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Entry: A0A348B107_9CREN
LinkDB: A0A348B107_9CREN
Original site: A0A348B107_9CREN 
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
//
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