AROKB_THEMA
ID AROKB_THEMA Reviewed; 492 AA.
AC Q9WYI3;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Bifunctional shikimate kinase/3-dehydroquinate synthase;
DE Includes:
DE RecName: Full=Shikimate kinase;
DE Short=SK;
DE EC=2.7.1.71;
DE Includes:
DE RecName: Full=3-dehydroquinate synthase;
DE EC=4.2.3.4;
GN Name=aroKB; OrderedLocusNames=TM_0348;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
CC -!- FUNCTION: Catalyzes the specific phosphorylation of the 3-hydroxyl
CC group of shikimic acid using ATP as a cosubstrate. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-
CC dehydroquinate + phosphate; Xref=Rhea:RHEA:21968, ChEBI:CHEBI:32364,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58394; EC=4.2.3.4;
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;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540; Evidence={ECO:0000250};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000250};
CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC 2/7.
CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC 5/7.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the shikimate kinase
CC family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the sugar phosphate
CC cyclases superfamily. Dehydroquinate synthase family. {ECO:0000305}.
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DR EMBL; AE000512; AAD35434.1; -; Genomic_DNA.
DR PIR; B72389; B72389.
DR RefSeq; NP_228159.1; NC_000853.1.
DR RefSeq; WP_004083135.1; NZ_CP011107.1.
DR AlphaFoldDB; Q9WYI3; -.
DR SMR; Q9WYI3; -.
DR STRING; 243274.THEMA_02975; -.
DR EnsemblBacteria; AAD35434; AAD35434; TM_0348.
DR KEGG; tma:TM0348; -.
DR eggNOG; COG0337; Bacteria.
DR eggNOG; COG0703; Bacteria.
DR InParanoid; Q9WYI3; -.
DR OMA; VSIWLRC; -.
DR OrthoDB; 1677032at2; -.
DR UniPathway; UPA00053; UER00085.
DR UniPathway; UPA00053; UER00088.
DR Proteomes; UP000008183; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003856; F:3-dehydroquinate synthase activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004765; F:shikimate kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IBA:GO_Central.
DR GO; GO:0008652; P:cellular amino acid 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; -; 1.
DR HAMAP; MF_00109; Shikimate_kinase; 1.
DR InterPro; IPR016037; DHQ_synth_AroB.
DR InterPro; IPR030960; DHQS/DOIS.
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 Pfam; PF01761; DHQ_synthase; 1.
DR Pfam; PF01202; SKI; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01357; aroB; 1.
DR PROSITE; PS01128; SHIKIMATE_KINASE; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; ATP-binding;
KW Cytoplasm; Kinase; Lyase; Magnesium; Metal-binding; Multifunctional enzyme;
KW NAD; Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..492
FT /note="Bifunctional shikimate kinase/3-dehydroquinate
FT synthase"
FT /id="PRO_0000192432"
FT REGION 1..161
FT /note="Shikimate kinase"
FT REGION 162..492
FT /note="3-dehydroquinate synthase"
FT BINDING 10..15
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 14
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 32
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 56
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 78
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 114
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 131
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 492 AA; 56385 MW; F04C7058237C1C1A CRC64;
MRIFLVGMMG SGKSTIGKRI SEVLDLQFID MDEEIERREG RSVRRIFEED GEEYFRLKEK
ELLKELVERD NVVVATGGGV VVDPENRELL KKEKTLFLYA PPEVLMERVT TENRPLLSEG
KERIREIWEK RKQFYAEFRR IDTSRLNEWE TTALVVLEAL DEKEISTIEK PHLVKIILGG
FKRVRNEELV FTTERVEKIY GRYLPENRLL FPDGEEVKTL EHVSRAYYEL IRMDFPRGKT
IAGVGGGALT DFTGFVASTF KRGVGLSFYP TTLLAQVDAS VGGKNAIDFA GVKNVVGTFR
MPDYVIIDPT VTLSMDEGRF EEGVVEAFKM TILSGRGVEL FDEPEKIEKR NLRVLSEMVK
ISVEEKARIV MEDPYDMGLR HALNLGHTLG HVYEMLEGVP HGIAVAWGIE KETMYLYRKG
IVPKETMRWI VEKVKQIVPI PVPSVDVEKA RNLILNDKKI LKGSRVRLPY VKEIGKIEFL
EVDPLELLEV VD
