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Database: UniProt
Entry: F9G0J6_FUSOF
LinkDB: F9G0J6_FUSOF
Original site: F9G0J6_FUSOF 
ID   F9G0J6_FUSOF            Unreviewed;       890 AA.
AC   F9G0J6;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   24-JAN-2024, entry version 50.
DE   RecName: Full=2-dehydropantoate 2-reductase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=FOXB_12178 {ECO:0000313|EMBL:EGU77294.1};
OS   Fusarium oxysporum (strain Fo5176) (Fusarium vascular wilt).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium oxysporum species complex.
OX   NCBI_TaxID=660025 {ECO:0000313|EMBL:EGU77294.1};
RN   [1] {ECO:0000313|EMBL:EGU77294.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fo5176 {ECO:0000313|EMBL:EGU77294.1};
RX   PubMed=21942452; DOI=10.1094/mpmi-08-11-0212;
RA   Thatcher L.F., Gardiner D.M., Kazan K., Manners J.;
RT   "A highly conserved effector in Fusarium oxysporum is required for full
RT   virulence on Arabidopsis.";
RL   Mol. Plant Microbe Interact. 25:180-190(2012).
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:EGU77294.1}.
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DR   EMBL; AFQF01003009; EGU77294.1; -; Genomic_DNA.
DR   AlphaFoldDB; F9G0J6; -.
DR   STRING; 660025.F9G0J6; -.
DR   PaxDb; 5507-FOXG_12046P0; -.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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   InterPro; IPR007568; RTA1.
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   Pfam; PF04479; RTA1; 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   Membrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        628..647
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        654..672
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        692..714
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        726..745
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        765..787
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        808..826
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        846..866
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
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   890 AA;  99615 MW;  C71A6C371C6100C2 CRC64;
     MTSPKDRVLL IGSGGIGTIA ALNLERGGLA EVTSVLRSNF QVVRTKGFTI RSCQHGDIHN
     WRPTESLDAI PNRYDAQGRP FDYIVCCTKN IPDIIPTLCD IIAPAVTPGH TAIVLIQNGL
     NIERPFIHRF PNNVIISGIS RIDAHEVAPG VIEQKQNDLL HIGAFNNPSL HLKVQEAAAK
     RFVEIYSMGG KTTCLYQPDV DFDRWSKLVY NASFNPICAL ARLNTGELQR TGRVVDTLVI
     PAMKEVLAVA EKAGHALPES IINDTIRSNP INDNITPSMQ IDLEKGNFIE HENIIGEVVR
     EGHERGVATP VLSILYELCC AVQWKLKGKR NDLTIDACIA GLSSRFAPRL SSPQTPAAAP
     NLGLLDLELM HNFCTSTYAT LSNDSAIRDL WRIRIVRLCL NCDYAMLAIL SVSALHLSHF
     STERREFLRE RAITYHNQAL SIASAFIDAY NDKNAQHLFA FSILTIYYSF AQTPEHDDGP
     YPPWVVLIKG CTSFMALARS TLLVGPFSAL LQKARRRLEL REQTFKTDYM QQLRFFVDET
     ITDSERRSVY HDAIHGLNQT YGSHRMRDAK IAKGYGHRVE VEAGLQPAHQ PRNRFQLKLQ
     AKMELFPRID TLADGKVDFK LYRYTPSFPA AIVATVIFAI LSCLHIWRLS KARAWYFIPF
     TIGGAFETIG YAARIVSHNN KESVPAYSVQ AILILVAPAL FAASIYMILG RIIISLRAQH
     LSLIPVRWLT KVFVCGDIVS FSLQAAGGGI QASGTIEAYD RGEKIILAGL FIQIVVFGFF
     VITSGLFHRK CLKNPTLAAR ENAFPWKLDL KVLYTVSIII LVRSVFRVVE YLQGNGGYLI
     SHEVFLYIFD AILMAIVMVI FLIWYVDHLQ YKDGNEYDLE PCVVDETNSS
//
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