ID W2SA93_9EURO Unreviewed; 831 AA.
AC W2SA93;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ETN45651.1};
GN ORFNames=HMPREF1541_09483 {ECO:0000313|EMBL:ETN45651.1};
OS Cyphellophora europaea CBS 101466.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Cyphellophoraceae; Cyphellophora.
OX NCBI_TaxID=1220924 {ECO:0000313|EMBL:ETN45651.1, ECO:0000313|Proteomes:UP000030752};
RN [1] {ECO:0000313|EMBL:ETN45651.1, ECO:0000313|Proteomes:UP000030752}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101466 {ECO:0000313|EMBL:ETN45651.1,
RC ECO:0000313|Proteomes:UP000030752};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Phialophora europaea CBS 101466.";
RL Submitted (MAR-2013) 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; KB822712; ETN45651.1; -; Genomic_DNA.
DR RefSeq; XP_008712379.1; XM_008714157.1.
DR AlphaFoldDB; W2SA93; -.
DR STRING; 1220924.W2SA93; -.
DR GeneID; 19976822; -.
DR VEuPathDB; FungiDB:HMPREF1541_09483; -.
DR eggNOG; KOG0692; Eukaryota.
DR HOGENOM; CLU_008871_0_1_1; -.
DR InParanoid; W2SA93; -.
DR OrthoDB; 2256238at2759; -.
DR Proteomes; UP000030752; 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:UP000030752}.
FT DOMAIN 498..578
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 782..812
FT /note="SDH C-terminal"
FT /evidence="ECO:0000259|Pfam:PF18317"
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 831 AA; 91698 MW; 21DB0C721C700E6B CRC64;
MSTPSQDRAT RSAPGSPRIM QKPPSLDRDG LFNHHGACSD HGTPSAATTN RTFSPDASIV
LVGVRGSGKR SLGLIAAAAL GRRFVTEDHF FQSVTGLSRQ DYLKLHGSEE FHKQDVDVTR
RMLEENKHRC VIDCGLGSLT SSLQEYLKQY CLTNPVVYLV RDMSRIRSLL NLGDRSARLL
EAGDPSHRKC SNFEFYNLED DTSGIPDEEL TDRTSPVYSF KLRQAQEDFS RFVRLITGNA
NDASPVSPFA LDVHLQARAY THALEVPLSR YGDSLDLKSL QAAGDVVELV VDRWHPSLTK
NLSKLVASIR RYVGTPIIIS LRLASFSPDV LTAILNHGLR LGIEYLSLDL ELDTERLVNL
IATRGHTRII GTFRSARTQL GWHDPLLFDL LKKADELHCD YVRIMLPALF REDHESLDWF
RDEVKSKLQI KAPLIAFNTG NLGRTSQALN PLLTSVTHPG LSLGGQGDAD MLAPVLTSSQ
ALRALGTSFM LDALQFCIVG GDVSDSLSPA MHNAAYEALG LHHSYTTRNI TSWDEVETLA
KNSHFGGASV VQPWKVKAVE KLSSLSANAK AIGAVNTLIP LRIDSNGRLM SLEQQAYNRN
RAGNIAGWHG DNTDFVGIKV CLNRSLSPRN VIHSKTTGLV VGAGGMARAA VYAMLQLGCR
NVFVYNRTTS NARAVANHFN DWLSKRSAPT NGSTSDMVRV LESLDEPWEA GFSMPTMVVS
CVTHEHIEGN VGSEFEIPKQ WLESPSGGVV VEMAYMTKET ALTKQIAQFR ASTGSPWVIV
SGVDTLIEQA VAQFEIFTAR RAPRAAMMQA VRAEMQTNRQ YMMDWGSYRP W
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