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Database: UniProt
Entry: W7TL47_9STRA
LinkDB: W7TL47_9STRA
Original site: W7TL47_9STRA 
ID   W7TL47_9STRA            Unreviewed;       554 AA.
AC   W7TL47;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=shikimate kinase {ECO:0000256|ARBA:ARBA00012154};
DE            EC=2.7.1.71 {ECO:0000256|ARBA:ARBA00012154};
GN   ORFNames=Naga_100108g2 {ECO:0000313|EMBL:EWM21156.1};
OS   Nannochloropsis gaditana.
OC   Eukaryota; Sar; Stramenopiles; Ochrophyta; Eustigmatophyceae;
OC   Eustigmatales; Monodopsidaceae; Nannochloropsis.
OX   NCBI_TaxID=72520 {ECO:0000313|EMBL:EWM21156.1, ECO:0000313|Proteomes:UP000019335};
RN   [1] {ECO:0000313|EMBL:EWM21156.1, ECO:0000313|Proteomes:UP000019335}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B-31 {ECO:0000313|EMBL:EWM21156.1,
RC   ECO:0000313|Proteomes:UP000019335};
RX   PubMed=23966634; DOI=10.1093/mp/sst120;
RA   Corteggiani Carpinelli E., Telatin A., Vitulo N., Forcato C., D'Angelo M.,
RA   Schiavon R., Vezzi A., Giacometti G.M., Morosinotto T., Valle G.;
RT   "Chromosome Scale Genome Assembly and Transcriptome Profiling of
RT   Nannochloropsis gaditana in Nitrogen Depletion.";
RL   Mol. Plant 7:323-335(2014).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + shikimate = 3-phosphoshikimate + ADP + H(+);
CC         Xref=Rhea:RHEA:13121, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:36208, ChEBI:CHEBI:145989, ChEBI:CHEBI:456216;
CC         EC=2.7.1.71; Evidence={ECO:0000256|ARBA:ARBA00000172};
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC       chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC       5/7. {ECO:0000256|ARBA:ARBA00004842}.
CC   -!- SIMILARITY: Belongs to the shikimate kinase family.
CC       {ECO:0000256|ARBA:ARBA00006997}.
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:EWM21156.1}.
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DR   EMBL; AZIL01002627; EWM21156.1; -; Genomic_DNA.
DR   AlphaFoldDB; W7TL47; -.
DR   EnsemblProtists; EWM21156; EWM21156; Naga_100108g2.
DR   OrthoDB; 865at2759; -.
DR   UniPathway; UPA00053; UER00088.
DR   Proteomes; UP000019335; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004765; F:shikimate kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008652; P:amino acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd00464; SK; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   HAMAP; MF_00109; Shikimate_kinase; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR031322; Shikimate/glucono_kinase.
DR   InterPro; IPR000623; Shikimate_kinase/TSH1.
DR   InterPro; IPR023000; Shikimate_kinase_CS.
DR   PANTHER; PTHR21087; SHIKIMATE KINASE; 1.
DR   PANTHER; PTHR21087:SF16; SHIKIMATE KINASE 1, CHLOROPLASTIC-RELATED; 1.
DR   Pfam; PF01202; SKI; 1.
DR   PRINTS; PR01100; SHIKIMTKNASE.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS01128; SHIKIMATE_KINASE; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW   Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EWM21156.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019335};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        80..102
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          159..180
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          448..554
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        468..492
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        534..554
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   554 AA;  60879 MW;  287EFC35A9BB6BF0 CRC64;
     MREGGWVVDG CNLSHPSRFL PLLPFVHPQA RGLRVGNLLP FTAPSISQQF PDSTLLLRLR
     TSTAVMDQLH QFHHPRRIQV LFPLVILLLS FLSSGTQGFL LFPSSILSSA PSRNIRLPQR
     ASPCSSRNLP STSSRLLPFY PASLSSSLSF DPSRFVRPQT QSLAASSSSP EEEGNNENTA
     EESAAIWGLT DLGNSNFGKF GSEQDPHRNI RPQFLDGRGA PWKEGADFLP ELMEIKMRIQ
     GVNVYLVGMP GSGKTTLGRM LAEGLQYRWM DLDQFIEQKL GKAATKVFEE DGEEVWRKQE
     TLGMGALQTY VQTVVSTGGG IMQRKENLPF LHSGLIVWLD LPPEGIVARM QSSGEIEKRP
     LLKAASDPVQ AVRSLYEERK GNYALADVRV VLRGEDDAVK CLKRVAHRII EELDLRPPKA
     KMWEEKRNKM KNLWETMKAK GSMTDINEVP AEEGGENPTI GAIKALNRDS KGKGEGKKDW
     GGKADKRGQK KKGFGGAVRK GGEGSSQEGR QESAPETAAV GSQGVGFGLG LEEYMKGEEG
     KRKEGEDGEV AEAA
//
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