ID F9FYC9_FUSOF Unreviewed; 1141 AA.
AC F9FYC9;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 24-JAN-2024, entry version 51.
DE RecName: Full=L-threonate dehydrogenase {ECO:0000256|ARBA:ARBA00039407};
DE EC=1.1.1.411 {ECO:0000256|ARBA:ARBA00038870};
GN ORFNames=FOXB_11411 {ECO:0000313|EMBL:EGU78067.1};
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:EGU78067.1};
RN [1] {ECO:0000313|EMBL:EGU78067.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fo5176 {ECO:0000313|EMBL:EGU78067.1};
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 -!- FUNCTION: Catalyzes oxidation of L-threonate to 2-oxo-tetronate. Can
CC use either NAD(+) or NADP(+) as cosubstrate, with a preference for
CC NAD(+). {ECO:0000256|ARBA:ARBA00037062}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-threonate + NAD(+) = 2-dehydro-L-erythronate + H(+) + NADH;
CC Xref=Rhea:RHEA:52548, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57561, ChEBI:CHEBI:57945, ChEBI:CHEBI:136669;
CC EC=1.1.1.411; Evidence={ECO:0000256|ARBA:ARBA00036958};
CC -!- SIMILARITY: Belongs to the HIBADH-related family. L-threonate
CC dehydrogenase subfamily. {ECO:0000256|ARBA:ARBA00037979}.
CC -!- SIMILARITY: Belongs to the four-carbon acid sugar kinase family.
CC {ECO:0000256|ARBA:ARBA00005715}.
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:EGU78067.1}.
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; AFQF01002878; EGU78067.1; -; Genomic_DNA.
DR AlphaFoldDB; F9FYC9; -.
DR STRING; 660025.F9FYC9; -.
DR PaxDb; 5507-FOXG_15409P0; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.980.20; Four-carbon acid sugar kinase, nucleotide binding domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.40.50.10840; Putative sugar-binding, N-terminal domain; 1.
DR InterPro; IPR002204; 3-OH-isobutyrate_DH-rel_CS.
DR InterPro; IPR010737; 4-carb_acid_sugar_kinase_N.
DR InterPro; IPR037051; 4-carb_acid_sugar_kinase_N_sf.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR013328; 6PGD_dom2.
DR InterPro; IPR006115; 6PGDH_NADP-bd.
DR InterPro; IPR029154; HIBADH-like_NADP-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR031475; NBD_C.
DR InterPro; IPR042213; NBD_C_sf.
DR PANTHER; PTHR43060; 3-HYDROXYISOBUTYRATE DEHYDROGENASE-LIKE 1, MITOCHONDRIAL-RELATED; 1.
DR PANTHER; PTHR43060:SF17; L-THREONATE DEHYDROGENASE; 1.
DR Pfam; PF14833; NAD_binding_11; 2.
DR Pfam; PF03446; NAD_binding_2; 1.
DR Pfam; PF17042; NBD_C; 1.
DR Pfam; PF07005; SBD_N; 1.
DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 2.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF142764; YgbK-like; 1.
DR PROSITE; PS00895; 3_HYDROXYISOBUT_DH; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 191..310
FT /note="3-hydroxyisobutyrate dehydrogenase-like NAD-binding"
FT /evidence="ECO:0000259|Pfam:PF14833"
FT DOMAIN 346..505
FT /note="6-phosphogluconate dehydrogenase NADP-binding"
FT /evidence="ECO:0000259|Pfam:PF03446"
FT DOMAIN 518..637
FT /note="3-hydroxyisobutyrate dehydrogenase-like NAD-binding"
FT /evidence="ECO:0000259|Pfam:PF14833"
FT DOMAIN 699..937
FT /note="Four-carbon acid sugar kinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF07005"
FT DOMAIN 966..1132
FT /note="Four-carbon acid sugar kinase nucleotide binding"
FT /evidence="ECO:0000259|Pfam:PF17042"
FT REGION 319..340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 319..339
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1141 AA; 121225 MW; 4C367823B358AE46 CRC64;
MPSHSSIGFI GFSPEKAKIA EALQLHLYGT IRVYDTFSDS VELIGAGQVQ RSDSVHHVVQ
HSQIVWIQEK DAEALSETLL GSSSGLIHCM QRQDNPKITH EARLADQLQA LPKDASLMLE
CLALPDYYQG LASRFTEAGR TDIKILDCSV VATSSRTKSS IWTSGSGAAI ESVAFLSKAH
DNVHVISGGL GAANKLRLTS YLLEATHAIT AAEATGLASK AGIDANEIYS IIINAAGNSS
AYEELVPHML QGNSQGKPSI ESLLHNINLV TSSSKSLNFP LPLCSASEQV CLLAYTQGYG
LEHVSSLVKL FESQHQKATP TDASGTYASK TSIDVTPPKT PPSVATIGMV GLGAMGQGMA
QSLVRAGFSV QGYDVWAPSV EKFAASGPSG MSIAASSPAE AAKGTAALIL MVQNAAQAWD
VLFGAGKAAE ELSDGATVIL SSTVPPSEAR RIGDRLESLG RGLSLVDAPV SGGVARAAKG
DLTMICSGTG SALGSVRGII LAMAGKESNI YNVKGGVGAA SSAKLINQLL AGVHIATAAE
SLAFASRLGL DTRQVYDIFN ESTAWSWMFQ NRATQMLDAD WTPHSALAIF VKDLGIVLNE
AKRLASYTPM SAVAHTLYID GAARGWAKES DAGVVRLWEA AGSDVSGSAS VKVSSPTTYQ
ESVKSLPAKV TLATLPAEYT TDLIESTKAR VDSGAMPVLV ALDDDPTGTQ TCNNIDVLAV
WDVGTLKEQF ATDCRGFFIL TNSRALPPTE ARELIVEITT NVNKAAEESG KAFEIVLRGD
STLRGHLPEE PEAVEEVLGK SDGWVFAPFF RQGGRFTIDD VHYVQEDDQL VPAAQTPFAQ
DATFGYKNSN LRQYILEKCG SRFTASSFTS ITLEDLRCGG PAKVEEKLLS GERCADRVII
VNAVADSDMN VFVAGLLAAE EKGYRFIYRT AAAFVSSRLG IKEIPPKSWA EVSLKADVDA
PRTGGLILAG SYVPKTTAQL KALRERRGAD LEVIELDVAQ LIESAEREQK IVDSAISETT
RLISAGRDVL VMTSRTLIKT DEAISSLEIG SKVAAALVRL LVNIQVRPRY IIAKGGITSS
DAATKGLKMR RALIVGQAAP GVPLWRCDEE TSRHRSVPFV VFPGNVGSET TLAEIVEQWA
L
//
