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}.
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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
//