AROB_FUSNN
ID AROB_FUSNN Reviewed; 664 AA.
AC Q8RF47;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Bifunctional 3-dehydroquinate synthase/phosphatase;
DE Includes:
DE RecName: Full=3-dehydroquinate synthase;
DE EC=4.2.3.4;
DE Includes:
DE RecName: Full=Unknown phosphatase;
DE EC=3.6.1.-;
GN Name=aroB; OrderedLocusNames=FN0871;
OS Fusobacterium nucleatum subsp. nucleatum (strain ATCC 25586 / DSM 15643 /
OS BCRC 10681 / CIP 101130 / JCM 8532 / KCTC 2640 / LMG 13131 / VPI 4355).
OC Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; Fusobacterium.
OX NCBI_TaxID=190304;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25586 / DSM 15643 / BCRC 10681 / CIP 101130 / JCM 8532 / KCTC
RC 2640 / LMG 13131 / VPI 4355;
RX PubMed=11889109; DOI=10.1128/jb.184.7.2005-2018.2002;
RA Kapatral V., Anderson I., Ivanova N., Reznik G., Los T., Lykidis A.,
RA Bhattacharyya A., Bartman A., Gardner W., Grechkin G., Zhu L., Vasieva O.,
RA Chu L., Kogan Y., Chaga O., Goltsman E., Bernal A., Larsen N., D'Souza M.,
RA Walunas T., Pusch G., Haselkorn R., Fonstein M., Kyrpides N.C.,
RA Overbeek R.;
RT "Genome sequence and analysis of the oral bacterium Fusobacterium nucleatum
RT strain ATCC 25586.";
RL J. Bacteriol. 184:2005-2018(2002).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-
CC dehydroquinate + phosphate; Xref=Rhea:RHEA:21968, ChEBI:CHEBI:32364,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58394; EC=4.2.3.4;
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540; Evidence={ECO:0000250};
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000250};
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 divalent metal cation per subunit. Can use either Co(2+)
CC or Zn(2+). {ECO:0000250};
CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC 2/7.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the sugar phosphate
CC cyclases superfamily. Dehydroquinate synthase family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the GppA/Ppx family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE009951; AAL95067.1; -; Genomic_DNA.
DR RefSeq; NP_603768.1; NC_003454.1.
DR AlphaFoldDB; Q8RF47; -.
DR SMR; Q8RF47; -.
DR STRING; 190304.FN0871; -.
DR EnsemblBacteria; AAL95067; AAL95067; FN0871.
DR KEGG; fnu:FN0871; -.
DR PATRIC; fig|190304.8.peg.1433; -.
DR eggNOG; COG0248; Bacteria.
DR eggNOG; COG0337; Bacteria.
DR HOGENOM; CLU_025862_0_0_0; -.
DR InParanoid; Q8RF47; -.
DR OMA; NIICFAT; -.
DR BioCyc; FNUC190304:G1FZS-1454-MON; -.
DR UniPathway; UPA00053; UER00085.
DR Proteomes; UP000002521; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003856; F:3-dehydroquinate synthase activity; IBA:GO_Central.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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; IBA:GO_Central.
DR GO; GO:0008652; P:cellular amino acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway.
DR HAMAP; MF_00110; DHQ_synthase; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR016037; DHQ_synth_AroB.
DR InterPro; IPR030960; DHQS/DOIS.
DR InterPro; IPR003695; Ppx_GppA.
DR Pfam; PF01761; DHQ_synthase; 1.
DR Pfam; PF02541; Ppx-GppA; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR TIGRFAMs; TIGR01357; aroB; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Cobalt;
KW Cytoplasm; Hydrolase; Lyase; Metal-binding; Multifunctional enzyme; NAD;
KW Nucleotide-binding; Reference proteome; Zinc.
FT CHAIN 1..664
FT /note="Bifunctional 3-dehydroquinate synthase/phosphatase"
FT /id="PRO_0000140814"
FT REGION 1..352
FT /note="3-dehydroquinate synthase"
FT REGION 353..664
FT /note="GPPA/PPX"
FT BINDING 61..66
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P9WPX9"
FT BINDING 95..99
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P9WPX9"
FT BINDING 119..120
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P9WPX9"
FT BINDING 132
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P9WPX9"
FT BINDING 141
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P9WPX9"
FT BINDING 159..162
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P9WPX9"
FT BINDING 174
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P9WPX9"
FT BINDING 238
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P9WPX9"
FT BINDING 255
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P9WPX9"
SQ SEQUENCE 664 AA; 76592 MW; BAA617D1664402AF CRC64;
MKKIFDDIYV GSNIISKLND YTEDFDKILI FSNETIADLY FEKFKSTLNE KDKVFYFAIK
DGEEYKNIES ILPVYDFMLE NNFSRKSLII SLGGGVICDM GGYISATYMR GIEFIQVPTS
LLAQVDASVG GKVAINHPKC KNMIGSFKNP YRVIIDVEFL KTLPKREFKS GMGELLKHSF
LTKDKSYLEY IENNVEKIKN LDNEVLENIV EQSIRIKKHY VDIDPFEKGE RAFLNLGHTY
AHALESFFDY KAYTHGEAVS KGIIFDLELS LLRGQIDKEY LERARNIFKL FDIDTDLIYL
PSDKFIPLMR KDKKNSFNKI ITILLDSEGH LSKTEVKEDE IVKIIDKYKN NFLRASIDIG
TNSCRLLIAE VEKDNENITF KKEIYKDLEI VKLGEDVNKN KFLKEEAIER TLKCLKKYRK
IIDKYSIEEK NIICFATSAT RDSTNKDYFI KKVFDETKIK INCISGDKEA YINFKGVISS
FDRDFKDNIL VFDIGGGSTE FTLGNMQGIE KKISLNIGSV RITEKFFLNN KLYNYSEENR
IKAKDWVKEN LKELEDFKKL NFSLIGVAGT TTTQVSVREK MEVYDSEKIH LSNLTSKEIN
DNLSLFIKNI NKQEIKGLDP KRKDVIIGGT IILKEILDYF GKDFIIVSEN DNLMGAILEG
VENK
