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Database: UniProt
Entry: Q2TY14_ASPOR
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Original site: Q2TY14_ASPOR 
ID   Q2TY14_ASPOR            Unreviewed;       812 AA.
AC   Q2TY14;
DT   24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT   24-JAN-2006, sequence version 1.
DT   27-MAR-2024, entry version 78.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:BAE65859.1};
GN   ORFNames=AO090103000430 {ECO:0000313|EMBL:BAE65859.1};
OS   Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=510516 {ECO:0000313|EMBL:BAE65859.1, ECO:0000313|Proteomes:UP000006564};
RN   [1] {ECO:0000313|EMBL:BAE65859.1, ECO:0000313|Proteomes:UP000006564}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42149 / RIB 40 {ECO:0000313|Proteomes:UP000006564};
RX   PubMed=16372010; DOI=10.1038/nature04300;
RA   Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA   Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA   Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA   Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA   Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA   Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA   Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA   Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA   Takahashi M., Takase K., Terabayashi Y., Wortman J., Yamada O.,
RA   Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA   Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA   Kikuchi H.;
RT   "Genome sequencing and analysis of Aspergillus oryzae.";
RL   Nature 438:1157-1161(2005).
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; AP007174; BAE65859.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2TY14; -.
DR   STRING; 510516.Q2TY14; -.
DR   EnsemblFungi; BAE65859; BAE65859; AO090103000430.
DR   VEuPathDB; FungiDB:AO090103000430; -.
DR   HOGENOM; CLU_008871_0_1_1; -.
DR   OMA; AQYELFT; -.
DR   OrthoDB; 2256238at2759; -.
DR   Proteomes; UP000006564; Chromosome 8.
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; 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:UP000006564}.
FT   DOMAIN          512..592
FT                   /note="Shikimate dehydrogenase substrate binding N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08501"
FT   DOMAIN          635..681
FT                   /note="Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA
FT                   reductase"
FT                   /evidence="ECO:0000259|Pfam:PF01488"
FT   DOMAIN          774..804
FT                   /note="SDH C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18317"
SQ   SEQUENCE   812 AA;  90765 MW;  30AE9F9B639A71C0 CRC64;
     MDSISVFETF TGVWVVRSGL CVSHDSHWWS SSPSPRASYI SSCETGANRR LTPLATLELR
     HIDVFQVPSS HVQHHGLPSS SRRYSSDASL VLVGFPGAGK KTLGIMAAVA LRRRLVDFVA
     VFQQRHGMHP QAYIVSHGSE RYRKLELEVT EEILTEHRKG CVIVGLGWLA SRQQQVLLEE
     FASCHPVLYI RRDRRDLQQL IATSQDKFER MWDAGNSFFE SCSNLEFYNV TEGSTDEARS
     ALPAYLKLKE TERTFVRFLH RIWGREHLTR YSADPLSASY TYALQVPMAC LEGPLESYEE
     LENGADAINL KVELSEFHGR RPSESMARAV AMLRRHSRAL VIVDIIPSSV PDILSYRKLL
     GMALRTIPDA ITCSMAHGDD LAQEVAAAKG YIKAIATYHQ EYSLARNETR PELFTFRQKA
     QSIGFDAIHI TGESTAPGDS LHGISFPHTL AKDSLIPTIA YDTGLFGRTS VCLNPILSPV
     VLESMKPTGV TLREAEMAVS ACFLRRRKRF GIFGQQLSHT LSPAMHNAAY AACGLPYTYG
     IAERERLSDI REILDDESYG GVAVSLPYKT EVLPYLDEIS PEALDINAVN TVVLHQECQP
     NGVRKTIRKG YNTDYLGIKD CIYKHLSPAN AIRDGSTALI IGAGGMAHAA IYACYQLGVR
     RICVYNRTLS NARRLVDYYR EWVKSKDKAP LELTILSSAD DPWPAHLRQP TVIVSCIPGQ
     KCDIESSSAL NIPDHWLQSR TGGVFVEVAY DPLETRLIRS MRQHVSRGWI IVDGLSVLVE
     QGIAQYELFT TRPAPVHVMR RAIQQSILER TV
//
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