AROD_METMP
ID AROD_METMP Reviewed; 218 AA.
AC Q6LXF7;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=3-dehydroquinate dehydratase {ECO:0000255|HAMAP-Rule:MF_00214};
DE Short=3-dehydroquinase {ECO:0000255|HAMAP-Rule:MF_00214};
DE EC=4.2.1.10 {ECO:0000255|HAMAP-Rule:MF_00214};
DE AltName: Full=Type I DHQase {ECO:0000255|HAMAP-Rule:MF_00214};
DE AltName: Full=Type I dehydroquinase {ECO:0000255|HAMAP-Rule:MF_00214};
DE Short=DHQ1 {ECO:0000255|HAMAP-Rule:MF_00214};
GN Name=aroD {ECO:0000255|HAMAP-Rule:MF_00214}; OrderedLocusNames=MMP1394;
OS Methanococcus maripaludis (strain S2 / LL).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanococcaceae; Methanococcus.
OX NCBI_TaxID=267377;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S2 / LL;
RX PubMed=15466049; DOI=10.1128/jb.186.20.6956-6969.2004;
RA Hendrickson E.L., Kaul R., Zhou Y., Bovee D., Chapman P., Chung J.,
RA Conway de Macario E., Dodsworth J.A., Gillett W., Graham D.E., Hackett M.,
RA Haydock A.K., Kang A., Land M.L., Levy R., Lie T.J., Major T.A.,
RA Moore B.C., Porat I., Palmeiri A., Rouse G., Saenphimmachak C., Soell D.,
RA Van Dien S., Wang T., Whitman W.B., Xia Q., Zhang Y., Larimer F.W.,
RA Olson M.V., Leigh J.A.;
RT "Complete genome sequence of the genetically tractable hydrogenotrophic
RT methanogen Methanococcus maripaludis.";
RL J. Bacteriol. 186:6956-6969(2004).
RN [2]
RP FUNCTION IN AROAAS BIOSYNTHESIS, PATHWAY, AND DISRUPTION PHENOTYPE.
RC STRAIN=S2 / LL;
RX PubMed=15262931; DOI=10.1128/jb.186.15.4940-4950.2004;
RA Porat I., Waters B.W., Teng Q., Whitman W.B.;
RT "Two biosynthetic pathways for aromatic amino acids in the archaeon
RT Methanococcus maripaludis.";
RL J. Bacteriol. 186:4940-4950(2004).
CC -!- FUNCTION: Involved in the third step of the chorismate pathway, which
CC leads to the biosynthesis of aromatic amino acids. Catalyzes the cis-
CC dehydration of 3-dehydroquinate (DHQ) and introduces the first double
CC bond of the aromatic ring to yield 3-dehydroshikimate.
CC {ECO:0000255|HAMAP-Rule:MF_00214, ECO:0000269|PubMed:15262931}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-dehydroquinate = 3-dehydroshikimate + H2O;
CC Xref=Rhea:RHEA:21096, ChEBI:CHEBI:15377, ChEBI:CHEBI:16630,
CC ChEBI:CHEBI:32364; EC=4.2.1.10; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00214};
CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC 3/7. {ECO:0000255|HAMAP-Rule:MF_00214, ECO:0000269|PubMed:15262931}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00214}.
CC -!- DISRUPTION PHENOTYPE: Deletion mutant is auxotrophic for all three
CC aromatic amino acids (AroAAs) and lacks 3-dehydroquinate dehydratase
CC activity. {ECO:0000269|PubMed:15262931}.
CC -!- SIMILARITY: Belongs to the type-I 3-dehydroquinase family.
CC {ECO:0000255|HAMAP-Rule:MF_00214}.
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DR EMBL; BX950229; CAF30950.1; -; Genomic_DNA.
DR RefSeq; WP_011171338.1; NC_005791.1.
DR AlphaFoldDB; Q6LXF7; -.
DR SMR; Q6LXF7; -.
DR STRING; 267377.MMP1394; -.
DR EnsemblBacteria; CAF30950; CAF30950; MMP1394.
DR GeneID; 2762224; -.
DR KEGG; mmp:MMP1394; -.
DR PATRIC; fig|267377.15.peg.1430; -.
DR eggNOG; arCOG02097; Archaea.
DR HOGENOM; CLU_064444_2_1_2; -.
DR OMA; ATMAMGE; -.
DR OrthoDB; 75928at2157; -.
DR BioCyc; MetaCyc:MON-14591; -.
DR BioCyc; MMAR267377:MMP_RS07175-MON; -.
DR UniPathway; UPA00053; UER00086.
DR Proteomes; UP000000590; Chromosome.
DR GO; GO:0003855; F:3-dehydroquinate dehydratase activity; 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 GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00502; DHQase_I; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR HAMAP; MF_00214; AroD; 1.
DR InterPro; IPR018508; 3-dehydroquinate_DH_AS.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR001381; DHquinase_I.
DR Pfam; PF01487; DHquinase_I; 1.
DR TIGRFAMs; TIGR01093; aroD; 1.
DR PROSITE; PS01028; DEHYDROQUINASE_I; 1.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Lyase;
KW Reference proteome; Schiff base.
FT CHAIN 1..218
FT /note="3-dehydroquinate dehydratase"
FT /id="PRO_1000043175"
FT ACT_SITE 116
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00214"
FT ACT_SITE 142
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00214"
FT BINDING 29..31
FT /ligand="3-dehydroquinate"
FT /ligand_id="ChEBI:CHEBI:32364"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00214"
FT BINDING 56
FT /ligand="3-dehydroquinate"
FT /ligand_id="ChEBI:CHEBI:32364"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00214"
FT BINDING 180
FT /ligand="3-dehydroquinate"
FT /ligand_id="ChEBI:CHEBI:32364"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00214"
FT BINDING 200
FT /ligand="3-dehydroquinate"
FT /ligand_id="ChEBI:CHEBI:32364"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00214"
FT BINDING 204
FT /ligand="3-dehydroquinate"
FT /ligand_id="ChEBI:CHEBI:32364"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00214"
SQ SEQUENCE 218 AA; 24532 MW; 306F9DD8A3D91FC0 CRC64;
MICIPVIDKD VSDAINSAKE ALKYGDIVEF RIDLLNDVNF KDIEEFSKIP SIITIRAEWE
GGAWRKSNEE RIELLKNAIK NNAKFIDIEL KEEKNLELVK YRNEIGSTTK IIVSYHDFEK
TPEIDELIDV VEKELKIGDI AKFATFAHSK EDTLKILNLM NRYSGKIIAI GMGESGKLTR
ILGLDFGSIL TFASMGGKAS APGQVDVKKL KEILKLIN
