ID C9LPG2_9FIRM Unreviewed; 357 AA.
AC C9LPG2;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=3-dehydroquinate synthase {ECO:0000313|EMBL:EEW97448.1};
DE EC=4.2.3.4 {ECO:0000313|EMBL:EEW97448.1};
GN Name=aroB {ECO:0000313|EMBL:EEW97448.1};
GN ORFNames=GCWU000321_01441 {ECO:0000313|EMBL:EEW97448.1};
OS Dialister invisus DSM 15470.
OC Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC Dialister.
OX NCBI_TaxID=592028 {ECO:0000313|EMBL:EEW97448.1, ECO:0000313|Proteomes:UP000004736};
RN [1] {ECO:0000313|EMBL:EEW97448.1, ECO:0000313|Proteomes:UP000004736}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15470 {ECO:0000313|EMBL:EEW97448.1,
RC ECO:0000313|Proteomes:UP000004736};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases.
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:EEW97448.1}.
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DR EMBL; ACIM02000001; EEW97448.1; -; Genomic_DNA.
DR RefSeq; WP_007070380.1; NZ_GG698602.1.
DR AlphaFoldDB; C9LPG2; -.
DR STRING; 592028.GCWU000321_01441; -.
DR GeneID; 78278025; -.
DR eggNOG; COG0337; Bacteria.
DR HOGENOM; CLU_001201_0_1_9; -.
DR OrthoDB; 9806583at2; -.
DR Proteomes; UP000004736; Unassembled WGS sequence.
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: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; IPR030963; DHQ_synth_fam.
DR InterPro; IPR030960; DHQS/DOIS.
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, ECO:0000313|EMBL:EEW97448.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW NAD {ECO:0000256|ARBA:ARBA00023027}.
FT DOMAIN 68..310
FT /note="3-dehydroquinate synthase"
FT /evidence="ECO:0000259|Pfam:PF01761"
SQ SEQUENCE 357 AA; 39214 MW; 0CF35F21F3A53EF2 CRC64;
MDTVHINLGN DSYDVIIDSG IIGRLGKETA PLSGHGRAVI ITEEGIDELY GQDLKRQLEK
ENLNVQQIVL SSSEKSRSLS VVSRVCEALA DFGFCAGDLL IGLGGRVVGD VTGFVAATYR
RGTPYVQVPT SLLAQIGSAI GGKISIDING RKNLIGTFYQ PKAVYVDPAM VRTLPARFFH
NGLGEAIKIG CVADKDLFEI FEKAASDQDI LRVLPEIIRR CITIKAHYVE IDPEDKGERR
ILDFGHTLGG AAERYYRFND LRLTHGEATA AGMYMITSAS EILGLTKRGT AERIKYVLQS
IGLPTNLDVP RDILVSLLEH GKNVKDEKIE TPLVLEIGKG YIYTGEIETL KKYIQME
//