ID A0A1F6APU7_9BACT Unreviewed; 363 AA.
AC A0A1F6APU7;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=3-dehydroquinate synthase domain-containing protein {ECO:0000259|Pfam:PF01761};
GN ORFNames=A2960_00910 {ECO:0000313|EMBL:OGG26716.1};
OS Candidatus Gottesmanbacteria bacterium RIFCSPLOWO2_01_FULL_39_12b.
OC Bacteria; Candidatus Gottesmanbacteria.
OX NCBI_TaxID=1798388 {ECO:0000313|EMBL:OGG26716.1, ECO:0000313|Proteomes:UP000176609};
RN [1] {ECO:0000313|EMBL:OGG26716.1, ECO:0000313|Proteomes:UP000176609}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(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:OGG26716.1}.
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DR EMBL; MFJR01000007; OGG26716.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F6APU7; -.
DR Proteomes; UP000176609; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016838; F:carbon-oxygen lyase activity, acting on phosphates; IEA:InterPro.
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}; Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 256..274
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 59..323
FT /note="3-dehydroquinate synthase"
FT /evidence="ECO:0000259|Pfam:PF01761"
SQ SEQUENCE 363 AA; 42156 MW; C6564A90E0785C10 CRC64;
MDELVIKSKI KDFKVKFVDN TNFLKEMFTI PHYVVFVGSI VHEFYKEKIF DRFPNEKMIV
MKLDEEKKTI DTAIKLYKKL MTKQGKKNLT MISFGGGINQ DIAGFVASTL YRGINWIYVP
TTLLAMADSS IGLKTSLNFG SIKNMIGSFY PPTEVYIDIN FLKTLKRQDY ASGVGEIMKL
LLMKEDSSKN LAKIVEKVEI LDCQEDKKRM IEIIKEAMQI KLSYMEGDEF DKGRRNLLNY
GHEFGHALEP ASDYQVPHGI AIVIGMIFAN YISVKRKWMR SKLFDYLNEN IFIPYMRRSM
IKLKKDFFKP STLLANMKKD KKRESSDLVL ILPKENLNLC KVQDLTIQEF ETGLREVQKI
LIF
//
