ID D4GU24_HALVD Unreviewed; 392 AA.
AC D4GU24; L9UN52;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 10-JUN-2026, entry version 83.
DE RecName: Full=3-dehydroquinate synthase {ECO:0000256|HAMAP-Rule:MF_01244};
DE Short=DHQ synthase {ECO:0000256|HAMAP-Rule:MF_01244};
DE EC=1.4.1.24 {ECO:0000256|HAMAP-Rule:MF_01244};
DE AltName: Full=3-dehydroquinate synthase II {ECO:0000256|HAMAP-Rule:MF_01244};
GN Name=aroB {ECO:0000313|EMBL:ADE03173.1};
GN Synonyms=aroB' {ECO:0000256|HAMAP-Rule:MF_01244};
GN OrderedLocusNames=HVO_0792 {ECO:0000313|EMBL:ADE03173.1};
OS Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 /
OS NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii).
OC Archaea; Methanobacteriati; Methanobacteriota; Stenosarchaea group;
OC Halobacteria; Halobacteriales; Haloferacaceae; Haloferax.
OX NCBI_TaxID=309800 {ECO:0000313|EMBL:ADE03173.1, ECO:0000313|Proteomes:UP000008243};
RN [1] {ECO:0000313|EMBL:ADE03173.1, ECO:0000313|Proteomes:UP000008243}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 /
RC VKM B-1768 / DS2 {ECO:0000313|Proteomes:UP000008243};
RX PubMed=20333302; DOI=10.1371/journal.pone.0009605;
RA Hartman A.L., Norais C., Badger J.H., Delmas S., Haldenby S., Madupu R.,
RA Robinson J., Khouri H., Ren Q., Lowe T.M., Maupin-Furlow J.,
RA Pohlschroder M., Daniels C., Pfeiffer F., Allers T., Eisen J.A.;
RT "The complete genome sequence of Haloferax volcanii DS2, a model
RT archaeon.";
RL PLoS ONE 5:E9605-E9605(2010).
CC -!- FUNCTION: Catalyzes the oxidative deamination and cyclization of 2-
CC amino-3,7-dideoxy-D-threo-hept-6-ulosonic acid (ADH) to yield 3-
CC dehydroquinate (DHQ), which is fed into the canonical shikimic pathway
CC of aromatic amino acid biosynthesis. {ECO:0000256|HAMAP-Rule:MF_01244}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-amino-2,3,7-trideoxy-D-lyxo-hept-6-ulosonate + NAD(+) + H2O
CC = 3-dehydroquinate + NH4(+) + NADH + H(+); Xref=Rhea:RHEA:25956,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:32364, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:58859; EC=1.4.1.24; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_01244};
CC -!- SIMILARITY: Belongs to the archaeal-type DHQ synthase family.
CC {ECO:0000256|HAMAP-Rule:MF_01244}.
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DR EMBL; CP001956; ADE03173.1; -; Genomic_DNA.
DR RefSeq; WP_004044144.1; NC_013967.1.
DR AlphaFoldDB; D4GU24; -.
DR STRING; 309800.HVO_0792; -.
DR PaxDb; 309800-HVO_0792; -.
DR EnsemblBacteria; ADE03173; ADE03173; HVO_0792.
DR GeneID; 8925180; -.
DR KEGG; hvo:HVO_0792; -.
DR PATRIC; fig|309800.29.peg.2848; -.
DR eggNOG; arCOG04353; Archaea.
DR HOGENOM; CLU_056379_0_0_2; -.
DR OrthoDB; 10265at2157; -.
DR Proteomes; UP000008243; Chromosome.
DR GO; GO:0003856; F:3-dehydroquinate synthase activity; IEA:InterPro.
DR GO; GO:0102042; F:dehydroquinate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0051287; F:NAD binding; IEA:UniProtKB-UniRule.
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 HAMAP; MF_01244; Arch_DHQ_synthase; 1.
DR InterPro; IPR002812; DHQS.
DR InterPro; IPR030960; DHQS/DOIS_N.
DR InterPro; IPR056179; DHQS_C.
DR NCBIfam; NF002623; PRK02290.1-1; 1.
DR PANTHER; PTHR33563; -; 1.
DR PANTHER; PTHR33563:SF1; 3-DEHYDROQUINATE SYNTHASE; 1.
DR Pfam; PF01959; DHQS; 1.
DR Pfam; PF26558; DHQS_2nd; 1.
DR PIRSF; PIRSF006655; DHQ_synth; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW Rule:MF_01244};
KW Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141,
KW ECO:0000256|HAMAP-Rule:MF_01244};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_01244};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_01244}; Reference proteome {ECO:0000313|Proteomes:UP000008243}.
FT DOMAIN 3..205
FT /note="3-dehydroquinate synthase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01959"
FT DOMAIN 219..392
FT /note="3-dehydroquinate synthase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF26558"
SQ SEQUENCE 392 AA; 43109 MW; C693E3C7873C9256 CRC64;
MTRSVWLKAD DAVGDWETRK RRITAGLEAG VDWVLVDEAD VERMRELGDV NIAAFRTDAD
VHVMEAEEDD GEPAALADAY IVGKDGEGDA TVELPSDFSG SADLTTLRRG DDLANGSYVR
ILSKDYEAFA EEAARDGDYT IVIGEDWTII PLENLIARIG EETDLIAGVT TAEEAKTAFE
TLELGSDGVL LDSDDPDEIR KTVEVRDEAE RESLDLVWAE VTEVERTGMA DRVCVDTGTI
MDHDEGMLVG SMARGLFFVH AETAKSPYVA SRPFRVNAGA VHAYARTPDG GTVYLSELES
GDEVQLIDTN GSTREAIVGR VKIEKRPMFR ISADYEGDRV TTLLQNAETI KVHTREGRTA
VTDLEPGDEM LIYYEDTARH FGEAVEESII EK
//
