DHQS_METHJ
ID DHQS_METHJ Reviewed; 328 AA.
AC Q2FQ51;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 25-MAY-2022, entry version 73.
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}; OrderedLocusNames=Mhun_1034;
OS Methanospirillum hungatei JF-1 (strain ATCC 27890 / DSM 864 / NBRC 100397 /
OS JF-1).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales; Methanospirillaceae; Methanospirillum.
OX NCBI_TaxID=323259;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27890 / DSM 864 / NBRC 100397 / JF-1;
RX PubMed=26744606; DOI=10.1186/s40793-015-0124-8;
RA Gunsalus R.P., Cook L.E., Crable B., Rohlin L., McDonald E., Mouttaki H.,
RA Sieber J.R., Poweleit N., Zhou H., Lapidus A.L., Daligault H.E., Land M.,
RA Gilna P., Ivanova N., Kyrpides N., Culley D.E., McInerney M.J.;
RT "Complete genome sequence of Methanospirillum hungatei type strain JF1.";
RL Stand. Genomic Sci. 11:2-2(2016).
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; CP000254; ABD40784.1; -; Genomic_DNA.
DR RefSeq; WP_011448063.1; NC_007796.1.
DR AlphaFoldDB; Q2FQ51; -.
DR STRING; 323259.Mhun_1034; -.
DR EnsemblBacteria; ABD40784; ABD40784; Mhun_1034.
DR GeneID; 3924642; -.
DR KEGG; mhu:Mhun_1034; -.
DR eggNOG; arCOG04353; Archaea.
DR HOGENOM; CLU_056379_0_0_2; -.
DR OMA; HFGMAIK; -.
DR OrthoDB; 29853at2157; -.
DR Proteomes; UP000001941; 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: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; Reference proteome.
FT CHAIN 1..328
FT /note="3-dehydroquinate synthase"
FT /id="PRO_0000372055"
SQ SEQUENCE 328 AA; 35158 MW; 54451BB3FD20C51D CRC64;
MKQVFVDLRP WDKELAIAAL ESGAAGVIAD SAGPVRELGR ILVIAPDGDL IPGQDIHEIT
IGNTEDQARA MEAARTCRII VHTPDWTIIP LENLVACGDN VIAVVSDIKE AEQALTVLEK
GVSGVLVKTD DPDLVRSICR MVQSGISGQQ LHRLTVTTVK PAGMGERVCV DTCSLMVDGE
GMLVGNTSSG FFLVHAETLV NPYVAPRPFR VNAGGVHAYL QVPEGKTAYL ADLKAGDRVM
IVHGNGSCRE ATVGRVKIER RPLFLVEAES ECQKVSIILQ NAETIRLVRP DNSAVSVTSL
KPGDVVLGRV ESGGRHFGMA IDETIIEK