ID T0LRD8_COLGC Unreviewed; 886 AA.
AC T0LRD8;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Shikimate dehydrogenase substrate binding domain-containing protein {ECO:0000313|EMBL:EQB54266.1};
GN ORFNames=CGLO_05924 {ECO:0000313|EMBL:EQB54266.1};
OS Colletotrichum gloeosporioides (strain Cg-14) (Anthracnose fungus)
OS (Glomerella cingulata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum gloeosporioides species complex.
OX NCBI_TaxID=1237896 {ECO:0000313|EMBL:EQB54266.1, ECO:0000313|Proteomes:UP000015530};
RN [1] {ECO:0000313|Proteomes:UP000015530}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Cg-14 {ECO:0000313|Proteomes:UP000015530};
RX PubMed=23902260; DOI=10.1094/MPMI-03-13-0080-R;
RA Alkan N., Meng X., Friedlander G., Reuveni E., Sukno S., Sherman A.,
RA Thon M., Fluhr R., Prusky D.;
RT "Global aspects of pacC regulation of pathogenicity genes in Colletotrichum
RT gloeosporioides as revealed by transcriptome analysis.";
RL Mol. Plant Microbe Interact. 26:1345-1358(2013).
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:EQB54266.1}.
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DR EMBL; AMYD01001180; EQB54266.1; -; Genomic_DNA.
DR AlphaFoldDB; T0LRD8; -.
DR STRING; 1237896.T0LRD8; -.
DR eggNOG; KOG0692; Eukaryota.
DR HOGENOM; CLU_008871_0_1_1; -.
DR OMA; CIPTHPI; -.
DR OrthoDB; 2256238at2759; -.
DR Proteomes; UP000015530; 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:UP000015530}.
FT DOMAIN 543..623
FT /note="Shikimate dehydrogenase substrate binding N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08501"
FT DOMAIN 685..727
FT /note="Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA
FT reductase"
FT /evidence="ECO:0000259|Pfam:PF01488"
FT DOMAIN 828..856
FT /note="SDH C-terminal"
FT /evidence="ECO:0000259|Pfam:PF18317"
FT REGION 20..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..60
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 886 AA; 97868 MW; 47894CC439C24FFD CRC64;
MATAGVKRSF VATAIDDEDA EHHHQLENPS KFIRVDTRNG YSTTPREPQS PRTNSSRYSM
AACSRPETPI TRPATPVTHL PNEIPPFPAD ASIVLAGIRG AGKSTLAIIA STAMARRALD
CEKAFQQVTG LTSFAYKRAH GPAECHRRQT DVLRDLLDQN SKGCLIVCSW MERSVQTLLR
DFCRTHPVVH IVRDVKAIQE HLKIEDEDKA RNLLAASSTI FRTCSNLEFF NVSETADPAA
ETDAARIEAH AGGQKPPAPY LTLKRAERHF LKFLSLIMPK GSIPFIESAF PLASIPTEDR
RFTYAISVSL SSLLNNEITV EELETGADAI EIVVDGLAGA TALDSERAAD IARIIGSIRR
STVIPLIYHV VLPDTTESVY MDYILHGLRL TPEYLTVDLR LNDYQLLHII SMKRRSKIIG
HLTPAVDSPS WADPFWMSHY HRARRIGCDL VRLVKPVTSI KDNFDVNHLK ALVDATTGHK
IPLIAYNSGP RGRHSAAMNH VLTSVVPEAM ASKYSPDQPC LTAVQATQAL YNSFLFDPMK
IYVFGAHVSY SLSPAMHNAA LKACGIPHVY RPFSTPSLNG LKDLIEDPYF AGASVGLPFK
VEIITLTHSL SRHAQAIGAV NTLVPVRRLN PDGTIPEDEK LFNCRNRAGP VRALYGENTD
WIGIRACLRR GLSPANAVRP TSCGLIIGAG GMARAATYSM LQLGVKNIVV YNRTVSNAEK
MVNHFTRLLK RHDLPLLSAN TDAETRFHII RTLDEAWPED FRPPTMIVSC IPTHSIGDVP
APNFVAPQAW LSSPTGGCLV ELGYKTLDTP ILNQARQVSH RGWVTMDGLD LLPEQGFAQF
ELFTGRRAPR RLMRGEVFRS YEPDGQDRSA LAQLGPRLNN IVEQEP
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