DHQS_METBU
ID DHQS_METBU Reviewed; 379 AA.
AC Q12UJ7;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
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}; OrderedLocusNames=Mbur_2000;
OS Methanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 /
OS ACE-M).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanococcoides.
OX NCBI_TaxID=259564;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6242 / NBRC 107633 / OCM 468 / ACE-M;
RX PubMed=19404327; DOI=10.1038/ismej.2009.45;
RA Allen M.A., Lauro F.M., Williams T.J., Burg D., Siddiqui K.S.,
RA De Francisci D., Chong K.W., Pilak O., Chew H.H., De Maere M.Z., Ting L.,
RA Katrib M., Ng C., Sowers K.R., Galperin M.Y., Anderson I.J., Ivanova N.,
RA Dalin E., Martinez M., Lapidus A., Hauser L., Land M., Thomas T.,
RA Cavicchioli R.;
RT "The genome sequence of the psychrophilic archaeon, Methanococcoides
RT burtonii: the role of genome evolution in cold adaptation.";
RL ISME J. 3:1012-1035(2009).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABE52879.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000300; ABE52879.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; Q12UJ7; -.
DR STRING; 259564.Mbur_2000; -.
DR EnsemblBacteria; ABE52879; ABE52879; Mbur_2000.
DR KEGG; mbu:Mbur_2000; -.
DR HOGENOM; CLU_056379_0_0_2; -.
DR Proteomes; UP000001979; 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..379
FT /note="3-dehydroquinate synthase"
FT /id="PRO_0000372048"
SQ SEQUENCE 379 AA; 40943 MW; 196F989C9FC45E45 CRC64;
MDKTIWIKAD KGHWEAHKDR ITTGLESGAN CVLVNSDEVE KVRELGDIQV AAFTYDDKSG
ADIVVVGKGG EGDGTKPLSP DPVGSLDMIT AIRLKEKGLT VGAYVVIQNK KYEEFAAEIG
KECDFLIIVG TDWKVIPLEN LIAALQDSDV KIIAGVRDQD EAKLALETME HGSEGVLLDS
DDPNTIKATV AVAERSGIED LKLVPGKVTK VEAVGMGDRV CVDTCNMMTK GEGMLVGSQA
SGMFLVHSES EESPYVASRP FRVNAGAVHA YVKVGDRTRY LSELSSGDEV TIVNAGGKQR
TGIVGRVKIE RRPLMLVEAE VNGEIIKNIL QNAETIKLVD INGEPISVAD LKPGNEVMVY
YEGGARHFGM KVEETIIEK