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Database: UniProt
Entry: W9XNN2_9EURO
LinkDB: W9XNN2_9EURO
Original site: W9XNN2_9EURO 
ID   W9XNN2_9EURO            Unreviewed;       790 AA.
AC   W9XNN2;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EXJ78920.1};
GN   ORFNames=A1O3_08420 {ECO:0000313|EMBL:EXJ78920.1};
OS   Capronia epimyces CBS 606.96.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Capronia.
OX   NCBI_TaxID=1182542 {ECO:0000313|EMBL:EXJ78920.1, ECO:0000313|Proteomes:UP000019478};
RN   [1] {ECO:0000313|EMBL:EXJ78920.1, ECO:0000313|Proteomes:UP000019478}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 606.96 {ECO:0000313|EMBL:EXJ78920.1,
RC   ECO:0000313|Proteomes:UP000019478};
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 Capronia epimyces CBS 606.96.";
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}.
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:EXJ78920.1}.
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DR   EMBL; AMGY01000008; EXJ78920.1; -; Genomic_DNA.
DR   RefSeq; XP_007736708.1; XM_007738518.1.
DR   AlphaFoldDB; W9XNN2; -.
DR   STRING; 1182542.W9XNN2; -.
DR   GeneID; 19172508; -.
DR   eggNOG; KOG0692; Eukaryota.
DR   HOGENOM; CLU_008871_0_1_1; -.
DR   OrthoDB; 2256238at2759; -.
DR   Proteomes; UP000019478; 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; IPR041121; SDH_C.
DR   InterPro; IPR031322; Shikimate/glucono_kinase.
DR   InterPro; IPR013708; Shikimate_DH-bd_N.
DR   InterPro; IPR022893; Shikimate_DH_fam.
DR   InterPro; IPR006151; Shikm_DH/Glu-tRNA_Rdtase.
DR   PANTHER; PTHR21089:SF1; BIFUNCTIONAL 3-DEHYDROQUINATE DEHYDRATASE_SHIKIMATE DEHYDROGENASE, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR21089; SHIKIMATE DEHYDROGENASE; 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; 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:UP000019478}.
FT   DOMAIN          496..576
FT                   /note="Shikimate dehydrogenase substrate binding N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08501"
FT   DOMAIN          619..677
FT                   /note="Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA
FT                   reductase"
FT                   /evidence="ECO:0000259|Pfam:PF01488"
FT   DOMAIN          751..781
FT                   /note="SDH C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18317"
FT   REGION          32..67
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   790 AA;  86906 MW;  33A8E7A8FD7B3DB7 CRC64;
     MAHSPVPPLG GQTRLQPKRT FEAYEADFGV QLEPAASESA GSRKLTRPGR AEAPALSRPP
     SPSSGNSLYD PRASILLVGF SGAGKRTLGI IAAAALRRQY VSFSSFFESH MGQTPYEYMS
     VHGLPGFRQA EIQITERLLN TCKENHVIGG LTGLGSTAQR EVLRSFAKTN PVIYIQRDKV
     DIEGMFGDKG NLDQLYKAGD TFYRSSSNLD FFNITQTVNT ADNASPVGTL KLKQTETDFI
     RFIHRIYGRP PKLLHSVDPF SPSYTYALQI RLEWLAAGSL EYDKLECGAD MISLVIDPKL
     DRIGHLQDQI PKQMALLRRY TRTPIMIDVL HAQPQDAVNY IRLLRLCLRS APEFLTVALS
     LDSGHLQVVA SAKGFTQMVG VIHQDTPWTG SPAKFQWSAL HDLAKELSCC AVRLTNPAVS
     TSENLPYLHD AGTAREVWTL PLIAYKTGAH GRTSICFNPV LSPVVLPSLQ PQGITVTQAQ
     SALYSSFILS KKKFTIFGRS VAYSLSPAMH NAAYAACGMP HSFSLLQSDE FSSIHSLLED
     EECGGITVSL PFKRKVLPML ASISSEARDI GAVNTVVVQR ERAEDGSPQI KLKGYNTDHI
     GIRKCIERSI SPANSIRDGS TALIIGAGGM ARAAIYACRM LGLTNICIYN RTLEHAQELA
     DYYSRQNMHI HVLRTTQEPW PGQLRQPTVL VSCIPAHSIG GQSAHDLTIP EHWLQSRTGG
     VFIELAYKPI VTRLIRQLQL MSKSGWITVD GLDVLIEQGI AQFEIFTGRP APVHVIRRAV
     RKQYDAVVGA
//
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