ID F4C059_METSG Unreviewed; 373 AA.
AC F4C059;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 28-JAN-2026, entry version 61.
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:AEB67950.1};
GN Synonyms=aroB' {ECO:0000256|HAMAP-Rule:MF_01244};
GN OrderedLocusNames=MCON_1239 {ECO:0000313|EMBL:AEB67950.1};
OS Methanothrix soehngenii (strain ATCC 5969 / DSM 3671 / JCM 10134 / NBRC
OS 103675 / OCM 69 / GP-6) (Methanosaeta concilii).
OC Archaea; Methanobacteriati; Methanobacteriota; Stenosarchaea group;
OC Methanomicrobia; Methanotrichales; Methanotrichaceae; Methanothrix.
OX NCBI_TaxID=990316 {ECO:0000313|EMBL:AEB67950.1, ECO:0000313|Proteomes:UP000007807};
RN [1] {ECO:0000313|EMBL:AEB67950.1, ECO:0000313|Proteomes:UP000007807}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 5969 / DSM 3671 / JCM 10134 / NBRC 103675 / OCM 69 / GP-6
RC {ECO:0000313|Proteomes:UP000007807};
RX PubMed=21571998; DOI=10.1128/JB.05031-11;
RA Barber R.D., Zhang L., Harnack M., Olson M.V., Kaul R., Ingram-Smith C.,
RA Smith K.S.;
RT "Complete genome sequence of Methanosaeta concilii, a specialist in
RT aceticlastic methanogenesis.";
RL J. Bacteriol. 193:3668-3669(2011).
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; CP002565; AEB67950.1; -; Genomic_DNA.
DR RefSeq; WP_013718999.1; NC_015416.1.
DR AlphaFoldDB; F4C059; -.
DR FunCoup; F4C059; 7.
DR STRING; 990316.MCON_1239; -.
DR GeneID; 10460874; -.
DR KEGG; mcj:MCON_1239; -.
DR HOGENOM; CLU_056379_0_0_2; -.
DR InParanoid; F4C059; -.
DR OrthoDB; 10265at2157; -.
DR Proteomes; UP000007807; 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; NF002626; PRK02290.1-4; 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}; Lyase {ECO:0000313|EMBL:AEB67950.1};
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:UP000007807}.
FT DOMAIN 1..186
FT /note="3-dehydroquinate synthase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01959"
FT DOMAIN 200..373
FT /note="3-dehydroquinate synthase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF26558"
SQ SEQUENCE 373 AA; 40448 MW; 436688E19F1FA58D CRC64;
MKEKWLMARG SWEEIKPQIT TALESGFECV IVDRENVERV RELGNIQVAC FGAEKGAEDI
LVIGRHGEGD GSVPLPKDLN SSMDYALAKT ISGNKAAYVV IAGKKYEQFA VEMGKHVDYL
LVIGTDWKVI PLENMIAGLQ GCQVKIISGV KSSDEAKLAL ATLEQGADGV LLDSSDLSEI
KRVMRAAEQS EKGRLDLIPA RVVSVKPVGM GDRVCVDTAN MMVPGEGMLI GSQAKGFFLV
HSESEDSPYV AARPFRVNAG AVHAYIRVGE KTRYLSELKS GDEVTIVSKD GLSRSAIVGR
AKIEKRPMIL IEAEADGVLI STLLQNAETI KLVSSDGTPR PVTELKAGDE VLVHLEEAAR
HFGMKIEESI VER
//
