ID A0A179F2E5_METCM Unreviewed; 862 AA.
AC A0A179F2E5;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Quinate pathway repressor protein QutR {ECO:0000313|EMBL:OAQ59606.1};
GN ORFNames=VFPPC_03827 {ECO:0000313|EMBL:OAQ59606.1};
OS Pochonia chlamydosporia 170.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Pochonia.
OX NCBI_TaxID=1380566 {ECO:0000313|EMBL:OAQ59606.1, ECO:0000313|Proteomes:UP000078397};
RN [1] {ECO:0000313|EMBL:OAQ59606.1, ECO:0000313|Proteomes:UP000078397}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=170 {ECO:0000313|EMBL:OAQ59606.1};
RX PubMed=27416025;
RA Wang G., Liu Z., Lin R., Li E., Mao Z., Ling J., Yang Y., Yin W.B., Xie B.;
RT "Biosynthesis of antibiotic leucinostatins in bio-control fungus
RT Purpureocillium lilacinum and their inhibition on phytophthora revealed by
RT genome mining.";
RL PLoS Pathog. 12:E1005685-E1005685(2016).
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:OAQ59606.1}.
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DR EMBL; LSBJ02000002; OAQ59606.1; -; Genomic_DNA.
DR RefSeq; XP_018137599.1; XM_018283281.1.
DR AlphaFoldDB; A0A179F2E5; -.
DR STRING; 1380566.A0A179F2E5; -.
DR GeneID; 28847275; -.
DR KEGG; pchm:VFPPC_03827; -.
DR OrthoDB; 2256238at2759; -.
DR Proteomes; UP000078397; 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 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; 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 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:UP000078397}.
FT DOMAIN 525..604
FT /note="Shikimate dehydrogenase substrate binding N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08501"
FT DOMAIN 667..712
FT /note="Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA
FT reductase"
FT /evidence="ECO:0000259|Pfam:PF01488"
FT DOMAIN 808..837
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..44
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 862 AA; 94581 MW; 27E3CA379B460DB9 CRC64;
MAGVKRSLAA MMADERLLSP SIDPSDSTAR SQSARTSAAS SEYATRAPSP ALPSFDGNMP
KFTPDASIVF IGVRGAGKTT LAIMAASALK KRIIDVETAF QRATSFSSAS YSKVHGPTQC
QRKQGEVLQD VLQSNDSGCI IVCSWMERRV QGLLRQFATT NPVVHIMRSK AAVQEHLKVE
SGIKWATFWS TSNAFFRTCS NLEFFNVSES AATEQIQPSI RKSNMADLPP YLALKQAERH
LLKFLSQIYP AGTIPFFESA YPLASVATDE RQFTYAVELS VEDINQDGVD IEGCSAGADA
VQITVGNIQN EWTNSTYREE YTKMANDITE AVGLVRRSSV LPIIVHIDHP QSASTTTTCF
YLDLLSHVLS LAPEMMTVDL RLDDVAISKL STLKRSSKLI GNYSPVENFN SWTSPKWMSL
YQRAVQLDCD LVRFIRPATT MSDNFEVSQF RSAVASLPDT HVPIIAYNSG LLGRHSACLN
PVLTLVSAKP HSPYDPKRDA SILTAQTATN ALYSSFLFDS MKLYVFGVNV SYSMSPAMHN
SALEACGVPH RYEPYSTNSL SQVTHLIHDA NFAGASIGLP FKVECITLAD ALSPHAQAIG
AINTMVPIRQ LNDDGTIPTG SAFFRGVNRA GPVRAIYGEN TDWIGIRACI RRGLSPANAV
RPASCGLVIG AGGMARAAVY ALLQVGVRNI AIYNRTVENG KRLAAHFTQL LQKKEFAGLG
AGTNTKFEVF TQLHDTWQSE FRLPSIIISC IPTHPIGDAP SPEFKLPEPW LGNQTGGVIV
ELGYKTLNTP LLQQAMEHAE QGWIAMDGLD LLPDQGFAQF ELFTGRRAPR RTMRKAIFEN
YPDQYGRSNP EELRRRLQTM VE
//
