ID A0A348B107_9CREN Unreviewed; 346 AA.
AC A0A348B107;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=3-dehydroquinate synthase {ECO:0000256|HAMAP-Rule:MF_00110};
DE Short=DHQS {ECO:0000256|HAMAP-Rule:MF_00110};
DE EC=4.2.3.4 {ECO:0000256|HAMAP-Rule:MF_00110};
GN Name=aroB {ECO:0000256|HAMAP-Rule:MF_00110};
GN ORFNames=GCM10007116_19490 {ECO:0000313|EMBL:GGU02491.1},
GN HS1genome_0248 {ECO:0000313|EMBL:BBD71859.1};
OS Sulfodiicoccus acidiphilus.
OC Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfodiicoccus.
OX NCBI_TaxID=1670455 {ECO:0000313|EMBL:BBD71859.1, ECO:0000313|Proteomes:UP000276741};
RN [1] {ECO:0000313|Proteomes:UP000276741}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HS-1 {ECO:0000313|Proteomes:UP000276741};
RA Sakai H.D., Kurosawa N.;
RT "Complete genome sequence of Sulfodiicoccus acidiphilus strain HS-1.";
RL Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:BBD71859.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HS-1 {ECO:0000313|EMBL:BBD71859.1};
RX PubMed=31331368;
RA Sakai H.D., Kurosawa N.;
RT "Complete genome sequence of the Sulfodiicoccus acidiphilus strain HS-1T,
RT the first crenarchaeon that lacks polB3, isolated from an acidic hot spring
RT in Ohwaku-dani, Hakone, Japan.";
RL BMC Res. Notes 12:444-444(2019).
RN [3] {ECO:0000313|EMBL:GGU02491.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=JCM 31740 {ECO:0000313|EMBL:GGU02491.1};
RX PubMed=30832757;
RA Wu L., Ma J.;
RT "The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing
RT project: providing services to taxonomists for standard genome sequencing
RT and annotation.";
RL Int. J. Syst. Evol. Microbiol. 69:895-898(2019).
RN [4] {ECO:0000313|EMBL:GGU02491.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=JCM 31740 {ECO:0000313|EMBL:GGU02491.1};
RA Sun Q., Ohkuma M.;
RL Submitted (SEP-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate
CC 7-phosphate (DAHP) to dehydroquinate (DHQ). {ECO:0000256|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:0000256|HAMAP-Rule:MF_00110};
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00110};
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00110};
CC Note=Binds 1 divalent metal cation per subunit. Can use either Co(2+)
CC or Zn(2+). {ECO:0000256|HAMAP-Rule:MF_00110};
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Evidence={ECO:0000256|ARBA:ARBA00001911,
CC ECO:0000256|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:0000256|HAMAP-Rule:MF_00110}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00110}.
CC -!- SIMILARITY: Belongs to the sugar phosphate cyclases superfamily.
CC Dehydroquinate synthase family. {ECO:0000256|HAMAP-Rule:MF_00110}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00110}.
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DR EMBL; AP018553; BBD71859.1; -; Genomic_DNA.
DR EMBL; BMQS01000022; GGU02491.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A348B107; -.
DR KEGG; sacd:HS1genome_0248; -.
DR OrthoDB; 21407at2157; -.
DR UniPathway; UPA00053; UER00085.
DR Proteomes; UP000276741; Chromosome.
DR Proteomes; UP000616143; Unassembled WGS sequence.
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:0008652; P:amino acid biosynthetic process; IEA:UniProtKB-KW.
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; cd08195; DHQS; 1.
DR Gene3D; 3.40.50.1970; -; 1.
DR Gene3D; 1.20.1090.10; Dehydroquinate synthase-like - alpha domain; 1.
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 NCBIfam; TIGR01357; aroB; 1.
DR PANTHER; PTHR43622; 3-DEHYDROQUINATE SYNTHASE; 1.
DR PANTHER; PTHR43622:SF1; 3-DEHYDROQUINATE SYNTHASE; 1.
DR Pfam; PF01761; DHQ_synthase; 1.
DR PIRSF; PIRSF001455; DHQ_synth; 1.
DR SUPFAM; SSF56796; Dehydroquinate synthase-like; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00110};
KW Aromatic amino acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00110};
KW Cobalt {ECO:0000256|ARBA:ARBA00023285, ECO:0000256|HAMAP-Rule:MF_00110};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00110};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00110};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00110};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_00110};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00110}; Reference proteome {ECO:0000313|Proteomes:UP000276741};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00110}.
FT DOMAIN 50..311
FT /note="3-dehydroquinate synthase"
FT /evidence="ECO:0000259|Pfam:PF01761"
FT BINDING 54..59
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00110"
FT BINDING 112..113
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00110"
FT BINDING 125
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00110"
FT BINDING 134
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00110"
FT BINDING 152..155
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00110"
FT BINDING 167
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00110"
FT BINDING 231
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00110"
FT BINDING 247
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00110"
SQ SEQUENCE 346 AA; 37471 MW; 37555843000D6795 CRC64;
MRNLEVDVGG RKVVVAIGNG TSSLLGEVSG KKLIVRSKNV KSPLEAEIEV VIEDGEESKT
LDSTLNLVRA MRRAGLGRSD FVVAVGGGSV LDVAGFAASI YLRGIGLINV PTTLLGMVDA
GLGGKNGINF EGLKNVLGTF YQPSMVIDDL SFLTTLPYDD FINGMAEVVK YGVTLDKEFY
DFLSIKVEDV KSRNESVVEE IVYRSVENKM RIVAEDELDI KEVRIVLNFG HTVGHAIEAG
TRFAVPHGKA VAVGMVCEAK IAEELGVAEE GVVEDVLWIL QLYGLPITPA QLGLPVDMEL
VERAIHGDKK IKGEEIVMAV PVRIGSWTKF KVSVETLRGL VRQCLE
//