ID A0A094BMK1_9PEZI Unreviewed; 808 AA.
AC A0A094BMK1;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KFY11607.1};
GN ORFNames=V491_07130 {ECO:0000313|EMBL:KFY11607.1};
OS Pseudogymnoascus sp. VKM F-3775.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420901 {ECO:0000313|EMBL:KFY11607.1, ECO:0000313|Proteomes:UP000029338};
RN [1] {ECO:0000313|EMBL:KFY11607.1, ECO:0000313|Proteomes:UP000029338}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-3775 {ECO:0000313|EMBL:KFY11607.1,
RC ECO:0000313|Proteomes:UP000029338};
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:KFY11607.1}.
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DR EMBL; JPJT01004407; KFY11607.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094BMK1; -.
DR HOGENOM; CLU_008871_0_1_1; -.
DR Proteomes; UP000029338; 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:UP000029338}.
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"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 808 AA; 90371 MW; 3DCE0A4A5E21486A CRC64;
MSVTRSQKPS WPRHESKSSN SLPAEEAHKF HQTTRNFDYN ATIVLVGSRG SGKRSLAFIG
ATHLGRRLVT EDQYFQQVTG LSRKDYLSRY GNKEFGRQNV EVLQRMLEDN ETGSIIECGM
SSLARESQIT LRHYAETHPV IHILRNPARI RLLLNLKDSE AARLEHADKS HQSCSNFEYY
NLQDSNCECH VEEISQDRRI PSYSFALKDA KQDFSRFLDK ITGLGAKQSA YESPFSVDAL
PPEDRPYTYA IPLSLSDLTN GAIDLPQLDS GGDAIELQVD MLTPNVMTIL SKEVSRIRRT
LGIPIIFCID EVLSNDASTF ISLLYHAIRL GVEYLVIPLW LEDNIIRKIV GVRGETKIIG
QFIDKNAVSW QDQLWISKFE RAKQFDCHIV RLLRTAHAIE DNADVRAFSS RVAAISPHQP
KLIAYNLGPL GKASIISNTI FSPVTHPAIR QKDSRPENFL ITAQEAMENL YETGVLDGMK
FVTFGAHVNY SLSPMMHGTA YEYLGMKGEY YRYTASSLDE LAAISQDPHF GGAGISQPFK
VEIMSRCIAH SRHAKAIGAS NTITPLRALP DGSPDFLLNQ ANRRGHAGPV CAWFADNTDF
LGILACLRRN ATPRNVVQPS KTTGLVIGAG GMARASIYAM ILLGCRNIFI YNRTLENARK
VADHFNSWAG ALSTNGRVVT VLRSRSEPWP AEYQQPTFLV SCVPAHDVEF HRPRDFEVPE
QWLGSPSGGV ALELAYKPLN TPLVQQIRRF RQKTGRAWVM VDGLEFIPAQ GFAQFELMTG
RRAPRAQMRA AAENNYEKVT GSTTDSMV
//
