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Database: UniProt
Entry: A0A1Y2URM6_9PEZI
LinkDB: A0A1Y2URM6_9PEZI
Original site: A0A1Y2URM6_9PEZI 
ID   A0A1Y2URM6_9PEZI        Unreviewed;       799 AA.
AC   A0A1Y2URM6;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:OTA86706.1};
GN   ORFNames=M434DRAFT_81922 {ECO:0000313|EMBL:OTA86706.1};
OS   Hypoxylon sp. CO27-5.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Xylariomycetidae; Xylariales; Hypoxylaceae; Hypoxylon.
OX   NCBI_TaxID=1001938 {ECO:0000313|EMBL:OTA86706.1, ECO:0000313|Proteomes:UP000194361};
RN   [1] {ECO:0000313|EMBL:OTA86706.1, ECO:0000313|Proteomes:UP000194361}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CO27-5 {ECO:0000313|EMBL:OTA86706.1,
RC   ECO:0000313|Proteomes:UP000194361};
RX   PubMed=28078400; DOI=10.1007/s00253-017-8091-1;
RA   Wu W., Davis R.W., Tran-Gyamfi M.B., Kuo A., LaButti K., Mihaltcheva S.,
RA   Hundley H., Chovatia M., Lindquist E., Barry K., Grigoriev I.V.,
RA   Henrissat B., Gladden J.M.;
RT   "Characterization of four endophytic fungi as potential consolidated
RT   bioprocessing hosts for conversion of lignocellulose into advanced
RT   biofuels.";
RL   Appl. Microbiol. Biotechnol. 101:2603-2618(2017).
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; KZ112567; OTA86706.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y2URM6; -.
DR   STRING; 1001938.A0A1Y2URM6; -.
DR   Proteomes; UP000194361; 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; 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:SF17; QUINATE REPRESSOR PROTEIN; 1.
DR   Pfam; PF01487; DHquinase_I; 1.
DR   Pfam; PF01488; Shikimate_DH; 1.
DR   Pfam; PF08501; Shikimate_dh_N; 1.
DR   Pfam; PF01202; SKI; 1.
DR   PRINTS; PR01100; SHIKIMTKNASE.
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:UP000194361}.
FT   DOMAIN          475..554
FT                   /note="Shikimate dehydrogenase substrate binding N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08501"
FT   DOMAIN          610..658
FT                   /note="Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA
FT                   reductase"
FT                   /evidence="ECO:0000259|Pfam:PF01488"
SQ   SEQUENCE   799 AA;  90204 MW;  4D7C87EF7CF47411 CRC64;
     MIPDSPIIPS SRTKRRIFHA DASIILVGCR GAGKRTLGFI AAKHLGRRLI TEDHSFEQAT
     GCTRATFLQK YGRETFNQQM AIVLARMIKP NQTNCVIECG TGTLSPAIEE ILKGYLETNP
     IIYIHRDKED LYKLLKLPVT DAEPLLIADQ KHRDFSNLEY FNVYDPSGEG HVTEDIPLRS
     ALTSSARLVD AKQDFKNFLD SIFGHSLTRS WVSNPFSIKA IPPEYRTYTY VLHLRLSTLI
     NINVDLAKLE APGEAVEFII DTWPNNMLDI IATQVALIRH KMDVPIIYNV EENPREERKR
     PIEERDAADL ELMLHGFRLG VEYLTLDLER SPHLVTHVLA MRGRTKIIGN YVARGFGAPK
     WTDDFYIERY LYAQRLGCNI VRIARFCAAA RDDSLRQAFV DRIRALPDPK PCLIAYDYSV
     FGVVLPFQDK IMNPVGHDSL EKSSREQMAG VSTTRGSLRD VFRKGYLQPL NFYTLGSNVY
     YSASPSMHRA AYEHYMMPHT FDARRCTTLE EVDRIRQEPG FGGASLTAPF KVAIMKHLDH
     LSTHAIAIGA VNTLLPLRGE TDSILDHANS RNRAGVASKF YGDNTDWSSI VTCLRRAISP
     RNSVQPSRTT GLVIGAGGMA RAAIYALIKL GCRMIFIHNR TKAKAEEVAR HFNTYALEQK
     LVRQNDGELI CHVIESPRDP WPDSYQPPTM IVSCIPASGV DDNPPVDFRM PSQWLKSPTG
     GVVIELAYEP LITPLVVQVR KIREEGNTSW VIVDGLEVVG EMAMEAFELM TGRQAPRRLM
     RRVCNETWEK TCAPFQPQR
//
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