AROB_FRATT
ID AROB_FRATT Reviewed; 359 AA.
AC Q5NFS1;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=3-dehydroquinate synthase {ECO:0000255|HAMAP-Rule:MF_00110};
DE Short=DHQS {ECO:0000255|HAMAP-Rule:MF_00110};
DE EC=4.2.3.4 {ECO:0000255|HAMAP-Rule:MF_00110};
GN Name=aroB {ECO:0000255|HAMAP-Rule:MF_00110}; OrderedLocusNames=FTT_1154c;
OS Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC Francisellaceae; Francisella.
OX NCBI_TaxID=177416;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCHU S4 / Schu 4;
RX PubMed=15640799; DOI=10.1038/ng1499;
RA Larsson P., Oyston P.C.F., Chain P., Chu M.C., Duffield M., Fuxelius H.-H.,
RA Garcia E., Haelltorp G., Johansson D., Isherwood K.E., Karp P.D.,
RA Larsson E., Liu Y., Michell S., Prior J., Prior R., Malfatti S.,
RA Sjoestedt A., Svensson K., Thompson N., Vergez L., Wagg J.K., Wren B.W.,
RA Lindler L.E., Andersson S.G.E., Forsman M., Titball R.W.;
RT "The complete genome sequence of Francisella tularensis, the causative
RT agent of tularemia.";
RL Nat. Genet. 37:153-159(2005).
RN [2] {ECO:0007744|PDB:5HVN}
RP X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) IN COMPLEX WITH NAD.
RA Minasov G., Light S.H., Shuvalova L., Dubrovska I., Winsor J., Zhou M.,
RA Grimshaw S., Kwon K., Joachimiak A., Anderson W.F.;
RT "3.0 angstrom crystal structure of 3-dehydroquinate synthase (AroB) from
RT Francisella tularensis in complex with NAD.";
RL Submitted (JAN-2016) to the PDB data bank.
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=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 -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Evidence={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; AJ749949; CAG45787.1; -; Genomic_DNA.
DR RefSeq; WP_003021364.1; NZ_CP010290.1.
DR RefSeq; YP_170121.1; NC_006570.2.
DR PDB; 5HVN; X-ray; 3.00 A; A=1-359.
DR PDBsum; 5HVN; -.
DR AlphaFoldDB; Q5NFS1; -.
DR SMR; Q5NFS1; -.
DR STRING; 177416.FTT_1154c; -.
DR DNASU; 3190946; -.
DR EnsemblBacteria; CAG45787; CAG45787; FTT_1154c.
DR KEGG; ftu:FTT_1154c; -.
DR eggNOG; COG0337; Bacteria.
DR OMA; IKMAVCF; -.
DR UniPathway; UPA00053; UER00085.
DR Proteomes; UP000001174; 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;
KW Reference proteome; Zinc.
FT CHAIN 1..359
FT /note="3-dehydroquinate synthase"
FT /id="PRO_0000231087"
FT BINDING 42
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|Ref.2, ECO:0007744|PDB:5HVN"
FT BINDING 70..75
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00110,
FT ECO:0000269|Ref.2, ECO:0007744|PDB:5HVN"
FT BINDING 105..109
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00110,
FT ECO:0000269|Ref.2, ECO:0007744|PDB:5HVN"
FT BINDING 129..130
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00110,
FT ECO:0000269|Ref.2, ECO:0007744|PDB:5HVN"
FT BINDING 142
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00110,
FT ECO:0000269|Ref.2, ECO:0007744|PDB:5HVN"
FT BINDING 151
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00110"
FT BINDING 169..172
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00110,
FT ECO:0000269|Ref.2, ECO:0007744|PDB:5HVN"
FT BINDING 184
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00110"
FT BINDING 247
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00110"
FT BINDING 264
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00110"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:5HVN"
FT STRAND 15..22
FT /evidence="ECO:0007829|PDB:5HVN"
FT HELIX 25..31
FT /evidence="ECO:0007829|PDB:5HVN"
FT TURN 32..34
FT /evidence="ECO:0007829|PDB:5HVN"
FT STRAND 35..42
FT /evidence="ECO:0007829|PDB:5HVN"
FT HELIX 43..57
FT /evidence="ECO:0007829|PDB:5HVN"
FT STRAND 63..68
FT /evidence="ECO:0007829|PDB:5HVN"
FT HELIX 72..74
FT /evidence="ECO:0007829|PDB:5HVN"
FT HELIX 77..89
FT /evidence="ECO:0007829|PDB:5HVN"
FT STRAND 97..104
FT /evidence="ECO:0007829|PDB:5HVN"
FT HELIX 105..117
FT /evidence="ECO:0007829|PDB:5HVN"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:5HVN"
FT STRAND 123..128
FT /evidence="ECO:0007829|PDB:5HVN"
FT HELIX 131..136
FT /evidence="ECO:0007829|PDB:5HVN"
FT STRAND 142..147
FT /evidence="ECO:0007829|PDB:5HVN"
FT STRAND 150..157
FT /evidence="ECO:0007829|PDB:5HVN"
FT STRAND 161..166
FT /evidence="ECO:0007829|PDB:5HVN"
FT HELIX 167..171
FT /evidence="ECO:0007829|PDB:5HVN"
FT HELIX 175..191
FT /evidence="ECO:0007829|PDB:5HVN"
FT HELIX 193..207
FT /evidence="ECO:0007829|PDB:5HVN"
FT HELIX 211..229
FT /evidence="ECO:0007829|PDB:5HVN"
FT HELIX 239..244
FT /evidence="ECO:0007829|PDB:5HVN"
FT HELIX 247..257
FT /evidence="ECO:0007829|PDB:5HVN"
FT STRAND 260..262
FT /evidence="ECO:0007829|PDB:5HVN"
FT HELIX 264..281
FT /evidence="ECO:0007829|PDB:5HVN"
FT HELIX 287..299
FT /evidence="ECO:0007829|PDB:5HVN"
FT HELIX 312..320
FT /evidence="ECO:0007829|PDB:5HVN"
FT STRAND 331..337
FT /evidence="ECO:0007829|PDB:5HVN"
FT STRAND 340..345
FT /evidence="ECO:0007829|PDB:5HVN"
FT HELIX 348..358
FT /evidence="ECO:0007829|PDB:5HVN"
SQ SEQUENCE 359 AA; 40156 MW; 8E442D40939BFC3E CRC64;
MISKLSVNPT FSPSYNIIVD SVLDFSHILE YVTNKQVLVV TNTTVAKLYL TKFLAALVDD
LDVRTCILED GEQYKSQQSL DKILSTLLEN HFTRNSTVLV ALGGGVIGDI TGFAAAIYQR
GIDFIQIPTT LLSQVDSSVG GKTAINHQLG KNMIGAFYQP KVVYTSIEFY KTLPQREYIA
GMAEVVKYAF ISKDFYLWLD SNRDKILAKD SVTLIEMVKR SCQIKAQVVA MDEKELTGAR
AILNFGHTFG HAIEKCQNYR GLKHGEAVGV GMAQAIDFSH YLGLISQQQA KDFNDFIVSF
GISIDFPNDI CQKEFLEAML LDKKNSNKEL KFILIENIGS LSLQKQSKNE LEQFLDISR
