AROB_STAAR
ID AROB_STAAR Reviewed; 354 AA.
AC Q6GGU4;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=3-dehydroquinate synthase {ECO:0000255|HAMAP-Rule:MF_00110, ECO:0000303|PubMed:15465043};
DE Short=DHQS {ECO:0000255|HAMAP-Rule:MF_00110, ECO:0000303|PubMed:15465043};
DE EC=4.2.3.4 {ECO:0000255|HAMAP-Rule:MF_00110};
GN Name=aroB {ECO:0000255|HAMAP-Rule:MF_00110}; OrderedLocusNames=SAR1476;
OS Staphylococcus aureus (strain MRSA252).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=282458;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MRSA252;
RX PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT for the rapid evolution of virulence and drug resistance.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
RN [2] {ECO:0007744|PDB:1XAG, ECO:0007744|PDB:1XAH, ECO:0007744|PDB:1XAI, ECO:0007744|PDB:1XAJ, ECO:0007744|PDB:1XAL}
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEXES WITH NAD AND ZINC.
RX PubMed=15465043; DOI=10.1016/j.jmb.2004.08.039;
RA Nichols C.E., Ren J., Leslie K., Dhaliwal B., Lockyer M., Charles I.,
RA Hawkins A.R., Stammers D.K.;
RT "Comparison of ligand-induced conformational changes and domain closure
RT mechanisms, between prokaryotic and eukaryotic dehydroquinate synthases.";
RL J. Mol. Biol. 343:533-546(2004).
CC -!- FUNCTION: Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate
CC 7-phosphate (DAHP) to dehydroquinate (DHQ). {ECO:0000255|HAMAP-
CC Rule:MF_00110}.
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 Evidence={ECO:0000255|HAMAP-Rule:MF_00110};
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00110};
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00110};
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00110};
CC Note=Binds 1 divalent metal cation per subunit. Can use either Co(2+)
CC or Zn(2+). {ECO:0000255|HAMAP-Rule:MF_00110};
CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC 2/7. {ECO:0000255|HAMAP-Rule:MF_00110}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00110}.
CC -!- SIMILARITY: Belongs to the sugar phosphate cyclases superfamily.
CC Dehydroquinate synthase family. {ECO:0000255|HAMAP-Rule:MF_00110}.
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DR EMBL; BX571856; CAG40474.1; -; Genomic_DNA.
DR RefSeq; WP_000776318.1; NC_002952.2.
DR PDB; 1XAG; X-ray; 2.45 A; A=1-354.
DR PDB; 1XAH; X-ray; 2.20 A; A/B=1-354.
DR PDB; 1XAI; X-ray; 2.30 A; A/B=1-354.
DR PDB; 1XAJ; X-ray; 2.35 A; A/B=1-354.
DR PDB; 1XAL; X-ray; 2.80 A; A/B=1-354.
DR PDBsum; 1XAG; -.
DR PDBsum; 1XAH; -.
DR PDBsum; 1XAI; -.
DR PDBsum; 1XAJ; -.
DR PDBsum; 1XAL; -.
DR AlphaFoldDB; Q6GGU4; -.
DR PCDDB; Q6GGU4; -.
DR SMR; Q6GGU4; -.
DR DrugBank; DB02592; Carbaphosphonate.
DR KEGG; sar:SAR1476; -.
DR HOGENOM; CLU_001201_0_1_9; -.
DR OMA; IKMAVCF; -.
DR OrthoDB; 1677032at2; -.
DR BRENDA; 4.2.3.4; 3352.
DR UniPathway; UPA00053; UER00085.
DR EvolutionaryTrace; Q6GGU4; -.
DR Proteomes; UP000000596; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
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 HAMAP; MF_00110; DHQ_synthase; 1.
DR InterPro; IPR016037; DHQ_synth_AroB.
DR InterPro; IPR030963; DHQ_synth_fam.
DR InterPro; IPR030960; DHQS/DOIS.
DR Pfam; PF01761; DHQ_synthase; 1.
DR PIRSF; PIRSF001455; DHQ_synth; 1.
DR TIGRFAMs; TIGR01357; aroB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW Cobalt; Cytoplasm; Lyase; Metal-binding; NAD; Nucleotide-binding; Zinc.
FT CHAIN 1..354
FT /note="3-dehydroquinate synthase"
FT /id="PRO_0000140782"
FT BINDING 39
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:15465043,
FT ECO:0007744|PDB:1XAH, ECO:0007744|PDB:1XAJ,
FT ECO:0007744|PDB:1XAL"
FT BINDING 45
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:15465043,
FT ECO:0007744|PDB:1XAH, ECO:0007744|PDB:1XAL"
FT BINDING 68..71
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:15465043,
FT ECO:0007744|PDB:1XAH, ECO:0007744|PDB:1XAJ,
FT ECO:0007744|PDB:1XAL"
FT BINDING 100..104
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00110,
FT ECO:0000269|PubMed:15465043, ECO:0007744|PDB:1XAH,
FT ECO:0007744|PDB:1XAJ, ECO:0007744|PDB:1XAL"
FT BINDING 124..125
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00110,
FT ECO:0000269|PubMed:15465043, ECO:0007744|PDB:1XAH,
FT ECO:0007744|PDB:1XAJ, ECO:0007744|PDB:1XAL"
FT BINDING 136
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00110,
FT ECO:0000269|PubMed:15465043, ECO:0007744|PDB:1XAH,
FT ECO:0007744|PDB:1XAJ, ECO:0007744|PDB:1XAL"
FT BINDING 145
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00110,
FT ECO:0000269|PubMed:15465043, ECO:0007744|PDB:1XAH,
FT ECO:0007744|PDB:1XAJ, ECO:0007744|PDB:1XAL"
FT BINDING 163..166
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00110,
FT ECO:0000269|PubMed:15465043, ECO:0007744|PDB:1XAH,
FT ECO:0007744|PDB:1XAJ, ECO:0007744|PDB:1XAL"
FT BINDING 178
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00110,
FT ECO:0000269|PubMed:15465043, ECO:0007744|PDB:1XAI"
FT BINDING 242
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00110,
FT ECO:0000269|PubMed:15465043, ECO:0007744|PDB:1XAI"
FT BINDING 256
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00110,
FT ECO:0000269|PubMed:15465043, ECO:0007744|PDB:1XAI"
FT STRAND 2..4
FT /evidence="ECO:0007829|PDB:1XAH"
FT STRAND 8..10
FT /evidence="ECO:0007829|PDB:1XAI"
FT STRAND 13..17
FT /evidence="ECO:0007829|PDB:1XAH"
FT HELIX 20..22
FT /evidence="ECO:0007829|PDB:1XAH"
FT HELIX 23..28
FT /evidence="ECO:0007829|PDB:1XAH"
FT STRAND 34..39
FT /evidence="ECO:0007829|PDB:1XAH"
FT HELIX 40..50
FT /evidence="ECO:0007829|PDB:1XAH"
FT TURN 52..55
FT /evidence="ECO:0007829|PDB:1XAG"
FT STRAND 59..64
FT /evidence="ECO:0007829|PDB:1XAH"
FT HELIX 67..70
FT /evidence="ECO:0007829|PDB:1XAH"
FT HELIX 73..84
FT /evidence="ECO:0007829|PDB:1XAH"
FT TURN 85..87
FT /evidence="ECO:0007829|PDB:1XAJ"
FT STRAND 93..99
FT /evidence="ECO:0007829|PDB:1XAH"
FT HELIX 100..112
FT /evidence="ECO:0007829|PDB:1XAH"
FT HELIX 113..115
FT /evidence="ECO:0007829|PDB:1XAG"
FT STRAND 118..123
FT /evidence="ECO:0007829|PDB:1XAH"
FT HELIX 128..131
FT /evidence="ECO:0007829|PDB:1XAH"
FT STRAND 136..139
FT /evidence="ECO:0007829|PDB:1XAH"
FT STRAND 142..144
FT /evidence="ECO:0007829|PDB:1XAH"
FT STRAND 148..151
FT /evidence="ECO:0007829|PDB:1XAH"
FT STRAND 155..160
FT /evidence="ECO:0007829|PDB:1XAH"
FT HELIX 161..166
FT /evidence="ECO:0007829|PDB:1XAH"
FT HELIX 169..186
FT /evidence="ECO:0007829|PDB:1XAH"
FT HELIX 188..197
FT /evidence="ECO:0007829|PDB:1XAH"
FT HELIX 201..206
FT /evidence="ECO:0007829|PDB:1XAH"
FT TURN 207..209
FT /evidence="ECO:0007829|PDB:1XAH"
FT HELIX 210..227
FT /evidence="ECO:0007829|PDB:1XAH"
FT TURN 228..230
FT /evidence="ECO:0007829|PDB:1XAI"
FT STRAND 231..233
FT /evidence="ECO:0007829|PDB:1XAH"
FT HELIX 234..239
FT /evidence="ECO:0007829|PDB:1XAH"
FT TURN 240..242
FT /evidence="ECO:0007829|PDB:1XAH"
FT HELIX 243..252
FT /evidence="ECO:0007829|PDB:1XAH"
FT HELIX 256..274
FT /evidence="ECO:0007829|PDB:1XAH"
FT HELIX 281..291
FT /evidence="ECO:0007829|PDB:1XAH"
FT HELIX 297..300
FT /evidence="ECO:0007829|PDB:1XAI"
FT HELIX 306..308
FT /evidence="ECO:0007829|PDB:1XAH"
FT TURN 310..312
FT /evidence="ECO:0007829|PDB:1XAI"
FT STRAND 324..328
FT /evidence="ECO:0007829|PDB:1XAH"
FT STRAND 331..334
FT /evidence="ECO:0007829|PDB:1XAH"
FT HELIX 339..351
FT /evidence="ECO:0007829|PDB:1XAH"
SQ SEQUENCE 354 AA; 40285 MW; 3B960112993F6F3F CRC64;
MKLQTTYPSN NYPIFVEHGA IDHISTYIDQ FDQSFILIDE HVNQYFADKF NDILSYENVH
KVIIPAGEKT KTFEQYQETL EYILSHHVTR NTAIIAVGGG ATGDFAGFVA ATLLRGVHFI
QVPTTILAHD SSVGGKVGIN SKQGKNLIGA FYRPTAVIYD LDFLKTLPFE QILSGYAEVY
KHALLNGESA TQDIEQHFKD REILQSLKGM DKYIAKGIET KLDIVVADEK EQGVRKFLNL
GHTFGHAVEY YHKIPHGHAV MVGIIYQFIV ANALFDSKHD INHYIQYLIQ LGYPLDMITD
LDFETLYQYM LSDKKNDKQG VQMVLIRQFG DIVVQHVDQL TLQHACEQLK TYFK
