AC   X0BQR5;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   SubName: Full=2-dehydropantoate 2-reductase {ECO:0000313|EMBL:EXK84535.1};
GN   ORFNames=FOQG_11324 {ECO:0000313|EMBL:EXK84535.1};
OS   Fusarium oxysporum f. sp. raphani 54005.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium oxysporum species complex.
OX   NCBI_TaxID=1089458 {ECO:0000313|EMBL:EXK84535.1, ECO:0000313|Proteomes:UP000030663};
RN   [1] {ECO:0000313|EMBL:EXK84535.1, ECO:0000313|Proteomes:UP000030663}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=54005 {ECO:0000313|EMBL:EXK84535.1,
RC   ECO:0000313|Proteomes:UP000030663};
RG   The Broad Institute Genome Sequencing Platform;
RA   Ma L.-J., Gale L.R., Schwartz D.C., Zhou S., Corby-Kistler H., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA   Freedman E., Gearin G., Goldberg J., Griggs A., Gujja S., Heiman D.,
RA   Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C.,
RA   Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N.,
RA   Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Fusarium oxysporum PHW815.";
RL   Submitted (NOV-2011) 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; JH658395; EXK84535.1; -; Genomic_DNA.
DR   AlphaFoldDB; X0BQR5; -.
DR   eggNOG; ENOG502SJ6A; Eukaryota.
DR   HOGENOM; CLU_419791_0_0_1; -.
DR   Proteomes; UP000030663; Unassembled WGS sequence.
DR   GO; GO:0008677; F:2-dehydropantoate 2-reductase activity; IEA:InterPro.
DR   GO; GO:0015940; P:pantothenate biosynthetic process; IEA:InterPro.
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; IPR003710; ApbA.
DR   InterPro; IPR021858; Fun_TF.
DR   InterPro; IPR013752; KPA_reductase.
DR   InterPro; IPR013332; KPR_N.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   NCBIfam; TIGR00745; apbA_panE; 1.
DR   PANTHER; PTHR21708:SF30; 2-REDUCTASE FAMILY PROTEIN, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G00740)-RELATED; 1.
DR   PANTHER; PTHR21708; PROBABLE 2-DEHYDROPANTOATE 2-REDUCTASE; 1.
DR   Pfam; PF02558; ApbA; 1.
DR   Pfam; PF08546; ApbA_C; 1.
DR   Pfam; PF11951; Fungal_trans_2; 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:UP000030663}.
FT   DOMAIN          8..166
FT                   /note="Ketopantoate reductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02558"
FT   DOMAIN          201..319
FT                   /note="Ketopantoate reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08546"
SQ   SEQUENCE   653 AA;  73636 MW;  6BE9B059E50A4EB0 CRC64;
     MTSPKDRVLL IGSGGIGTIA ALNLERGGLA EVTSVLRSNF QVVRTKGFTI RSCQHGDIHN
     WRPTESLDAI PNRYDAQGRP FDYIVCCTKN IPDIIPTLCD IIAPAVTPGH TAIVLIQNGL
     NIERPFIHRF PNNVIISGIS RIDAHEVAPG VIEQKQNDLL HIGAFNNPSL HLKVQKAAAK
     RFVEIYSMGG KTTCLYQPDV DFDRWSKLVY NASFNPICAL ARLNTGELQR TGRVVDTLVI
     PAMKEVLAVA EKAGHALPES IINDTIRSNP INDNITPSMQ IDLEKGNFIE HENIIGEVVR
     EGHERGVATP VLSILYELCC AVQWKLKGKR NDLTVDARTA HLSSRFAPRL SSPQTPAAAP
     NLGLLDLELM HNFCTSTYAT LSNDSAIRDL WRIRIVRLCL NCDYATLAIL SVSALHLSHF
     STERREFLRE RAITYHNQAL SIASAFIDAY NDKNAQHLFA FSILTIYYSF AQTPEHDDGP
     YPPWVVLIKG CTSFMALARS TLLVGPFSAL LQKARRRLEL REQTFKTDYM QQLRFFVDET
     ITDSEQRSVY LDAIHGLNQT YGVFYEVEGD KDLVDIFSWI VFAKDFLTFV ADEEEEALVV
     LSYFCVLLHK LPCQWWLNSW VNHIMTRIYS SVGEVYLTYL VWPMEEIGWL PKH
//
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