AROB_AERPE
ID AROB_AERPE Reviewed; 358 AA.
AC Q9YEJ9;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=3-dehydroquinate synthase {ECO:0000250|UniProtKB:P07639};
DE Short=DHQS {ECO:0000250|UniProtKB:P07639};
DE EC=4.2.3.4 {ECO:0000250|UniProtKB:P07639};
GN Name=aroB; OrderedLocusNames=APE_0579;
OS Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 /
OS K1).
OC Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC Desulfurococcaceae; Aeropyrum.
OX NCBI_TaxID=272557;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1;
RX PubMed=10382966; DOI=10.1093/dnares/6.2.83;
RA Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K.,
RA Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A.,
RA Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S.,
RA Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A.,
RA Aoki K., Kubota K., Nakamura Y., Nomura N., Sako Y., Kikuchi H.;
RT "Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon,
RT Aeropyrum pernix K1.";
RL DNA Res. 6:83-101(1999).
CC -!- FUNCTION: Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate
CC 7-phosphate (DAHP) to dehydroquinate (DHQ).
CC {ECO:0000250|UniProtKB:P07639}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-
CC dehydroquinate + phosphate; Xref=Rhea:RHEA:21968, ChEBI:CHEBI:32364,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58394; EC=4.2.3.4;
CC Evidence={ECO:0000250|UniProtKB:P07639};
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Evidence={ECO:0000250|UniProtKB:P07639};
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000250|UniProtKB:P07639};
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P07639};
CC Note=Binds 1 divalent metal cation per subunit. Can use either Co(2+)
CC or Zn(2+). {ECO:0000250|UniProtKB:P07639};
CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC 2/7. {ECO:0000250|UniProtKB:P07639}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P07639}.
CC -!- SIMILARITY: Belongs to the sugar phosphate cyclases superfamily.
CC Dehydroquinate synthase family. {ECO:0000305}.
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DR EMBL; BA000002; BAA79547.1; -; Genomic_DNA.
DR PIR; C72643; C72643.
DR AlphaFoldDB; Q9YEJ9; -.
DR SMR; Q9YEJ9; -.
DR STRING; 272557.APE_0579; -.
DR EnsemblBacteria; BAA79547; BAA79547; APE_0579.
DR KEGG; ape:APE_0579; -.
DR PATRIC; fig|272557.25.peg.428; -.
DR eggNOG; arCOG00983; Archaea.
DR OMA; YGVIWDA; -.
DR UniPathway; UPA00053; UER00085.
DR Proteomes; UP000002518; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003856; F:3-dehydroquinate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-KW.
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 InterPro; IPR016037; DHQ_synth_AroB.
DR InterPro; IPR030963; DHQ_synth_fam.
DR InterPro; IPR030960; DHQS/DOIS.
DR Pfam; PF01761; DHQ_synthase; 1.
DR PIRSF; PIRSF001455; DHQ_synth; 1.
DR TIGRFAMs; TIGR01357; aroB; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Cobalt;
KW Cytoplasm; Lyase; Metal-binding; NAD; Nucleotide-binding;
KW Reference proteome; Zinc.
FT CHAIN 1..358
FT /note="3-dehydroquinate synthase"
FT /id="PRO_0000140815"
FT BINDING 72..77
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P9WPX9"
FT BINDING 106..110
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P9WPX9"
FT BINDING 130..131
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P9WPX9"
FT BINDING 143
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P9WPX9"
FT BINDING 151
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q6GGU4"
FT BINDING 184
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P9WPX9"
FT BINDING 245
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P9WPX9"
FT BINDING 261
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P9WPX9"
SQ SEQUENCE 358 AA; 37446 MW; 45EFBCEB9A33DBD4 CRC64;
MAQAAVERRV FRLSVDEETV VAAGVGALSE APRAAGGTAY IVHEEALSAE AARLARILEA
RGVEVLGAVA GGGERVKSLD WVTRLWDLML QAGVERSTTV YIIGGGALLD AAGFAASTLM
RGLSTVNIPS TTLAAFDAAA GGKTGVNLRG KNMVGTFHNP RMVLVEPGIV AGQPDEGYRD
GFAELVKHVA LSGDREPAAS LLPQALARRP APLARLAFWS LGYKMQVVAG DPRERGLRRI
LNLGHTIGHA LEAASSYTLS HGRSVSIGLA GELELSRRLA GLPRGEAEDV LDMLSTAGLP
LEPPPGLAGE AAGLVGLDKK REGGSIVMPL LERLGRPRLS RVPVETVSRL MVELWGGG
