ID G0L9G7_ZOBGA Unreviewed; 386 AA.
AC G0L9G7;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=3-Dehydroquinate synthase {ECO:0000313|EMBL:CAZ94564.1};
DE EC=4.2.3.4 {ECO:0000313|EMBL:CAZ94564.1};
GN Name=aroB1 {ECO:0000313|EMBL:CAZ94564.1};
GN OrderedLocusNames=zobellia_493 {ECO:0000313|EMBL:CAZ94564.1};
OS Zobellia galactanivorans (strain DSM 12802 / CCUG 47099 / CIP 106680 /
OS NCIMB 13871 / Dsij).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Zobellia.
OX NCBI_TaxID=63186 {ECO:0000313|EMBL:CAZ94564.1, ECO:0000313|Proteomes:UP000008898};
RN [1] {ECO:0000313|Proteomes:UP000008898}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12802 / CCUG 47099 / CIP 106680 / NCIMB 13871 / Dsij
RC {ECO:0000313|Proteomes:UP000008898};
RG Genoscope - CEA;
RT "Complete genome sequence of Zobellia galactanivorans Dsij.";
RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CAZ94564.1, ECO:0000313|Proteomes:UP000008898}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12802 / CCUG 47099 / CIP 106680 / NCIMB 13871 / Dsij
RC {ECO:0000313|Proteomes:UP000008898};
RX PubMed=22513138; DOI=10.1111/j.1462-2920.2012.02751.x;
RA Thomas F., Barbeyron T., Tonon T., Genicot S., Czjzek M., Michel G.;
RT "Characterization of the first alginolytic operons in a marine bacterium:
RT from their emergence in marine Flavobacteriia to their independent
RT transfers to marine Proteobacteria and human gut Bacteroides.";
RL Environ. Microbiol. 14:2379-2394(2012).
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; FP476056; CAZ94564.1; -; Genomic_DNA.
DR RefSeq; WP_013991876.1; NC_015844.1.
DR AlphaFoldDB; G0L9G7; -.
DR STRING; 63186.ZOBELLIA_493; -.
DR KEGG; zga:ZOBELLIA_493; -.
DR PATRIC; fig|63186.3.peg.488; -.
DR HOGENOM; CLU_001201_0_4_10; -.
DR OrthoDB; 9806583at2; -.
DR Proteomes; UP000008898; Chromosome.
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:0008652; P:amino acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd08198; DHQS-like; 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:SF7; 3-DEHYDROQUINATE SYNTHASE, CHLOROPLASTIC; 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:CAZ94564.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Reference proteome {ECO:0000313|Proteomes:UP000008898}.
FT DOMAIN 81..332
FT /note="3-dehydroquinate synthase"
FT /evidence="ECO:0000259|Pfam:PF01761"
SQ SEQUENCE 386 AA; 43346 MW; 087E2B3D20D37B9F CRC64;
MFKTIEQKFE VSYRYGLYFT ENLFGTTNTL FRDIIKEYKN EPVKLLFVID DGVALAHPQL
VKSIETYCQN YQENLVHMKS MVVQGGEACK NDQGQVEDIL KAVSEYAICR HSFVVVIGGG
AVIDMTGYAA AIAHRGVKLI RIPTTVLSQD DSAVGVKNSV NAFGKKNFIG TFAPPYAIIN
DTDFLKTLEQ RDWIAGISEA LKVALIKDAV FFEYLEKNAH LLRDRNMEAM QYTIYRCAEM
HMHHIAQGGD PFESGSSRPL DFGHWAAHKL EYMTNYALRH GEAVAKGIVL DVAYAHLIGL
INEADLNRIV RVFQNIGFDL SFPLASAKEV DELLNGIEEF REHLGGVLTI TLISDIGVKH
DVHEIDREVM KKALDVVNEI SKLKVE
//
