ID A0A2J6STL4_9HELO Unreviewed; 804 AA.
AC A0A2J6STL4;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:PMD54099.1};
GN ORFNames=K444DRAFT_570685 {ECO:0000313|EMBL:PMD54099.1};
OS Hyaloscypha bicolor E.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Hyaloscyphaceae; Hyaloscypha; Hyaloscypha bicolor.
OX NCBI_TaxID=1095630 {ECO:0000313|EMBL:PMD54099.1, ECO:0000313|Proteomes:UP000235371};
RN [1] {ECO:0000313|EMBL:PMD54099.1, ECO:0000313|Proteomes:UP000235371}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E {ECO:0000313|EMBL:PMD54099.1,
RC ECO:0000313|Proteomes:UP000235371};
RG DOE Joint Genome Institute;
RA Martino E., Morin E., Grelet G., Kuo A., Kohler A., Daghino S., Barry K.,
RA Choi C., Cichocki N., Clum A., Copeland A., Hainaut M., Haridas S.,
RA Labutti K., Lindquist E., Lipzen A., Khouja H.-R., Murat C., Ohm R.,
RA Olson A., Spatafora J., Veneault-Fourrey C., Henrissat B., Grigoriev I.,
RA Martin F., Perotto S.;
RT "A degradative enzymes factory behind the ericoid mycorrhizal symbiosis.";
RL Submitted (APR-2016) 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}.
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DR EMBL; KZ613866; PMD54099.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2J6STL4; -.
DR STRING; 1095630.A0A2J6STL4; -.
DR InParanoid; A0A2J6STL4; -.
DR OrthoDB; 2256238at2759; -.
DR Proteomes; UP000235371; 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:SF17; 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:UP000235371}.
FT DOMAIN 483..561
FT /note="Shikimate dehydrogenase substrate binding N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08501"
FT DOMAIN 625..670
FT /note="Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA
FT reductase"
FT /evidence="ECO:0000259|Pfam:PF01488"
FT DOMAIN 766..792
FT /note="SDH C-terminal"
FT /evidence="ECO:0000259|Pfam:PF18317"
SQ SEQUENCE 804 AA; 89576 MW; C47B639D46DA5937 CRC64;
MSVTTQLAPS LSSSWNIENR PSPCIRDFPP EASIVLVGSR GSGKRTLGFI GATHLGRRLI
TEDHCFQEAT GTTRGIFLRQ YGNQAFYRKN VEVLKQMLDN HRTGCIIECG MGSLSYPAQK
ALAEYSKTHP VIYITRGSHR IKSLLRLGDE EAARLEIADL AHRNCSNLEY YNLYDPSGDG
AETPPENGLG NVSSRLKYAK EDFSSFLDLL TGQGVIRSGF ESPFSIAALP PECRSFTYAL
SLRLSTIPAI DLVELEAGAD AVQLKIDTWS PDLQKLIGKQ VATIRRNLGV PVIFQVENYA
FEGTQLTMAE REHAYFILME WALRLAVEYI IVDLKYSSER VSHLVRSSGR TRVIGHYLSR
DENPWGWDED TSMTEYNKAK SLGCDIVRFV RATSKESDND FVRAFVNRIE SIPDHLPIIA
YNLGDHGRPS LVANKIFTPV THPIMNTTVS KSQIRQFLPT ASEAMQALYQ SRILDPLHFY
HLGASVFYSL SPAMHTAAYQ VCGMSNDFQS LQVSSLEDIH RIIHDQNFGG AAITQPFKVQ
ILSRIAAKSY HAKAIGAVNT LLPLRTFQNS SPLDGSTESL LRQANQRCKA GPIAAYYGDN
TDFIGIMTCI RRNMSPRNAI QPSKTTGLVI GAGGMARAAV YAMIQLGCRK VFICNRTVEN
AEAVARHFNS WASGLSSDGE IVRVLRSTNE DWPVGYRQPT MIVSCVPARS VGDHAPANFE
MPMQWLGSPT GGVVVELAYL PLDTPLLKQI RRVREEAKQA WVIVDGLEVL PEQAIAQFEL
MTGRKAPKRR MRLEVLQNYH RYEE
//
