DHQS_METM6
ID DHQS_METM6 Reviewed; 361 AA.
AC A9A8T5;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 25-MAY-2022, entry version 68.
DE RecName: Full=3-dehydroquinate synthase {ECO:0000255|HAMAP-Rule:MF_01244};
DE Short=DHQ synthase {ECO:0000255|HAMAP-Rule:MF_01244};
DE EC=1.4.1.24 {ECO:0000255|HAMAP-Rule:MF_01244};
DE AltName: Full=3-dehydroquinate synthase II {ECO:0000255|HAMAP-Rule:MF_01244};
GN Name=aroB' {ECO:0000255|HAMAP-Rule:MF_01244};
GN OrderedLocusNames=MmarC6_0943;
OS Methanococcus maripaludis (strain C6 / ATCC BAA-1332).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanococcaceae; Methanococcus.
OX NCBI_TaxID=444158;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C6 / ATCC BAA-1332;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Clum A., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Mikhailova N., Sieprawska-Lupa M., Whitman W.B.,
RA Richardson P.;
RT "Complete sequence of Methanococcus maripaludis C6.";
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
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:0000255|HAMAP-Rule:MF_01244}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-amino-2,3,7-trideoxy-D-lyxo-hept-6-ulosonate + H2O + NAD(+)
CC = 3-dehydroquinate + H(+) + NADH + NH4(+); 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:0000255|HAMAP-
CC Rule:MF_01244};
CC -!- SIMILARITY: Belongs to the archaeal-type DHQ synthase family.
CC {ECO:0000255|HAMAP-Rule:MF_01244}.
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DR EMBL; CP000867; ABX01758.1; -; Genomic_DNA.
DR RefSeq; WP_012193709.1; NC_009975.1.
DR AlphaFoldDB; A9A8T5; -.
DR STRING; 444158.MmarC6_0943; -.
DR EnsemblBacteria; ABX01758; ABX01758; MmarC6_0943.
DR GeneID; 5738681; -.
DR KEGG; mmx:MmarC6_0943; -.
DR eggNOG; arCOG04353; Archaea.
DR HOGENOM; CLU_056379_0_0_2; -.
DR OMA; HFGMAIK; -.
DR OrthoDB; 29853at2157; -.
DR PhylomeDB; A9A8T5; -.
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: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 HAMAP; MF_01244; Arch_DHQ_synthase; 1.
DR InterPro; IPR002812; DHQ_synth.
DR PANTHER; PTHR33563; PTHR33563; 1.
DR Pfam; PF01959; DHQS; 1.
DR PIRSF; PIRSF006655; DHQ_synth; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; NAD;
KW Oxidoreductase.
FT CHAIN 1..361
FT /note="3-dehydroquinate synthase"
FT /id="PRO_0000372049"
SQ SEQUENCE 361 AA; 39882 MW; 4BD0CA2D1C1F41FD CRC64;
MKFGWIKTTG TDSEERMDSV KDALESSIPG IIAEKDEISS VRELGNIKIV SDSLDADVVL
INKGEDLEIL KSAKLSGKET AVYVVINTKD DEVYATEVSK LDFVDYIVLE GSDWTIIPLE
NIIADLFGEE IKIVSVVTSV KDAEAAYEIL EKGVDGVVLI PNDINEVKDF SKLIERMNSE
SVKLDYATVT KIEPVGSGDR VCIDTCSMME MGEGMLIGSY SRGMFLVHSE TVENPYVATR
PFRVNAGPVH AYILCPENKT KYLSDLKAGD KVLVVNKNGE TRESIIGRVK IEKRPLFLVE
AEYNGENLRT ILQNAETIRL VGEDGKPVSV VDLKVGTKVL IKPDENARHF GMAIKETIIE
K