ID G3JI97_CORMM Unreviewed; 852 AA.
AC G3JI97;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Quinate pathway repressor protein QutR, putative {ECO:0000313|EMBL:EGX91847.1};
GN ORFNames=CCM_06004 {ECO:0000313|EMBL:EGX91847.1};
OS Cordyceps militaris (strain CM01) (Caterpillar fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Cordyceps.
OX NCBI_TaxID=983644 {ECO:0000313|EMBL:EGX91847.1, ECO:0000313|Proteomes:UP000001610};
RN [1] {ECO:0000313|EMBL:EGX91847.1, ECO:0000313|Proteomes:UP000001610}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CM01 {ECO:0000313|EMBL:EGX91847.1,
RC ECO:0000313|Proteomes:UP000001610};
RX PubMed=22112802; DOI=10.1186/gb-2011-12-11-r116;
RA Zheng P., Xia Y., Xiao G., Xiong C., Hu X., Zhang S., Zheng H., Huang Y.,
RA Zhou Y., Wang S., Zhao G.P., Liu X., St Leger R.J., Wang C.;
RT "Genome sequence of the insect pathogenic fungus Cordyceps militaris, a
RT valued traditional Chinese medicine.";
RL Genome Biol. 12:RESEARCH116.1-RESEARCH116.21(2011).
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}.
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DR EMBL; JH126402; EGX91847.1; -; Genomic_DNA.
DR RefSeq; XP_006671211.1; XM_006671148.1.
DR AlphaFoldDB; G3JI97; -.
DR STRING; 983644.G3JI97; -.
DR GeneID; 18168022; -.
DR KEGG; cmt:CCM_06004; -.
DR VEuPathDB; FungiDB:CCM_06004; -.
DR eggNOG; KOG0692; Eukaryota.
DR HOGENOM; CLU_008871_0_1_1; -.
DR InParanoid; G3JI97; -.
DR OMA; CIPTHPI; -.
DR OrthoDB; 2256238at2759; -.
DR Proteomes; UP000001610; 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:UP000001610}.
FT DOMAIN 514..594
FT /note="Shikimate dehydrogenase substrate binding N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08501"
FT DOMAIN 656..698
FT /note="Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA
FT reductase"
FT /evidence="ECO:0000259|Pfam:PF01488"
FT DOMAIN 798..827
FT /note="SDH C-terminal"
FT /evidence="ECO:0000259|Pfam:PF18317"
FT REGION 14..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 852 AA; 93024 MW; 8DFD5DE79F6CBB8F CRC64;
MTMAGVKRPF ASLTENDAVG RTQPNFASAR DQHRTSITPP DRIASPNVEP FSKTVPEFHK
DATIVLVGVR GSGKSTLAVI ASTALGRTVI DLEAAFQRAH AVTSTTYRKL HGSENCQLKQ
AEILQDSLQK NPTGRILVCS WMSRHAQVLL HEFASTNPIV HIVRDAEAIK SHLKLDNDAK
VESLIAVATI FFRTCTNLEF FNLTEQSPQT AEASPPDDEF IPSLALKHAE KHFTKFLSLL
YPAGTIPFVN SAFPLASIPL EERQFTYIIP LPISHILTRK FDIDDAVCGA DAVEITIDIT
ESDDLSTSHS TLAADVTKAV GIVRRTTVLP IICHLRVKEA ANAAIWDVYT QLIAHTFKLA
PEMVTVDLRL ENDAIRTLLK GRRRSKVIGC REMHVSSEAW NGHHWKALYG KAVDVCCDMV
RFTRPASSLQ DNVEVAQFRT IPAMVPGRGI PVAAYNSGSL GRMSACFNSL LTVTSAANMP
ETPCEPGVDS AITPIQATKA LFAAFVYEPM KLYVFGANVD YSMSPIMHSS ALMGYGMPHV
YRPYSSSSLS GIQHLIRDPC FGGASIGLPF KVEVISITDS LSRHARAIGA VNTLIPIRHL
NDDGSIPAGG TFFNNMNRTG EVRAFYGENT DWIGIKACIQ SGLSPANAVR PSTCGVVIGA
GGMARAAVYA MLQIGVRNIV IYNRTPANAE KVVAHFENLF QRDTDMLLIK GPAAVRFHIL
ATRDAPWPAD YRAPTILISC IPTHQIGEAP APNFTAPAAW LTSPTGGVIF ELGYKTLDTP
LLEQARAAAA RGWVAMDGID LLPEQGFAQF ELFTGRRAPR GLMRRALFRH YKDESGSAVI
PGLRRRMQMM AR
//
