ID A0A1J9QJP6_9PEZI Unreviewed; 904 AA.
AC A0A1J9QJP6;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Quinate pathway repressor protein {ECO:0000313|EMBL:OJD28689.1};
GN ORFNames=BKCO1_1200007 {ECO:0000313|EMBL:OJD28689.1};
OS Diplodia corticola.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC Diplodia.
OX NCBI_TaxID=236234 {ECO:0000313|EMBL:OJD28689.1, ECO:0000313|Proteomes:UP000183809};
RN [1] {ECO:0000313|EMBL:OJD28689.1, ECO:0000313|Proteomes:UP000183809}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 112549 {ECO:0000313|EMBL:OJD28689.1,
RC ECO:0000313|Proteomes:UP000183809};
RA Fernandes I., De Jonge R., Van De Peer Y., Devreese B., Alves A.,
RA Esteves A.C.;
RT "Proteomics and genomics reveal pathogen-plant mechanisms compatible with a
RT hemibiotrophic lifestyle of Diplodia corticola.";
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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:OJD28689.1}.
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DR EMBL; MNUE01000120; OJD28689.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J9QJP6; -.
DR STRING; 236234.A0A1J9QJP6; -.
DR OrthoDB; 2256238at2759; -.
DR Proteomes; UP000183809; Unassembled WGS sequence.
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 CDD; cd01065; NAD_bind_Shikimate_DH; 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; IPR006151; Shikm_DH/Glu-tRNA_Rdtase.
DR PANTHER; PTHR21090; AROM/DEHYDROQUINATE SYNTHASE; 1.
DR PANTHER; PTHR21090:SF27; QUINATE REPRESSOR PROTEIN; 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 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:UP000183809}.
FT DOMAIN 559..639
FT /note="Shikimate dehydrogenase substrate binding N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08501"
FT DOMAIN 698..744
FT /note="Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA
FT reductase"
FT /evidence="ECO:0000259|Pfam:PF01488"
FT DOMAIN 848..874
FT /note="SDH C-terminal"
FT /evidence="ECO:0000259|Pfam:PF18317"
FT REGION 228..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 238..257
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 904 AA; 99418 MW; B898E64FC48CC8AC CRC64;
MAYATAGVKR PYSYIADAPI AAAPRQYHSP PFADSQRDHA YSFDRYESPK SRPGSVPPTP
VSAQSLIAAP RCFSPDASIV LIGVRGTGKS TLAVIASAGF QRRVIDTDHA FQEVAGQCSS
SYRKTHGAAA HNQRQLDVLR TVLAKYDKDC ILVCGTNSIE RGAQLLLQEY SKTHPVIHIV
RDSKSIKDYL KVWDEPKVES LLRASSSIFR ACSNYEFYNY TEKQQTIHSD SPEHSIDDMS
SRSSPSGTRS SQEPPPGQRW PASFLTLKRA ERHFLKFVTL IMARGALRSL ESAYPLSHVP
TTARSYTYAV SVPLQAILSA SLDMEELEVG ADAFEIKVAD HGSLAHPAGP ARLDQISQAF
STVRRTTVVP IIYHVMRTSC GTNMGLPEED YFEIVRHGLR FAPELATVDL EADEQLITQT
IIAKGATKII GDFHKGLSTG WDDKIWVEMY EKGRRLGCDL IRFTRPAGRS EDAFVVHHMR
SRVASLEGPH IPLLAFNVGD SGRTSACFNK TLTSVTHPAL QEFVRERNID APHHPVITSA
EATRALYASF VFDPLRIYVI GAKVNYSLSP AMHTAGFKAL GLPHTYSIHQ TSSLNNAHSI
LSDPNYGGSS VGQPYKIEII ALTHSLSRHA RAIGAVNTLI PVRNLKPDGS IPEDIDLLRE
RSQIGPVKAL YGENTDWIGI RACIRRGLSP ANAVGPRTTA LVVGAGGMAR ATVYALLQLG
VRNIFIHNRT LANAEKLVAH FKRVLSGSGT GSPPLLSARE NAPPTHFGII KSREDAWPES
CRQPTIIVSC IPTNSVGDSP APDFTLPLQW FKSPTGGVVV ELAYRNLDSP LLRQIRSESH
RGWVAMDGLD LLPEQGFAQF ELFTGRRAPR RTMRIEVLKS YRDENGETDP TVQARLDASN
DWEP
//
