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Database: UniProt
Entry: A0A0A1UT32_9HYPO
LinkDB: A0A0A1UT32_9HYPO
Original site: A0A0A1UT32_9HYPO 
ID   A0A0A1UT32_9HYPO        Unreviewed;       863 AA.
AC   A0A0A1UT32;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   SubName: Full=Negative regulator of quinate utilization {ECO:0000313|EMBL:EXU98987.1};
GN   ORFNames=X797_007985 {ECO:0000313|EMBL:EXU98987.1};
OS   Metarhizium robertsii.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX   NCBI_TaxID=568076 {ECO:0000313|EMBL:EXU98987.1, ECO:0000313|Proteomes:UP000030151};
RN   [1] {ECO:0000313|EMBL:EXU98987.1, ECO:0000313|Proteomes:UP000030151}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ARSEF 2575 {ECO:0000313|EMBL:EXU98987.1,
RC   ECO:0000313|Proteomes:UP000030151};
RA   Giuliano Garisto Donzelli B., Roe B.A., Macmil S.L., Krasnoff S.B.,
RA   Gibson D.M.;
RT   "The genome sequence of the entomopathogenic fungus Metarhizium robertsii
RT   ARSEF 2575.";
RL   Submitted (FEB-2014) 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:EXU98987.1}.
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DR   EMBL; JELW01000022; EXU98987.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0A1UT32; -.
DR   eggNOG; KOG0692; Eukaryota.
DR   HOGENOM; CLU_008871_0_1_1; -.
DR   OrthoDB; 2256238at2759; -.
DR   Proteomes; UP000030151; 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;
FT   DOMAIN          525..605
FT                   /note="Shikimate dehydrogenase substrate binding N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08501"
FT   DOMAIN          668..719
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          15..57
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        21..50
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   863 AA;  95434 MW;  AFDE554353ECF2EC CRC64;
     MAGVKRSLAA MMADERSLSL GDTTEPITRP RSAKTSVNSS EYTSEAPSPT LPPLNGHMPR
     FSPDASIVIV GVRGAGKTTL AIMAASALKK RIVDLEGAFQ RATNFSSPTY SKVHGTTQCQ
     IKQGDVLQSI LETNTTGCII VCSWMERRVQ GLLRQFAASN PVVHVMRSKE AVQEHLRVES
     GTKWETFWST SNAFFRTCSN LEFFNVSESA AVEKSLSSLR NSNGVDLPPY LALKQAERHL
     LKFFSQIYPA GTIPFFESAY PLASVATEQR QYTYAVDISV EEIIHNRVDI EDCSAGADAM
     QITLEDIQID WAHCRYLDEH TKMANRVTEA VGLVRRSSVL PIIVHIGFPN PSAATTSTYF
     YLDLLSHVLT LAPEMMTVDL RLDDNAIAKL ASLKRSCKLI GHYAPIANFD SWTSPQWISH
     YQRAVRLDCD LVRFVRPAEA VTDNFEVARF RSTVESLPDS HAPIIAYNSG NLGKHSAFLN
     PILTSVSPRL ESQNNEKQRQ TGLLADSATR ALYASFLFDP MKLYVFGANV GYSMSPAMHN
     SALEVCGVPH RYEPYSTNSL QQVRHLIQDP NFAGASIGLP FKVEFITLTD SLSPHAQAIG
     AINTLIPIRH LNDDGTVPTG AASFFRGVNR AGPVLALYGE NTDWIGIRSC IRRGLSPANA
     VRPATCGLVI GAGGMARAAV YALLQVGVSN IAIYNRTVEN GKKLADHFTQ LLQKREFEGL
     GAGVKTKFEV LPTLHHDWQS EFRLPSIIIS CIPTHPIGDV PSPEFRLPES WLENQTGGVI
     VELGYKTLNT PLLQQAMEHA SRRWIAMDGL DLLPDQGFAQ FELFTGKRAP RKTMKKAIFE
     NYPDQYGRSN PEELRRRLQT MLE
//
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