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Database: UniProt
Entry: A0A1R2AWZ3_9CILI
LinkDB: A0A1R2AWZ3_9CILI
Original site: A0A1R2AWZ3_9CILI 
ID   A0A1R2AWZ3_9CILI        Unreviewed;       622 AA.
AC   A0A1R2AWZ3;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=Shikimate dehydrogenase substrate binding N-terminal domain-containing protein {ECO:0000259|Pfam:PF08501};
GN   ORFNames=SteCoe_33330 {ECO:0000313|EMBL:OMJ69049.1};
OS   Stentor coeruleus.
OC   Eukaryota; Sar; Alveolata; Ciliophora; Postciliodesmatophora;
OC   Heterotrichea; Heterotrichida; Stentoridae; Stentor.
OX   NCBI_TaxID=5963 {ECO:0000313|EMBL:OMJ69049.1, ECO:0000313|Proteomes:UP000187209};
RN   [1] {ECO:0000313|EMBL:OMJ69049.1, ECO:0000313|Proteomes:UP000187209}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WM001 {ECO:0000313|EMBL:OMJ69049.1};
RA   Slabodnick M., Ruby J.G., Reiff S.B., Swart E.C., Gosai S., Prabakaran S.,
RA   Witkowska E., Larue G.E., Fisher S., Freeman R.M., Gunawardena J., Chu W.,
RA   Stover N.A., Gregory B.D., Nowacki M., Derisi J., Roy S.W., Marshall W.F.,
RA   Sood P.;
RT   "The macronuclear genome of Stentor coeruleus: a giant cell with tiny
RT   introns.";
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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:OMJ69049.1}.
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DR   EMBL; MPUH01001247; OMJ69049.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1R2AWZ3; -.
DR   OrthoDB; 865at2759; -.
DR   Proteomes; UP000187209; Unassembled WGS sequence.
DR   GO; GO:0003855; F:3-dehydroquinate dehydratase activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004764; F:shikimate 3-dehydrogenase (NADP+) activity; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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; IPR031322; Shikimate/glucono_kinase.
DR   InterPro; IPR013708; Shikimate_DH-bd_N.
DR   InterPro; IPR022893; Shikimate_DH_fam.
DR   InterPro; IPR023000; Shikimate_kinase_CS.
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; PF08501; Shikimate_dh_N; 1.
DR   Pfam; PF01202; SKI; 1.
DR   PRINTS; PR01100; SHIKIMTKNASE.
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.
DR   PROSITE; PS01128; SHIKIMATE_KINASE; 1.
PE   4: Predicted;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000187209};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          373..453
FT                   /note="Shikimate dehydrogenase substrate binding N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08501"
SQ   SEQUENCE   622 AA;  71506 MW;  FAFB285D90B7D208 CRC64;
     MRGVGKSTFG MKLAQEIGWE FVDLDFLIQE DLQIDSLGEW ITDNGIDNFR NLEYVYLQKC
     LLFNKTIIST GGGIVEHLQA QTLLMAHYPV IWIRTSLENI SSNLENKTSH RVPLNIYEAY
     AKRVPLFEKI YDYQFNYSTL CVETNSENFN LFCYKVLGKK CPLPNDFSNF GCVSSSEDLD
     VIEKSQYLTA VEIRADFYES IENSYKDLNI VKEKLKGGLS IFTFRGNVDE KYWEILMNAG
     KYLPDFIDVQ FEFGSKWLEN FESLRLAFPS IRIILSYHTE IHNQDFESIF NFMCSLSPDI
     VKFISPCFAL PLTVLPHIHF SLGLENLVTR IKNTYFSPVR LGKSTGKGQL SYEELKNFQL
     SLNIMPEKKC FYLAGNNISR SPAKKLYNRL FSSYGLDYTY EFLETNSLDE VIQTLKSPYC
     LGMSITIPYK ESIIPYLDEI SSEAKILGAV NTIIKRNGRL IGTNTDWHGL YYPLKFRRIH
     KTYNSAAVLG AGGTSKAAIY ALSKLKFKIT LWNRSKERLM LGNWPCMITQ DLDEIKNANV
     IVSTIPGNAE VLLPWLSNKH IVLESAYFPD ETFIGKQANQ SGAVLITGKE MYLYMARYQF
     RIFTGKDISK EIIRNRFPIF KN
//
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