ID A0A0F4ZI68_9PEZI Unreviewed; 986 AA.
AC A0A0F4ZI68;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KKA29900.1};
GN ORFNames=TD95_001496 {ECO:0000313|EMBL:KKA29900.1};
OS Thielaviopsis punctulata.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Microascales; Ceratocystidaceae; Thielaviopsis.
OX NCBI_TaxID=72032 {ECO:0000313|EMBL:KKA29900.1, ECO:0000313|Proteomes:UP000033483};
RN [1] {ECO:0000313|EMBL:KKA29900.1, ECO:0000313|Proteomes:UP000033483}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CR-DP1 {ECO:0000313|EMBL:KKA29900.1};
RA Radwan O., Al-Naeli F.A., Rendon G.A., Fields C.;
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
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:KKA29900.1}.
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DR EMBL; LAEV01000634; KKA29900.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F4ZI68; -.
DR OrthoDB; 2256238at2759; -.
DR Proteomes; UP000033483; 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:UP000033483}.
FT DOMAIN 630..710
FT /note="Shikimate dehydrogenase substrate binding N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08501"
FT DOMAIN 772..839
FT /note="Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA
FT reductase"
FT /evidence="ECO:0000259|Pfam:PF01488"
FT DOMAIN 929..956
FT /note="SDH C-terminal"
FT /evidence="ECO:0000259|Pfam:PF18317"
FT REGION 66..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 986 AA; 108062 MW; ECB7CDA92B6F95C3 CRC64;
MTTASVGVTG VKRSYSSMDV DASQISPATI SPATAAFTAS AQPQSNGSHA KCARLDAYSI
DGIINNDNHS SNTHNNNNNN NTPKNHQPES TARISGQSTP LGLYAQSRAV TPISHNHSHC
QNQTHAAAVT MIPERREPAF SATASIVLVG IRGSGKSTLA IIASTAMKRR VIDCEKTFQQ
ALRLSSAAYM KAHGTAECHR VQAAILRDVL RENAQRCIIV CSWVDRAILS LLRDFSRANP
VIQVLRDPRA IQEHLKIETA EKTQSIVSAS TAIFRTCSNL EFFNISERVR DVASQNLAQV
KDTDDMSGER RPAPYLALKR AERHFLKFLS LVMPNGSIPF IESAFPLASI PTEDRRFTYA
TSVRLSSLLQ DDRGIDIEQL ETGADAIEIV IDDIDIMYGA SRGRRPPPPG TTLDPERGSQ
ITKVFGTIRR DTVIPLIYHI LLPSPANAND SAAFHTLYMD YIQHGLRLAC EYVTIDLRLS
AYEIDHITSQ RHNSKLIGHF TSPPSAPPSP ATSWLDPMWM AHYHRARLQG CNLVRFIKPV
ATIKDNFDIN QLKSKVESLD GPKVPLIAFN SGNRGRHSAV MNHVLTSVGT EPTVGFIPDT
PHPPGPRITA QQATQALYAS FLFDPMKLYV FGSDVDYSLS PAIHNGALAA LGIPHHYRPH
STYNLRGLKE LIDDPYFAGA SVGLPFKVEI IALTHSLSRH ARAIGAVNTL IPVRRLNPDG
SIPEDETLFN CRNRAGPVRA LYGDNTDWVG IRACLRRGLS PANAVRPTSC GLVIGAGGMA
RAAVYAMLQL GVQNIVIYNR TYANAQKLAA HFSQLLQRGD LPLLSSVAES DAAATAAAAA
ALDAQTRFHV IDKLSDPWPG DFRKPTMIVV CIPIHSIGDC PAPHFVAPDS WLESPTGGVL
VDLGYKVLDT PILNQVRALQ HKGWVTMDGL DLLPEQGFAQ FELFTGRRAP RRLMRRFCLQ
AYTDEQGRSD LARLKPRLKD ITEQEP
//
