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Database: UniProt
Entry: F4FZT7_METCR
LinkDB: F4FZT7_METCR
Original site: F4FZT7_METCR 
ID   F4FZT7_METCR            Unreviewed;       348 AA.
AC   F4FZT7;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 63.
DE   SubName: Full=3-dehydroquinate synthase {ECO:0000313|EMBL:AEB94516.1};
GN   OrderedLocusNames=Mcup_0408 {ECO:0000313|EMBL:AEB94516.1};
OS   Metallosphaera cuprina (strain Ar-4).
OC   Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Metallosphaera.
OX   NCBI_TaxID=1006006 {ECO:0000313|EMBL:AEB94516.1, ECO:0000313|Proteomes:UP000007812};
RN   [1] {ECO:0000313|EMBL:AEB94516.1, ECO:0000313|Proteomes:UP000007812}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ar-4 {ECO:0000313|EMBL:AEB94516.1,
RC   ECO:0000313|Proteomes:UP000007812};
RX   PubMed=21551305; DOI=10.1128/JB.05038-11;
RA   Liu L.J., You X.Y., Zheng H., Wang S., Jiang C.Y., Liu S.J.;
RT   "Complete genome sequence of Metallosphaera cuprina, a metal sulfide-
RT   oxidizing archaeon from a hot spring.";
RL   J. Bacteriol. 193:3387-3388(2011).
CC   -!- COFACTOR:
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC         Evidence={ECO:0000256|ARBA:ARBA00001941};
CC   -!- COFACTOR:
CC       Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC         Evidence={ECO:0000256|ARBA:ARBA00001911};
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DR   EMBL; CP002656; AEB94516.1; -; Genomic_DNA.
DR   RefSeq; WP_013737014.1; NC_015435.1.
DR   AlphaFoldDB; F4FZT7; -.
DR   STRING; 1006006.Mcup_0408; -.
DR   GeneID; 10492602; -.
DR   KEGG; mcn:Mcup_0408; -.
DR   PATRIC; fig|1006006.8.peg.410; -.
DR   eggNOG; arCOG00983; Archaea.
DR   HOGENOM; CLU_001201_0_1_2; -.
DR   OrthoDB; 21407at2157; -.
DR   Proteomes; UP000007812; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0003856; F:3-dehydroquinate synthase activity; IEA:InterPro.
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:InterPro.
DR   CDD; cd08195; DHQS; 1.
DR   Gene3D; 3.40.50.1970; -; 1.
DR   Gene3D; 1.20.1090.10; Dehydroquinate synthase-like - alpha domain; 1.
DR   InterPro; IPR016037; DHQ_synth_AroB.
DR   InterPro; IPR030963; DHQ_synth_fam.
DR   InterPro; IPR030960; DHQS/DOIS.
DR   NCBIfam; TIGR01357; aroB; 1.
DR   PANTHER; PTHR43622; 3-DEHYDROQUINATE SYNTHASE; 1.
DR   PANTHER; PTHR43622:SF1; 3-DEHYDROQUINATE SYNTHASE DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF01761; DHQ_synthase; 1.
DR   PIRSF; PIRSF001455; DHQ_synth; 1.
DR   SUPFAM; SSF56796; Dehydroquinate synthase-like; 1.
PE   4: Predicted;
KW   Cobalt {ECO:0000256|ARBA:ARBA00023285};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          50..311
FT                   /note="3-dehydroquinate synthase"
FT                   /evidence="ECO:0000259|Pfam:PF01761"
SQ   SEQUENCE   348 AA;  38665 MW;  8F3BD704769ADCB5 CRC64;
     MIDFSEKICC SEVRVKIGRE VLGELDSLQG KKGIVHPRTL RTQLKADLDI EIEDGERGKD
     ISVAMRIVDE LLSSGFTRGD YLIAMGGGTV LDVTGFSASI FMRGLNLINV PTTLLGMVDA
     AIGGKNGVNY RLAKNMIGTF YQPFMIVEDL SFLDTLPVEE FRRGMAEVIK YALVLDKELY
     DFLSLNHDSI MKRNQDVLEK VIYSSVKDKL FVVSEDERET KGVRIVLNFG HTIGHAIEAG
     SDFKVPHGLA ISVGMVCEAK IAEEMGYAEE GVVEDVLWLL QLYGLPISMD QLNAKVEVER
     ALKSMLMDKK RRGEETLMPF PTRIGNWRSV SVPNDTLVSF SKQCLGGN
//
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