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}.
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; 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
//