(data stored in SCRATCH zone)

SWISSPROT: E6UYZ8_VARPE

ID   E6UYZ8_VARPE            Unreviewed;       312 AA.
AC   E6UYZ8;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   08-MAY-2019, entry version 61.
DE   RecName: Full=Shikimate kinase {ECO:0000256|HAMAP-Rule:MF_00109};
DE            Short=SK {ECO:0000256|HAMAP-Rule:MF_00109};
DE            EC=2.7.1.71 {ECO:0000256|HAMAP-Rule:MF_00109};
GN   Name=aroK {ECO:0000256|HAMAP-Rule:MF_00109};
GN   OrderedLocusNames=Varpa_0105 {ECO:0000313|EMBL:ADU34327.1};
OS   Variovorax paradoxus (strain EPS).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Variovorax.
OX   NCBI_TaxID=595537 {ECO:0000313|EMBL:ADU34327.1, ECO:0000313|Proteomes:UP000008917};
RN   [1] {ECO:0000313|Proteomes:UP000008917}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EPS {ECO:0000313|Proteomes:UP000008917};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L.,
RA   Pitluck S., Teshima H., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Kyrpides N., Ivanova N., Ovchinnikova G., Orwin P.,
RA   Han J.-I.G., Woyke T.;
RT   "Complete sequence of Variovorax paradoxus EPS.";
RL   Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADU34327.1, ECO:0000313|Proteomes:UP000008917}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EPS {ECO:0000313|EMBL:ADU34327.1,
RC   ECO:0000313|Proteomes:UP000008917};
RX   PubMed=24158554;
RA   Han J.I., Spain J.C., Leadbetter J.R., Ovchinnikova G., Goodwin L.A.,
RA   Han C.S., Woyke T., Davenport K.W., Orwin P.M.;
RT   "Genome of the Root-Associated Plant Growth-Promoting Bacterium
RT   Variovorax paradoxus Strain EPS.";
RL   Genome Announc. 1:e00843-13(2013).
CC   -!- FUNCTION: Catalyzes the specific phosphorylation of the 3-hydroxyl
CC       group of shikimic acid using ATP as a cosubstrate.
CC       {ECO:0000256|HAMAP-Rule:MF_00109}.
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|HAMAP-Rule:MF_00109};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00109};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_00109};
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate
CC       biosynthesis; chorismate from D-erythrose 4-phosphate and
CC       phosphoenolpyruvate: step 5/7. {ECO:0000256|HAMAP-Rule:MF_00109}.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00109}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00109}.
CC   -!- SIMILARITY: Belongs to the shikimate kinase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00109}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00109}.
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DR   EMBL; CP002417; ADU34327.1; -; Genomic_DNA.
DR   RefSeq; WP_013538574.1; NC_014931.1.
DR   STRING; 595537.Varpa_0105; -.
DR   EnsemblBacteria; ADU34327; ADU34327; Varpa_0105.
DR   GeneID; 29715604; -.
DR   KEGG; vpe:Varpa_0105; -.
DR   eggNOG; ENOG4107VZ3; Bacteria.
DR   eggNOG; COG0703; LUCA.
DR   HOGENOM; HOG000220121; -.
DR   KO; K15546; -.
DR   OMA; SPEWILL; -.
DR   OrthoDB; 1542870at2; -.
DR   BioCyc; VPAR595537:G1GQO-102-MONOMER; -.
DR   UniPathway; UPA00053; UER00088.
DR   Proteomes; UP000008917; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   GO; GO:0004765; F:shikimate kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd00093; HTH_XRE; 1.
DR   CDD; cd00464; SK; 1.
DR   HAMAP; MF_00109; Shikimate_kinase; 1.
DR   InterPro; IPR001387; Cro/C1-type_HTH.
DR   InterPro; IPR010982; Lambda_DNA-bd_dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR031322; Shikimate/glucono_kinase.
DR   InterPro; IPR000623; Shikimate_kinase/TSH1.
DR   Pfam; PF01381; HTH_3; 1.
DR   Pfam; PF01202; SKI; 1.
DR   SMART; SM00530; HTH_XRE; 1.
DR   SUPFAM; SSF47413; SSF47413; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS50943; HTH_CROC1; 1.
PE   3: Inferred from homology;
DR   PRODOM; E6UYZ8.
DR   SWISS-2DPAGE; E6UYZ8.
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00109};
KW   Aromatic amino acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00109};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00109};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008917};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00109};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00109, ECO:0000313|EMBL:ADU34327.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00109};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00109};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00109};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008917};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00109,
KW   ECO:0000313|EMBL:ADU34327.1}.
FT   DOMAIN       37     91       HTH cro/C1-type. {ECO:0000259|PROSITE:
FT                                PS50943}.
FT   NP_BIND     148    153       ATP. {ECO:0000256|HAMAP-Rule:MF_00109}.
FT   METAL       152    152       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00109}.
FT   BINDING     194    194       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00109}.
FT   BINDING     217    217       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00109}.
FT   BINDING     256    256       ATP. {ECO:0000256|HAMAP-Rule:MF_00109}.
FT   BINDING     275    275       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00109}.
SQ   SEQUENCE   312 AA;  33564 MW;  512BA0BDB11F8129 CRC64;
     MNEHVDAVLA TAPESGTNAA PAGEAKNPLL AALGDRVRNL RAQRGLTRKA VAVAADVSER
     HLANLEYGIG NASILVLQQV AGALHCSLAE LVGDITTSSP EWLLIRELLE NRSEADLRRV
     RVALGELLGT ASVDSARHRR IALVGLRGAG KSTLGQMLAD DLDVPFVELS REIEKLAGCS
     VREIHDLYGT NAYRRYERRA LEEAIQIYGE VVIATPGGIV SDPATFNELL AHCTTVWLQA
     APEEHMGRVA AQGDMRPMAA SKEAMDDLRR ILDGRAAFYS KADLRVDTGG KTVQQAFEAL
     RTAVGTVVRE AA
//

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