ID Q0SMC9_BORAP Unreviewed; 447 AA.
AC Q0SMC9;
DT 05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2006, sequence version 1.
DT 24-JAN-2024, entry version 116.
DE RecName: Full=ATP-dependent 6-phosphofructokinase {ECO:0000256|HAMAP-Rule:MF_01981};
DE Short=ATP-PFK {ECO:0000256|HAMAP-Rule:MF_01981};
DE Short=Phosphofructokinase {ECO:0000256|HAMAP-Rule:MF_01981};
DE EC=2.7.1.11 {ECO:0000256|HAMAP-Rule:MF_01981};
DE AltName: Full=Phosphohexokinase {ECO:0000256|HAMAP-Rule:MF_01981};
GN Name=pfk6 {ECO:0000313|EMBL:AEL69944.1};
GN Synonyms=pfkA {ECO:0000256|HAMAP-Rule:MF_01981};
GN OrderedLocusNames=BafPKo_0751 {ECO:0000313|EMBL:AEL69944.1};
OS Borreliella afzelii (strain PKo) (Borrelia afzelii).
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Borreliaceae;
OC Borreliella.
OX NCBI_TaxID=390236 {ECO:0000313|EMBL:AEL69944.1, ECO:0000313|Proteomes:UP000005216};
RN [1] {ECO:0000313|EMBL:AEL69944.1, ECO:0000313|Proteomes:UP000005216}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PKo {ECO:0000313|EMBL:AEL69944.1,
RC ECO:0000313|Proteomes:UP000005216};
RX PubMed=22123755; DOI=10.1128/JB.05951-11;
RA Casjens S.R., Mongodin E.F., Qiu W.-G., Dunn J.J., Luft B.J.,
RA Fraser-Liggett C.M., Schutzer S.E.;
RT "Whole-genome sequences of two Borrelia afzelii and two Borrelia garinii
RT Lyme disease agent isolates.";
RL J. Bacteriol. 193:6995-6996(2011).
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:0000256|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;
CC Evidence={ECO:0000256|ARBA:ARBA00000432, ECO:0000256|HAMAP-
CC Rule:MF_01981};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC ECO:0000256|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:0000256|HAMAP-Rule:MF_01981}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01981}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|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:0000256|HAMAP-Rule:MF_01981}.
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DR EMBL; CP002933; AEL69944.1; -; Genomic_DNA.
DR AlphaFoldDB; Q0SMC9; -.
DR STRING; 29518.BLA32_00595; -.
DR KEGG; bafz:BafPKo_0751; -.
DR PATRIC; fig|390236.22.peg.717; -.
DR eggNOG; COG0205; Bacteria.
DR HOGENOM; CLU_020655_7_4_12; -.
DR OMA; YGHERFA; -.
DR OrthoDB; 9802503at2; -.
DR UniPathway; UPA00109; UER00182.
DR Proteomes; UP000005216; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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 Gene3D; 3.40.50.450; -; 1.
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 PANTHER; PTHR45770; ATP-DEPENDENT 6-PHOSPHOFRUCTOKINASE 1; 1.
DR PANTHER; PTHR45770:SF11; ATP-DEPENDENT 6-PHOSPHOFRUCTOKINASE 1; 1.
DR Pfam; PF00365; PFK; 1.
DR PIRSF; PIRSF000534; PPi_PFK_TP0108; 1.
DR PRINTS; PR00476; PHFRCTKINASE.
DR SUPFAM; SSF53784; Phosphofructokinase; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_01981};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01981};
KW Glycolysis {ECO:0000256|HAMAP-Rule:MF_01981};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_01981};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01981};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01981}; Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01981};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01981}.
FT DOMAIN 81..393
FT /note="Phosphofructokinase"
FT /evidence="ECO:0000259|Pfam:PF00365"
FT ACT_SITE 210
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01981"
FT BINDING 88
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01981"
FT BINDING 154..155
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01981"
FT BINDING 179..182
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01981"
FT BINDING 180
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01981"
FT BINDING 208..210
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01981"
FT BINDING 253..255
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01981"
FT BINDING 315
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01981"
FT BINDING 368..371
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01981"
FT SITE 181
FT /note="Important for substrate specificity; cannot use PPi
FT as phosphoryl donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01981"
SQ SEQUENCE 447 AA; 49805 MW; 05FE843CECC3BF23 CRC64;
MYRIKNENLD FKIDSLGECK QNNPLIDFYA SEGSSHFVNE KNKIKFSVYR NEDEGDKYED
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 YFDHFPRKKD DSGNLLYEDI GLYIKDKITE YFKAKNIQFT
LKYIDPSYII RSSPANASDS LYCARLGSNA VHAAMSGKTK MLISLWSTKF VHIPIKMAVI
DRNKVNPNGS FWRDVLSSTG QPISMKN
//