ID A0A484FN15_COLOR Unreviewed; 877 AA.
AC A0A484FN15;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE SubName: Full=Quinate repressor protein {ECO:0000313|EMBL:TDZ19081.1};
GN Name=qa-1s {ECO:0000313|EMBL:TDZ19081.1};
GN ORFNames=Cob_v007995 {ECO:0000313|EMBL:TDZ19081.1};
OS Colletotrichum orbiculare (strain 104-T / ATCC 96160 / CBS 514.97 / LARS
OS 414 / MAFF 240422) (Cucumber anthracnose fungus) (Colletotrichum
OS lagenarium).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum orbiculare species complex.
OX NCBI_TaxID=1213857 {ECO:0000313|EMBL:TDZ19081.1, ECO:0000313|Proteomes:UP000014480};
RN [1] {ECO:0000313|Proteomes:UP000014480}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=104-T / ATCC 96160 / CBS 514.97 / LARS 414 / MAFF 240422
RC {ECO:0000313|Proteomes:UP000014480};
RX PubMed=23252678; DOI=10.1111/nph.12085;
RA Gan P., Ikeda K., Irieda H., Narusaka M., O'Connell R.J., Narusaka Y.,
RA Takano Y., Kubo Y., Shirasu K.;
RT "Comparative genomic and transcriptomic analyses reveal the hemibiotrophic
RT stage shift of Colletotrichum fungi.";
RL New Phytol. 197:1236-1249(2013).
RN [2] {ECO:0000313|Proteomes:UP000014480}
RP GENOME REANNOTATION.
RC STRAIN=104-T / ATCC 96160 / CBS 514.97 / LARS 414 / MAFF 240422
RC {ECO:0000313|Proteomes:UP000014480};
RX PubMed=30893003; DOI=10.1094/MPMI-12-18-0352-A;
RA Gan P., Tsushima A., Narusaka M., Narusaka Y., Takano Y., Kubo Y.,
RA Shirasu K.;
RT "Genome sequence resources for four phytopathogenic fungi from the
RT Colletotrichum orbiculare species complex.";
RL Mol. Plant Microbe Interact. 32:1088-1090(2019).
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:TDZ19081.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AMCV02000021; TDZ19081.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A484FN15; -.
DR STRING; 1213857.A0A484FN15; -.
DR Proteomes; UP000014480; 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:UP000014480}.
FT DOMAIN 534..614
FT /note="Shikimate dehydrogenase substrate binding N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08501"
FT DOMAIN 676..717
FT /note="Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA
FT reductase"
FT /evidence="ECO:0000259|Pfam:PF01488"
FT DOMAIN 819..847
FT /note="SDH C-terminal"
FT /evidence="ECO:0000259|Pfam:PF18317"
FT REGION 1..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 877 AA; 97012 MW; BEFB04A67E079DA2 CRC64;
MDDDDAERKH HVENPSKFIR VDSRNGYGYN ASPKEPQSPR TNSSRHSMAA CSRPDTPVTR
PVTPITHLPN EIPPFPADAS IVLAGIRGAG KSTLAIIAST AMARRAIDCE KVFQQATGLT
SYAYKRAHGQ VECHRRQADV LRDLLDQYSK GFLIVCSWME RGVQTLLRDF CRTHPVVHIV
RDVKAIQEHL KIEDEEKARN LLAASSTIFR TCSNLEFFNV SETADPWVET DAARIESHAG
GQKPPAPYLT LKRAERHFLK FLSLVLPKGS IPFIESAFPL ASIPTEDRRF TYAISVPLSS
LLNNEVDIEE LETGADAIEI VVDGISGAGP AAALDSERAA DIARIIGSIR RSTVVPLIYH
VVLPDSSDSV YMDYILHGLR LCPEYLTLDL RVSDYQLLQI ISMKRRAKII GHLTPAADSP
PWGDSFWMSH YHRARRLGCD LARLIKPVTS IKDNFDVNHL KALVDAITGH KIPLIAYNSG
PRGRHSAAMN HVLTSVVPEA MAARHDPHQP CLTAVQATQA LYNSFLFDPM KMYVFGAHVS
YSLSPAMHNA ALRACGIPHV YRPFSTPTLN GLRELIEDPC FAGASVGLPF KVEIITLTHS
LSRHAQAIGA VNTLVPVRRL NPDGSIPEDE KLFNCRNRAG PVRALYGENT DWIGIRACLR
RGLSPANAVR PTSCGLVIGA GGMARATTYS MLQLGVKNIV VYNRTLENAE KMVGHFTRLL
KRRNLPLLSA TSDVETRFHI IKSLDEPWPE DLRLPTLIVS CIPTHSIGDV PAPNFVAPQA
WLASPTGGCL VELGYKTLDT PILNQARQAS HRGWVTMDGL DLLPEQGFAQ FELFTGRRAP
RRLMRGEVFR AYNPDGQDRS ALAQLQPRLD NIVEQEP
//
