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Database: UniProt
Entry: Q0SMC9_BORAP
LinkDB: Q0SMC9_BORAP
Original site: Q0SMC9_BORAP 
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
//
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