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Database: UniProt
Entry: G6B1J3_9BACT
LinkDB: G6B1J3_9BACT
Original site: G6B1J3_9BACT 
ID   G6B1J3_9BACT            Unreviewed;       549 AA.
AC   G6B1J3;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   24-JAN-2024, entry version 50.
DE   RecName: Full=Pyrophosphate--fructose 6-phosphate 1-phosphotransferase {ECO:0000256|HAMAP-Rule:MF_01980};
DE            EC=2.7.1.90 {ECO:0000256|HAMAP-Rule:MF_01980};
DE   AltName: Full=6-phosphofructokinase, pyrophosphate dependent {ECO:0000256|HAMAP-Rule:MF_01980};
DE   AltName: Full=PPi-dependent phosphofructokinase {ECO:0000256|HAMAP-Rule:MF_01980};
DE            Short=PPi-PFK {ECO:0000256|HAMAP-Rule:MF_01980};
DE   AltName: Full=Pyrophosphate-dependent 6-phosphofructose-1-kinase {ECO:0000256|HAMAP-Rule:MF_01980};
GN   Name=pfp {ECO:0000256|HAMAP-Rule:MF_01980};
GN   ORFNames=HMPREF0673_02764 {ECO:0000313|EMBL:EHJ36393.1};
OS   Leyella stercorea DSM 18206.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Leyella.
OX   NCBI_TaxID=1002367 {ECO:0000313|EMBL:EHJ36393.1, ECO:0000313|Proteomes:UP000004407};
RN   [1] {ECO:0000313|EMBL:EHJ36393.1, ECO:0000313|Proteomes:UP000004407}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18206 {ECO:0000313|EMBL:EHJ36393.1,
RC   ECO:0000313|Proteomes:UP000004407};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA   Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA   Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA   Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA   Chinwalla A., Mardis E.R., Wilson R.K.;
RL   Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate, the
CC       first committing step of glycolysis. Uses inorganic phosphate (PPi) as
CC       phosphoryl donor instead of ATP like common ATP-dependent
CC       phosphofructokinases (ATP-PFKs), which renders the reaction reversible,
CC       and can thus function both in glycolysis and gluconeogenesis.
CC       Consistently, PPi-PFK can replace the enzymes of both the forward (ATP-
CC       PFK) and reverse (fructose-bisphosphatase (FBPase)) reactions.
CC       {ECO:0000256|ARBA:ARBA00003138, ECO:0000256|HAMAP-Rule:MF_01980}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=beta-D-fructose 6-phosphate + diphosphate = beta-D-fructose
CC         1,6-bisphosphate + H(+) + phosphate; Xref=Rhea:RHEA:13613,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:32966, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57634; EC=2.7.1.90;
CC         Evidence={ECO:0000256|ARBA:ARBA00000628, ECO:0000256|HAMAP-
CC         Rule:MF_01980};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946,
CC         ECO:0000256|HAMAP-Rule:MF_01980};
CC   -!- ACTIVITY REGULATION: Non-allosteric. {ECO:0000256|HAMAP-Rule:MF_01980}.
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_01980}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01980}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01980}.
CC   -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) family.
CC       PPi-dependent PFK group II subfamily. Clade 'Long' sub-subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_01980}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_01980}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EHJ36393.1}.
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DR   EMBL; AFZZ01000246; EHJ36393.1; -; Genomic_DNA.
DR   RefSeq; WP_007902847.1; NZ_JH379469.1.
DR   AlphaFoldDB; G6B1J3; -.
DR   GeneID; 78338155; -.
DR   PATRIC; fig|1002367.3.peg.2231; -.
DR   eggNOG; COG0205; Bacteria.
DR   HOGENOM; CLU_022288_0_1_10; -.
DR   UniPathway; UPA00109; UER00182.
DR   Proteomes; UP000004407; Unassembled WGS sequence.
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:InterPro.
DR   GO; GO:0047334; F:diphosphate-fructose-6-phosphate 1-phosphotransferase activity; IEA:UniProtKB-EC.
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   Gene3D; 3.40.50.460; Phosphofructokinase domain; 1.
DR   HAMAP; MF_01980; Phosphofructokinase_II_Long; 1.
DR   InterPro; IPR022953; ATP_PFK.
DR   InterPro; IPR011183; PfpB_PPi_PFK.
DR   InterPro; IPR000023; Phosphofructokinase_dom.
DR   InterPro; IPR035966; PKF_sf.
DR   NCBIfam; TIGR02477; PFKA_PPi; 1.
DR   PANTHER; PTHR43650; PYROPHOSPHATE--FRUCTOSE 6-PHOSPHATE 1-PHOSPHOTRANSFERASE; 1.
DR   PANTHER; PTHR43650:SF1; PYROPHOSPHATE--FRUCTOSE 6-PHOSPHATE 1-PHOSPHOTRANSFERASE SUBUNIT BETA 2; 1.
DR   Pfam; PF00365; PFK; 1.
DR   PIRSF; PIRSF005677; PPi_PFK_PfpB; 1.
DR   PRINTS; PR00476; PHFRCTKINASE.
DR   SUPFAM; SSF53784; Phosphofructokinase; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01980};
KW   Glycolysis {ECO:0000256|HAMAP-Rule:MF_01980};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_01980};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01980};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_01980};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_01980}.
FT   DOMAIN          69..322
FT                   /note="Phosphofructokinase"
FT                   /evidence="ECO:0000259|Pfam:PF00365"
FT   ACT_SITE        201
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01980"
FT   BINDING         77
FT                   /ligand="diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:33019"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01980"
FT   BINDING         171
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01980"
FT   BINDING         199..201
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01980"
FT   BINDING         238..239
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01980"
FT   BINDING         246..248
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01980"
FT   BINDING         307
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01980"
FT   BINDING         422..425
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01980"
FT   SITE            172
FT                   /note="Important for catalytic activity and substrate
FT                   specificity; stabilizes the transition state when the
FT                   phosphoryl donor is PPi; prevents ATP from binding by
FT                   mimicking the alpha-phosphate group of ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01980"
FT   SITE            198
FT                   /note="Important for catalytic activity; stabilizes the
FT                   transition state when the phosphoryl donor is PPi"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01980"
SQ   SEQUENCE   549 AA;  60082 MW;  0E92340875369A9E CRC64;
     MEISALQIAR AAYQPKLPKA LQGPVKAVEG EATQSVGNQE EIKALFPNTY GMPVITFEAG
     EKTELPAFNV GVILSGGQAP GGHNVISGLF DGVKSLNPEN KLYGFILGPG GLVDHKYIEI
     TSELMDQYRN TGGFDIIGSG RTKLEKEEQF EKGIEILREL GIKALVIIGG DDSNTNACVL
     AEYYAAKKYG VQVIGCPKTI DGDLKNEQIE TSFGFDTACK TYSELIGNIQ RDCNSARKYW
     HFIKLMGRSA SHIALECALQ TQPNICLVSE EVEAKEMSLD DVVTYIAQAV ADRAADGNNF
     GTVLIPEGLI EFIPAIKKLI AELNEVLTDP ATGESREFAN AEEQIAFVKS SIAKENLAVL
     ESLPADVARQ LCLDRDPHGN VQVSLIETEK LLSRMVATKL NAWKAEGKFC GKFSAQHHFF
     GYEGRCAAPS NYDADYCYSL GFNASRLISN GKTGYMSIIQ NTTAPAEQWI AGGVPITMMM
     NIERRNGANK PVIRKALVEL DGAPFKFFAA HREEWAKNTC YVYPGPIQYW GPTEVCDQTT
     KTLKLEQAK
//
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