ID S7VJT7_9FLAO Unreviewed; 356 AA.
AC S7VJT7;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE SubName: Full=3-dehydroquinate synthase {ECO:0000313|EMBL:EPR69737.1};
DE EC=4.2.3.4 {ECO:0000313|EMBL:EPR69737.1};
GN ORFNames=ADIWIN_4012 {ECO:0000313|EMBL:EPR69737.1};
OS Winogradskyella psychrotolerans RS-3.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Winogradskyella.
OX NCBI_TaxID=641526 {ECO:0000313|EMBL:EPR69737.1, ECO:0000313|Proteomes:UP000014962};
RN [1] {ECO:0000313|EMBL:EPR69737.1, ECO:0000313|Proteomes:UP000014962}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RS-3 {ECO:0000313|EMBL:EPR69737.1,
RC ECO:0000313|Proteomes:UP000014962};
RX PubMed=23950132;
RA Kumar Pinnaka A., Ara S., Singh A., Shivaji S.;
RT "Draft Genome Sequence of Winogradskyella psychrotolerans RS-3T, Isolated
RT from the Marine Transect of Kongsfjorden, Ny-Alesund, Svalbard, Arctic
RT Ocean.";
RL Genome Announc. 1:e00630-e00613(2013).
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:EPR69737.1}.
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DR EMBL; ATMR01000215; EPR69737.1; -; Genomic_DNA.
DR RefSeq; WP_020896270.1; NZ_ATMR01000215.1.
DR AlphaFoldDB; S7VJT7; -.
DR STRING; 641526.ADIWIN_4012; -.
DR PATRIC; fig|641526.4.peg.3984; -.
DR eggNOG; COG0337; Bacteria.
DR OrthoDB; 9806583at2; -.
DR Proteomes; UP000014962; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
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: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, ECO:0000313|EMBL:EPR69737.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000014962};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 63..320
FT /note="3-dehydroquinate synthase"
FT /evidence="ECO:0000259|Pfam:PF01761"
SQ SEQUENCE 356 AA; 39439 MW; 54D13870E2B204DB CRC64;
MESISTKNAV VHFNSEVYTE LNNYIKTAKP SKIFILVDTN THDYCLPKFQ ERIESHDIAI
EVMEMPNGEE HKSIDICTGV WEALSEYNAD RKSLLINLGG GVVTDLGGFV ASTYMRGITY
INIPTSLLAM VDASVGGKTG VDLGTLKNQV GVINEGVMVG VDTSFLDTLP QNEMVSGFAE
MLKHGLIYDE AYWNTLTNLE NLDLSDLDGL IYDSIVIKNT VVTSDPTEQG LRKILNFGHT
LGHAIESYFM ENADKTPLLH GEAIAIGMIL ETYLSTKICG LSHDHLEIIT KGILKTFSKV
EITKVDQQQI IEFLKYDKKN SHGVVKFVLL EAIGKPKLDC VVSNDLIIEA FDYYAN
//