HEPPK_BORBR
ID HEPPK_BORBR Reviewed; 313 AA.
AC Q7WGU8;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=D-beta-D-heptose 7-phosphate kinase;
DE EC=2.7.1.167;
DE AltName: Full=D-beta-D-heptose 7-phosphotransferase;
DE AltName: Full=D-glycero-beta-D-manno-heptose-7-phosphate kinase;
GN Name=rfaE; OrderedLocusNames=BB3463;
OS Bordetella bronchiseptica (strain ATCC BAA-588 / NCTC 13252 / RB50)
OS (Alcaligenes bronchisepticus).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=257310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-588 / NCTC 13252 / RB50;
RX PubMed=12910271; DOI=10.1038/ng1227;
RA Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
RA Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
RA Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
RA Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T.,
RA Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S.,
RA Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E.,
RA Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M.,
RA Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S.,
RA Barrell B.G., Maskell D.J.;
RT "Comparative analysis of the genome sequences of Bordetella pertussis,
RT Bordetella parapertussis and Bordetella bronchiseptica.";
RL Nat. Genet. 35:32-40(2003).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, MASS SPECTROMETRY, AND PATHWAY.
RX PubMed=20050615; DOI=10.1021/bi902018y;
RA Wang L., Huang H., Nguyen H.H., Allen K.N., Mariano P.S.,
RA Dunaway-Mariano D.;
RT "Divergence of biochemical function in the HAD superfamily: D-glycero-D-
RT manno-heptose-1,7-bisphosphate phosphatase (GmhB).";
RL Biochemistry 49:1072-1081(2010).
CC -!- FUNCTION: Catalyzes the phosphorylation of D-glycero-D-manno-heptose 7-
CC phosphate at the C-1 position to selectively form D-glycero-beta-D-
CC manno-heptose-1,7-bisphosphate. {ECO:0000269|PubMed:20050615}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + D-glycero-beta-D-manno-heptose 7-phosphate = ADP + D-
CC glycero-beta-D-manno-heptose 1,7-bisphosphate + H(+);
CC Xref=Rhea:RHEA:27473, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:60204, ChEBI:CHEBI:60208, ChEBI:CHEBI:456216;
CC EC=2.7.1.167; Evidence={ECO:0000269|PubMed:20050615};
CC -!- PATHWAY: Nucleotide-sugar biosynthesis; ADP-L-glycero-beta-D-manno-
CC heptose biosynthesis; ADP-L-glycero-beta-D-manno-heptose from D-
CC glycero-beta-D-manno-heptose 7-phosphate: step 1/4.
CC {ECO:0000269|PubMed:20050615}.
CC -!- PATHWAY: Bacterial outer membrane biogenesis; LPS core biosynthesis.
CC {ECO:0000269|PubMed:20050615}.
CC -!- MASS SPECTROMETRY: Mass=33846; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:20050615};
CC -!- SIMILARITY: Belongs to the carbohydrate kinase PfkB family.
CC {ECO:0000305}.
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DR EMBL; BX640447; CAE33955.1; -; Genomic_DNA.
DR RefSeq; WP_003813350.1; NC_002927.3.
DR AlphaFoldDB; Q7WGU8; -.
DR SMR; Q7WGU8; -.
DR STRING; 257310.BB3463; -.
DR EnsemblBacteria; CAE33955; CAE33955; BB3463.
DR GeneID; 56477938; -.
DR GeneID; 66438018; -.
DR KEGG; bbr:BB3463; -.
DR eggNOG; COG2870; Bacteria.
DR HOGENOM; CLU_021150_0_1_4; -.
DR OMA; CEFANAA; -.
DR OrthoDB; 1030724at2; -.
DR BRENDA; 2.7.1.167; 227.
DR UniPathway; UPA00356; UER00437.
DR UniPathway; UPA00958; -.
DR Proteomes; UP000001027; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0033785; F:heptose 7-phosphate kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:InterPro.
DR GO; GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; IEA:InterPro.
DR GO; GO:0097171; P:ADP-L-glycero-beta-D-manno-heptose biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009244; P:lipopolysaccharide core region biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd01172; RfaE_like; 1.
DR Gene3D; 3.40.1190.20; -; 1.
DR InterPro; IPR002173; Carboh/pur_kinase_PfkB_CS.
DR InterPro; IPR011611; PfkB_dom.
DR InterPro; IPR011913; RfaE_dom_I.
DR InterPro; IPR029056; Ribokinase-like.
DR Pfam; PF00294; PfkB; 1.
DR SUPFAM; SSF53613; SSF53613; 1.
DR TIGRFAMs; TIGR02198; rfaE_dom_I; 1.
DR PROSITE; PS00583; PFKB_KINASES_1; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Carbohydrate metabolism; Kinase;
KW Lipopolysaccharide biosynthesis; Nucleotide-binding; Transferase.
FT CHAIN 1..313
FT /note="D-beta-D-heptose 7-phosphate kinase"
FT /id="PRO_0000424237"
FT ACT_SITE 264
FT /evidence="ECO:0000255"
FT BINDING 196..199
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 313 AA; 33846 MW; 0A8D381A6A5E88D0 CRC64;
MNQYPAERIA RARVLVVGDV MLDRYWFGEV DRISPEAPVP VVRVARREDR LGGAANVARN
VAALGAQVTL IGVVGADEVG HRIERMAAEE GVRTDLVSDT EHPTTLKMRV LGRQQQLLRV
DFEQHPEPAA LDGISAAVAR QLAQHDIVVL SDYAKGVLDR VESIIAAAVG HSLPVLVDPK
GDHYERYRGA TLVTPNRAEM REAVGRWKTE DELAERAQRL RLDLDLEALL VTRSEQGMTL
FTDAGRDHAD AAAHEVYDVS GAGDTVLATL AVMRAVGLSW GDAMRWANRA GGIVVGKLGT
SVVTAAELAG EST
