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Database: UniProt
Entry: A0A094HVT4_9PEZI
LinkDB: A0A094HVT4_9PEZI
Original site: A0A094HVT4_9PEZI 
ID   A0A094HVT4_9PEZI        Unreviewed;       808 AA.
AC   A0A094HVT4;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KFZ19555.1};
GN   ORFNames=V502_03579 {ECO:0000313|EMBL:KFZ19555.1};
OS   Pseudogymnoascus sp. VKM F-4520 (FW-2644).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1420915 {ECO:0000313|EMBL:KFZ19555.1, ECO:0000313|Proteomes:UP000029308};
RN   [1] {ECO:0000313|EMBL:KFZ19555.1, ECO:0000313|Proteomes:UP000029308}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-4520 (FW-2644) {ECO:0000313|Proteomes:UP000029308};
RA   Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA   Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA   Ozerskaya S.M.;
RT   "Population genomics of a fungus Geomyces pannorum provides evidence of
RT   horizontal gene transfer but not of sexual reproduction.";
RL   Submitted (JUL-2014) 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:KFZ19555.1}.
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DR   EMBL; JPKE01001409; KFZ19555.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A094HVT4; -.
DR   STRING; 1420915.A0A094HVT4; -.
DR   HOGENOM; CLU_008871_0_1_1; -.
DR   OrthoDB; 2256238at2759; -.
DR   Proteomes; UP000029308; 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:UP000029308}.
FT   DOMAIN          484..563
FT                   /note="Shikimate dehydrogenase substrate binding N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08501"
FT   DOMAIN          621..667
FT                   /note="Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA
FT                   reductase"
FT                   /evidence="ECO:0000259|Pfam:PF01488"
FT   DOMAIN          769..792
FT                   /note="SDH C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18317"
SQ   SEQUENCE   808 AA;  90200 MW;  D0D5CA48CF77DCB1 CRC64;
     MSVVRSQKPS WPRRGSKSNN TLPVEEAFKF HQTTRHFDCN ATIVLVGSRG SGKRSLAFIG
     ATHLGRRLVT EDQYFQQVTG LSRKDYLSKY GSKEFGRQNV EVLQRMLEDN ETGSIIECGM
     SSLARESQNT LRHYAETHPV IHILRNSARI RLLLNLKDSE AARLEHADKS HQSCSNFEYY
     NLQDSNCECH VEEISQDRRI PSYSFALKDA KQDFSRFLDK ITGLGAKQYA YESPFSVDAL
     PPENRPYTYA IPLSLSDLTN GAIDLPQLDS GGDAIELQVD MLTPNVMTIV SKEVARIRRT
     LGIPIIFHID EVLSNDVGAI ISLLYHAIRL GVEYLVIPLW LEDKTIREIV HVRGETKIIG
     QFIDKKAVSW QDQMWISKFE RAKQFDCHIV RLLRMALTDE DNTDVRAFSS RVATISTRPP
     KLIAYNLGPL GKASVIANTI FSPVTHPAIR QKDSRPENFL ITAQEAMENL YETGVLDGLK
     FVTFGVHVNY SLSPMMHETA YAHLGMKGQY YRYTGSSLDE LAAISQDPRF GGAGISQPFK
     VEIMSRCVAH SRHAKAIGAS NTITALRALP DGSADFLLNQ ANRRGHAGPV CAWFADNTDF
     LGILACLRRN ATPRNVVQPS KTTGLVIGAG GMARASIYAM ILLGCRNIFI YNRTLKNAET
     VADHFNSWAG ALSANGRVVT VLRSRNDPWP VEYQQPTFLV SCVPAHEVEI HSPADFEVPE
     QWLGSPSGGV ALELAYKPLN TPLVQQIRRF RQKTGRAWVM VDGLEFIPAQ GFAQFELMTG
     RRAPRAQMRA AAENNYEKVT GSTTDSMV
//
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