ID K3VZX8_FUSPC Unreviewed; 848 AA.
AC K3VZX8;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EKJ73175.1};
GN ORFNames=FPSE_06599 {ECO:0000313|EMBL:EKJ73175.1};
OS Fusarium pseudograminearum (strain CS3096) (Wheat and barley crown-rot
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=1028729 {ECO:0000313|EMBL:EKJ73175.1, ECO:0000313|Proteomes:UP000007978};
RN [1] {ECO:0000313|EMBL:EKJ73175.1, ECO:0000313|Proteomes:UP000007978}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CS3096 {ECO:0000313|EMBL:EKJ73175.1,
RC ECO:0000313|Proteomes:UP000007978};
RX PubMed=23028337; DOI=10.1371/journal.ppat.1002952;
RA Gardiner D.M., McDonald M.C., Covarelli L., Solomon P.S., Rusu A.G.,
RA Marshall M., Kazan K., Chakraborty S., McDonald B.A., Manners J.M.;
RT "Comparative pathogenomics reveals horizontally acquired novel virulence
RT genes in fungi infecting cereal hosts.";
RL PLoS Pathog. 8:E1002952-E1002952(2012).
CC -!- SIMILARITY: In the 2nd section; belongs to the type-I 3-dehydroquinase
CC family. {ECO:0000256|ARBA:ARBA00006477}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the shikimate kinase
CC family. {ECO:0000256|ARBA:ARBA00009349}.
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:EKJ73175.1}.
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; AFNW01000183; EKJ73175.1; -; Genomic_DNA.
DR RefSeq; XP_009257992.1; XM_009259717.1.
DR AlphaFoldDB; K3VZX8; -.
DR EnsemblFungi; EKJ73175; EKJ73175; FPSE_06599.
DR GeneID; 20365217; -.
DR KEGG; fpu:FPSE_06599; -.
DR eggNOG; KOG0692; Eukaryota.
DR HOGENOM; CLU_008871_0_1_1; -.
DR OrthoDB; 2256238at2759; -.
DR Proteomes; UP000007978; Chromosome 2.
DR GO; GO:0003855; F:3-dehydroquinate dehydratase activity; IEA:InterPro.
DR GO; GO:0004764; F:shikimate 3-dehydrogenase (NADP+) activity; IEA:InterPro.
DR CDD; cd00502; DHQase_I; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR Gene3D; 3.40.50.10860; Leucine Dehydrogenase, chain A, domain 1; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR046346; Aminoacid_DH-like_N_sf.
DR InterPro; IPR001381; DHquinase_I.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR041121; SDH_C.
DR InterPro; IPR031322; Shikimate/glucono_kinase.
DR InterPro; IPR013708; Shikimate_DH-bd_N.
DR InterPro; IPR022893; Shikimate_DH_fam.
DR InterPro; IPR006151; Shikm_DH/Glu-tRNA_Rdtase.
DR PANTHER; PTHR21089:SF1; BIFUNCTIONAL 3-DEHYDROQUINATE DEHYDRATASE_SHIKIMATE DEHYDROGENASE, CHLOROPLASTIC; 1.
DR PANTHER; PTHR21089; SHIKIMATE DEHYDROGENASE; 1.
DR Pfam; PF01487; DHquinase_I; 1.
DR Pfam; PF18317; SDH_C; 1.
DR Pfam; PF01488; Shikimate_DH; 1.
DR Pfam; PF08501; Shikimate_dh_N; 1.
DR Pfam; PF01202; SKI; 1.
DR PRINTS; PR01100; SHIKIMTKNASE.
DR SUPFAM; SSF51569; Aldolase; 1.
DR SUPFAM; SSF53223; Aminoacid dehydrogenase-like, N-terminal domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000007978}.
FT DOMAIN 521..600
FT /note="Shikimate dehydrogenase substrate binding N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08501"
FT DOMAIN 653..701
FT /note="Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA
FT reductase"
FT /evidence="ECO:0000259|Pfam:PF01488"
FT DOMAIN 809..838
FT /note="SDH C-terminal"
FT /evidence="ECO:0000259|Pfam:PF18317"
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 695..721
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 848 AA; 94168 MW; 7AF4B966CBA610C6 CRC64;
MSTTPHPDDE TANFTRSPYT PSTRAGTPKD LPEYSNAPTP KTPKSRTYSP DAIRRATEYA
PDASIALIGM RGSGLSTLAV LASSTLGFRV LDADQYFYKV TGLSRAAYKA AHGISKYRHE
ELQLMRSMLF DNPTGAIIVC GPGAVEGKGK EWLTEFAKEH LVIYILRDAE DIQRHLRVFD
LDTIRNLIRR ATPAYRRLSN FEYYNTSDTS LQKSDTSPSR GDLSPSALAL KNVEKDFLNL
IHGIVRRDDS YGKYKAQHSL SCLPLVSRSF TYALSIPLAT LIALVSELRE VDIEADAVEF
SIPMSTLCKD GHELDDTATD SISRQVSIVR RNICLPIIYQ VNSYDMQQVN ADEYFRFLDH
GLRLGAEYLC VDLAFDTARI QNLVSSKGQT KIIGHYSASD NGDDGWDSPK QWAMIQRAHT
LGCDILRICK KATSLADNFA AQHFVHRVKA SQQYTIPIIA YNTGHLGRMS CYLNSILSPV
THPLIRNLAP DCPSSHSRLT VKESQKATFA SFLLDDQFFG IYGNNTSKSL SPAMHEAAFK
LLGMPHRYNI YTKDSMDDLF EMVKNVKFGG ASITAPFKTA VIPKLDFLSE EAKAIGAVNT
MICLKSPTVD SLLDRNTAGP TVALFGENTD WIGIHTCVQR NLSPINAVRR RTTGLIVGAG
GMARAAAYAF LRLGIKTIVV HNRTRSKAEE LIKQFKSQEN STNRHDEAGF PGSERKSESP
DRMVDPVFKI LDSKKDKWPE DLSLPTIVVS CIATKDVDGK CSVDTSLPGD WLSSPTGGVV
IELSYTPLET PLLQQAKQLA DRGWIAVDGL QVLPEQGMMQ FELFTTRRAP ANVMRQAVFR
AYNKRVRR
//
