GenomeNet

Database: UniProt
Entry: A0A1U7LXC1_9FIRM
LinkDB: A0A1U7LXC1_9FIRM
Original site: A0A1U7LXC1_9FIRM 
ID   A0A1U7LXC1_9FIRM        Unreviewed;       347 AA.
AC   A0A1U7LXC1;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   SubName: Full=3-dehydroquinate synthase {ECO:0000313|EMBL:OLR64072.1};
GN   ORFNames=BIV18_00115 {ECO:0000313|EMBL:OLR64072.1};
OS   Peptoniphilus porci.
OC   Bacteria; Bacillota; Tissierellia; Tissierellales; Peptoniphilaceae;
OC   Peptoniphilus.
OX   NCBI_TaxID=1261639 {ECO:0000313|EMBL:OLR64072.1, ECO:0000313|Proteomes:UP000187166};
RN   [1] {ECO:0000313|EMBL:OLR64072.1, ECO:0000313|Proteomes:UP000187166}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=35-6-1 {ECO:0000313|EMBL:OLR64072.1,
RC   ECO:0000313|Proteomes:UP000187166};
RX   PubMed=27613689;
RA   Trachsel J., Bayles D.O., Looft T., Levine U.Y., Allen H.K.;
RT   "Function and Phylogeny of Bacterial Butyryl Coenzyme A:Acetate
RT   Transferases and Their Diversity in the Proximal Colon of Swine.";
RL   Appl. Environ. Microbiol. 82:6788-6798(2016).
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};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OLR64072.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; MJIH01000001; OLR64072.1; -; Genomic_DNA.
DR   RefSeq; WP_075658517.1; NZ_MJIH01000001.1.
DR   AlphaFoldDB; A0A1U7LXC1; -.
DR   STRING; 1465756.BIV18_00115; -.
DR   OrthoDB; 9806583at2; -.
DR   Proteomes; UP000187166; Unassembled WGS sequence.
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; 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          62..310
FT                   /note="3-dehydroquinate synthase"
FT                   /evidence="ECO:0000259|Pfam:PF01761"
SQ   SEQUENCE   347 AA;  39998 MW;  2A962C2276CDA737 CRC64;
     MKIQVKENNY TIDIVYKCEE KIKNFLNKNR DSKYLVITDE NVYNLYSERL KNIMYGLNFY
     IFKFPAGEKS KSMENYININ KFLLENNFNR GDIIIAFGGG VVGDISGFVA ATYLRGIDFI
     AMPTTLLSMI DSSVGGKNGI NFMNLKNQIG SFYFPKYVYI DYSFLETLDD RNINNGLAEI
     FKYSVLKDKN LFYYLKSCNK LDYKKIIYES LNIKLDFVKE DERDKGKRQK LNLGHTIGHG
     IESLSNYKLN HGESIGIGTI YMARAAYKMG IAKSDFSKEL ILAFKNHNLP TSYDFDTDEI
     LEILKHDKKI NKNLINVILP IKIGEVINKK VTFDELREIV ELGKGNE
//
DBGET integrated database retrieval system