PFKA_BORBU
ID PFKA_BORBU Reviewed; 447 AA.
AC O51669;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 25-JAN-2012, sequence version 2.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=ATP-dependent 6-phosphofructokinase {ECO:0000255|HAMAP-Rule:MF_01981};
DE Short=ATP-PFK {ECO:0000255|HAMAP-Rule:MF_01981};
DE Short=Phosphofructokinase {ECO:0000255|HAMAP-Rule:MF_01981};
DE EC=2.7.1.11 {ECO:0000255|HAMAP-Rule:MF_01981};
DE AltName: Full=Phosphohexokinase {ECO:0000255|HAMAP-Rule:MF_01981};
GN Name=pfkA {ECO:0000255|HAMAP-Rule:MF_01981}; OrderedLocusNames=BB_0727;
OS Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31)
OS (Borrelia burgdorferi).
OC Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX NCBI_TaxID=224326;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31;
RX PubMed=9403685; DOI=10.1038/37551;
RA Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A.,
RA Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K., Gwinn M.L.,
RA Dougherty B.A., Tomb J.-F., Fleischmann R.D., Richardson D.L.,
RA Peterson J.D., Kerlavage A.R., Quackenbush J., Salzberg S.L., Hanson M.,
RA van Vugt R., Palmer N., Adams M.D., Gocayne J.D., Weidman J.F.,
RA Utterback T.R., Watthey L., McDonald L.A., Artiach P., Bowman C.,
RA Garland S.A., Fujii C., Cotton M.D., Horst K., Roberts K.M., Hatch B.,
RA Smith H.O., Venter J.C.;
RT "Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi.";
RL Nature 390:580-586(1997).
CC -!- FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate to
CC fructose 1,6-bisphosphate by ATP, the first committing step of
CC glycolysis. {ECO:0000255|HAMAP-Rule:MF_01981}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 1,6-
CC bisphosphate + H(+); Xref=Rhea:RHEA:16109, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:32966, ChEBI:CHEBI:57634,
CC ChEBI:CHEBI:456216; EC=2.7.1.11; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01981};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01981};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 3/4.
CC {ECO:0000255|HAMAP-Rule:MF_01981}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01981}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01981}.
CC -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) family.
CC PPi-dependent PFK group II subfamily. Atypical ATP-dependent clade 'X'
CC sub-subfamily. {ECO:0000255|HAMAP-Rule:MF_01981}.
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DR EMBL; AE000783; AAC67070.2; -; Genomic_DNA.
DR RefSeq; NP_212861.2; NC_001318.1.
DR RefSeq; WP_002656298.1; NC_001318.1.
DR AlphaFoldDB; O51669; -.
DR SMR; O51669; -.
DR STRING; 224326.BB_0727; -.
DR PRIDE; O51669; -.
DR EnsemblBacteria; AAC67070; AAC67070; BB_0727.
DR KEGG; bbu:BB_0727; -.
DR PATRIC; fig|224326.49.peg.1118; -.
DR HOGENOM; CLU_020655_7_4_12; -.
DR UniPathway; UPA00109; UER00182.
DR Proteomes; UP000001807; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:CAFA.
DR GO; GO:0003872; F:6-phosphofructokinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006002; P:fructose 6-phosphate metabolic process; IEA:InterPro.
DR HAMAP; MF_01981; Phosphofructokinase_II_X; 1.
DR InterPro; IPR022953; ATP_PFK.
DR InterPro; IPR000023; Phosphofructokinase_dom.
DR InterPro; IPR035966; PKF_sf.
DR InterPro; IPR012004; PyroP-dep_PFK_TP0108.
DR Pfam; PF00365; PFK; 1.
DR PIRSF; PIRSF000534; PPi_PFK_TP0108; 1.
DR PRINTS; PR00476; PHFRCTKINASE.
DR SUPFAM; SSF53784; SSF53784; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Glycolysis; Kinase; Magnesium; Metal-binding;
KW Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..447
FT /note="ATP-dependent 6-phosphofructokinase"
FT /id="PRO_0000429714"
FT ACT_SITE 210
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01981"
FT BINDING 88
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01981"
FT BINDING 154..155
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01981"
FT BINDING 179..182
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01981"
FT BINDING 180
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01981"
FT BINDING 208..210
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01981"
FT BINDING 253..255
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01981"
FT BINDING 315
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01981"
FT BINDING 368..371
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01981"
FT SITE 181
FT /note="Important for substrate specificity; cannot use PPi
FT as phosphoryl donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01981"
SQ SEQUENCE 447 AA; 49788 MW; C911BE4C19469402 CRC64;
MYRIKNENLD FKIDSLGECK QNNPLIDFYA SEGSSHFVNE KNKIKFSVYR NEDKGDRYED
VLLEKAGPRE KIYFVPRHVK AAITTCGGLC PGFNDVIRSI VRTLWKIYGV RNIYGVKFGY
QGLLPESNSP FINLNPDVVD DINKFGGTIL GSSRGGIKPV EIVDTLERMN INMIFNIGGD
GTQKGSLLIA EEIEKRNLKI AVVGIPKTVD NDFMFVQKSF GFETAVEQAV AAVAGAHFEA
NSAYNGIGLV KVMGRDSGFI AAHTALSSND VNFCLIPELD FDIEGPNGFL VHLERRLLEK
ESLEEIPHAV ILIAEGAGQK YFDHFPKKKD DSGNLLYEDI GLYIKDKITE YFKAKNIQFT
LKYIDPSYII RSSPANASDS LYCARLGSNA VHAAMAGKTK MLISLWSTKF VHIPIKMAVI
DRNKVNPNGS FWRDVLSSTG QPISMKN
