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Database: UniProt
Entry: A0A1M6PI84_9FIRM
LinkDB: A0A1M6PI84_9FIRM
Original site: A0A1M6PI84_9FIRM 
ID   A0A1M6PI84_9FIRM        Unreviewed;       362 AA.
AC   A0A1M6PI84;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=3-dehydroquinate synthase {ECO:0000256|ARBA:ARBA00017684, ECO:0000256|HAMAP-Rule:MF_00110};
DE            Short=DHQS {ECO:0000256|HAMAP-Rule:MF_00110};
DE            EC=4.2.3.4 {ECO:0000256|ARBA:ARBA00013031, ECO:0000256|HAMAP-Rule:MF_00110};
GN   Name=aroB {ECO:0000256|HAMAP-Rule:MF_00110};
GN   ORFNames=SAMN02745123_00600 {ECO:0000313|EMBL:SHK07642.1};
OS   Desulforamulus aeronauticus DSM 10349.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae;
OC   Desulforamulus.
OX   NCBI_TaxID=1121421 {ECO:0000313|EMBL:SHK07642.1, ECO:0000313|Proteomes:UP000183997};
RN   [1] {ECO:0000313|EMBL:SHK07642.1, ECO:0000313|Proteomes:UP000183997}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10349 {ECO:0000313|EMBL:SHK07642.1,
RC   ECO:0000313|Proteomes:UP000183997};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate
CC       7-phosphate (DAHP) to dehydroquinate (DHQ).
CC       {ECO:0000256|ARBA:ARBA00003485, ECO:0000256|HAMAP-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|ARBA:ARBA00001393, ECO:0000256|HAMAP-
CC         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|ARBA:ARBA00004661, ECO:0000256|HAMAP-Rule:MF_00110}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|HAMAP-Rule:MF_00110}.
CC   -!- SIMILARITY: Belongs to the sugar phosphate cyclases superfamily.
CC       Dehydroquinate synthase family. {ECO:0000256|ARBA:ARBA00005412,
CC       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; FRAR01000006; SHK07642.1; -; Genomic_DNA.
DR   RefSeq; WP_072910794.1; NZ_FRAR01000006.1.
DR   AlphaFoldDB; A0A1M6PI84; -.
DR   STRING; 1121421.SAMN02745123_00600; -.
DR   OrthoDB; 9806583at2; -.
DR   UniPathway; UPA00053; UER00085.
DR   Proteomes; UP000183997; 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:SF7; 3-DEHYDROQUINATE SYNTHASE, CHLOROPLASTIC; 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|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW   Rule:MF_00110};
KW   Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141,
KW   ECO:0000256|HAMAP-Rule:MF_00110};
KW   Cobalt {ECO:0000256|ARBA:ARBA00023285, ECO:0000256|HAMAP-Rule:MF_00110};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, 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};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00110}.
FT   DOMAIN          68..326
FT                   /note="3-dehydroquinate synthase"
FT                   /evidence="ECO:0000259|Pfam:PF01761"
FT   BINDING         106..110
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00110"
FT   BINDING         130..131
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00110"
FT   BINDING         143
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00110"
FT   BINDING         152
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00110"
FT   BINDING         170..173
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00110"
FT   BINDING         185
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00110"
FT   BINDING         248
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00110"
FT   BINDING         265
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00110"
SQ   SEQUENCE   362 AA;  39095 MW;  EF13C81FFF67C2E6 CRC64;
     MRTVRVELAS RSYPIYIGTG LLQQLGEQLA ALSLGKKILL VTDTQVGLLY GNKVKDLLSG
     VGFSVTMVQI PAGEPSKTLE QAAKLYDAAF AFGLDRTCAV LALGGGVVGD LAGFVAATYM
     RGIPFIQVPT TLLAQVDSSV GGKVAVNHPR GKNIIGAFYQ PKLVLIDVST LHTLSAKELR
     AGLAEVIKYG VIWDAEFFSW LEENSINLLK LEPEALEYAI ETCCKIKAAV VEQDETEQGS
     RAILNYGHTV GHALESLTNY ERYLHGEAVA VGMVAAARLA LQQGLLSKHD YQRIHSLLDR
     VDLPTAIPAD LKPESITRLM FYDKKVNNGK LTLILPLGIG KAKISLDFPE NQLSGLFTNG
     VS
//
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