ID A0A443HYW8_BYSSP Unreviewed; 806 AA.
AC A0A443HYW8;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE SubName: Full=Quinate repressor protein {ECO:0000313|EMBL:RWQ97042.1};
GN ORFNames=C8Q69DRAFT_443445 {ECO:0000313|EMBL:RWQ97042.1};
OS Byssochlamys spectabilis (Paecilomyces variotii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Thermoascaceae; Paecilomyces.
OX NCBI_TaxID=264951 {ECO:0000313|EMBL:RWQ97042.1, ECO:0000313|Proteomes:UP000283841};
RN [1] {ECO:0000313|EMBL:RWQ97042.1, ECO:0000313|Proteomes:UP000283841}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101075 {ECO:0000313|EMBL:RWQ97042.1,
RC ECO:0000313|Proteomes:UP000283841};
RX PubMed=30619145; DOI=10.3389/fmicb.2018.03058;
RA Urquhart A.S., Mondo S.J., Makela M.R., Hane J.K., Wiebenga A., He G.,
RA Mihaltcheva S., Pangilinan J., Lipzen A., Barry K., de Vries R.P.,
RA Grigoriev I.V., Idnurm A.;
RT "Genomic and genetic insights into a cosmopolitan fungus, Paecilomyces
RT variotii (Eurotiales).";
RL Front. Microbiol. 9:3058-3058(2018).
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:RWQ97042.1}.
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DR EMBL; RCNU01000003; RWQ97042.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A443HYW8; -.
DR STRING; 264951.A0A443HYW8; -.
DR OrthoDB; 2256238at2759; -.
DR Proteomes; UP000283841; 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; 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:UP000283841}.
FT DOMAIN 498..578
FT /note="Shikimate dehydrogenase substrate binding N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08501"
FT DOMAIN 620..668
FT /note="Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA
FT reductase"
FT /evidence="ECO:0000259|Pfam:PF01488"
FT DOMAIN 760..790
FT /note="SDH C-terminal"
FT /evidence="ECO:0000259|Pfam:PF18317"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 806 AA; 90295 MW; 7E7FAC4734F5F807 CRC64;
MEHHTGLPGS RKRAFWGTTE ASEAGEPQAK YPSNKLRVTG DITGTDDNYV ISNLKSDVDG
HQLCNHQPRP LRHQYKGDES LVLVGFWGAG KRTLGFIASV ALRREFVDFD AIFERKTKLS
RGAYIASHGP KAYRIVEYEI TVEVLRTKKE GCVLAGFFMM ADRRQCQLLH ELSKTNPVIH
VMRDKGDLLD SLGHDRGKAE HAYEISNRLC GQYSNFDYFN MTQQFTPNAI GPLKLKQTEQ
DFVRFIRGVF NQRPCLVRSA NALSRSYTYA LQVPAAWLDR SDVDLTELDS GADSINLIFD
PSFAEQKCLS SLSRQIAVLR RHTRVPIILD IHVQNGLEQA RHADILQLAL RQLPDMITVS
LDTDYTLVDV LSVAKCHTKI IGTTQLSDRW PTEKDSLRWQ IIYDKANSLG CDAVRITRIP
TSPLENLDCI NFMMRIIQPC EIPVMGYNVG LIGITSVCFS PTLSPVVLSS MERDGVTLKQ
AQHALYSSFT LRKKRFAIFG QSLSYSLSPT MHNAAYRACG MPHSCYTAES NQFQDINRLL
QNDEIGGLAI ALPYKVQFLS ILDEMTPDVR DIGAVNTVVV DRQHDRDGTL KTFLKGYNTD
HMGVRICMER NLSPANVITS ETSVLILGAG GIARAAIYAC YQAGVRKICI FNRTSSNARH
LAERFRQWAT SRASTPLHIV VLESLNAPWP SNMSQPTIIM SCRPAHEIGG QEPPAFDIPE
QWLGSKTGGV FIELAYEPLV TPLMKQMIQR SSRGWIVVDG LDVLVEQGIA QFEILTGRPA
PVHVMKRAVR EQYQATRGSY DRHNSG
//
