ID   AROKB_BIFLO             Reviewed;         540 AA.
AC   Q8G5X4;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 114.
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=aroB; Synonyms=aroK/B; OrderedLocusNames=BL0877;
OS   Bifidobacterium longum (strain NCC 2705).
OC   Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC   Bifidobacterium.
OX   NCBI_TaxID=206672;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCC 2705;
RX   PubMed=12381787; DOI=10.1073/pnas.212527599;
RA   Schell M.A., Karmirantzou M., Snel B., Vilanova D., Berger B., Pessi G.,
RA   Zwahlen M.-C., Desiere F., Bork P., Delley M., Pridmore R.D., Arigoni F.;
RT   "The genome sequence of Bifidobacterium longum reflects its adaptation to
RT   the human gastrointestinal tract.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14422-14427(2002).
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=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   -!- SUBUNIT: Monomer. {ECO:0000250}.
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; AE014295; AAN24690.1; -; Genomic_DNA.
DR   RefSeq; NP_696054.1; NC_004307.2.
DR   RefSeq; WP_007052140.1; NC_004307.2.
DR   AlphaFoldDB; Q8G5X4; -.
DR   SMR; Q8G5X4; -.
DR   STRING; 206672.BL0877; -.
DR   EnsemblBacteria; AAN24690; AAN24690; BL0877.
DR   GeneID; 66505003; -.
DR   KEGG; blo:BL0877; -.
DR   PATRIC; fig|206672.9.peg.572; -.
DR   HOGENOM; CLU_001201_5_2_11; -.
DR   OMA; VSIWLRC; -.
DR   PhylomeDB; Q8G5X4; -.
DR   UniPathway; UPA00053; UER00085.
DR   UniPathway; UPA00053; UER00088.
DR   Proteomes; UP000000439; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003856; F:3-dehydroquinate synthase activity; IEA:UniProtKB-UniRule.
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; IEA:UniProtKB-UniRule.
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_00110; DHQ_synthase; 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   Pfam; PF01761; DHQ_synthase; 1.
DR   Pfam; PF01202; SKI; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR01357; aroB; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis; ATP-binding;
KW   Cytoplasm; Kinase; Lyase; Multifunctional enzyme; NAD; Nucleotide-binding;
KW   Reference proteome; Transferase.
FT   CHAIN           1..540
FT                   /note="Bifunctional shikimate kinase/3-dehydroquinate
FT                   synthase"
FT                   /id="PRO_0000192431"
FT   REGION          1..166
FT                   /note="Shikimate kinase"
FT   REGION          167..540
FT                   /note="3-dehydroquinate synthase"
FT   BINDING         11..18
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   540 AA;  58712 MW;  4619CB23F87C5B5A CRC64;
     MTARPRAVII GMMGAGKTRV GKEVAHMLRL PFADADVEIE REVGMKIPSY FEEYGEPAFR
     EVEADLIADM LEDFDGIFSL GGGAPMTPST QHALASYIDH GGRVVYLDAD PAEAMERANR
     GGGRPMLNGN ANSRWKKLFK QRDPVFREVA NVHVHTRGLT PQGAAKKVID MVSERAVHVT
     GAAIEPYDVV IGEGAMNHLV DVLGPKPAKI ALIHTQPVQR HSDRARALLR QGGYEVSDIV
     IPDAEPGKTI TVANGIWERL GNEGFTRSDA VVGLGGGAAT DLAGFVAATW MRGVRYVNCP
     TSLLAMVDAS TGGKTGINTP QGKNLVGSFY TPAGVLADTK TLATLPNDIF IEGLGEVAKS
     GFIRDPEILH ILEDHAAELR AFDGSTFLGS PLEDVVAELI ERTVKVKAYH VSSDLKEKGL
     REFLNYGHTM GHAIEKLEHF RWRHGNAVAV GMVYAAELAH LIGYIDQDLV DYHRSLLASM
     GLPTSWNGGS FDDVLALMHR DKKARGNELR FVVLDEIGHV VHLDNPPAEA VEEAFRRIQQ