ID F2AY86_RHOBT Unreviewed; 383 AA.
AC F2AY86;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=3-dehydroquinate synthase {ECO:0000313|EMBL:EGF25403.1};
GN ORFNames=RBWH47_00873 {ECO:0000313|EMBL:EGF25403.1};
OS Rhodopirellula baltica WH47.
OC Bacteria; Planctomycetota; Planctomycetia; Pirellulales; Pirellulaceae;
OC Rhodopirellula.
OX NCBI_TaxID=991778 {ECO:0000313|EMBL:EGF25403.1, ECO:0000313|Proteomes:UP000006222};
RN [1] {ECO:0000313|EMBL:EGF25403.1, ECO:0000313|Proteomes:UP000006222}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WH47 {ECO:0000313|EMBL:EGF25403.1,
RC ECO:0000313|Proteomes:UP000006222};
RX PubMed=23273849;
RA Wegner C.E., Richter-Heitmann T., Klindworth A., Klockow C., Richter M.,
RA Achstetter T., Glockner F.O., Harder J.;
RT "Expression of sulfatases in Rhodopirellula baltica and the diversity of
RT sulfatases in the genus Rhodopirellula.";
RL Mar. Genomics 0:0-0(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};
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:EGF25403.1}.
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DR EMBL; AFAR01000232; EGF25403.1; -; Genomic_DNA.
DR RefSeq; WP_007328596.1; NZ_AFAR01000232.1.
DR AlphaFoldDB; F2AY86; -.
DR PATRIC; fig|991778.3.peg.4966; -.
DR Proteomes; UP000006222; Unassembled WGS sequence.
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: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};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW NAD {ECO:0000256|ARBA:ARBA00023027}.
FT DOMAIN 80..332
FT /note="3-dehydroquinate synthase"
FT /evidence="ECO:0000259|Pfam:PF01761"
SQ SEQUENCE 383 AA; 42184 MW; 4FBE71787D653A9D CRC64;
MTEHDISFEV KFVHRLRQTD DVSQADFPVL ESVLHGEQSD TAAPKALFCL DSNLEGGEFA
TALIEKMRTS DRMRLVREPM IVPGGESCKN SEHTLRDLLA AINSHDLDRR SYIIVAGGGA
VLDAVGFAAS IAHRGVRLIR LPSTTLAQAD SGVGVKNAIN YFEKKNWIGS FAVPWAVFND
TAILKTLPDR DFRSGLTEAV KVALLKDSAF FDFLRRSASK LRRRVADVSK EAIACSCQLH
LDHITAGGDP FEALEARPLD FGHWSAHRME PMSNYALRHG EAVGIGVALD TLYSARKFGF
PTPLAHAVCQ TIADLGSPLW CDQLDTPDEV LRGLEEFRQH LGGRLTVTML KNPGEAINVH
EIDLPVMKSC IDELREIAKQ QTA
//
