ID   A0A641ARF4_9ACTN        Unreviewed;       342 AA.
AC   A0A641ARF4;
DT   22-APR-2020, integrated into UniProtKB/TrEMBL.
DT   22-APR-2020, sequence version 1.
DT   02-JUN-2021, entry version 6.
DE   RecName: Full=Pyrophosphate--fructose 6-phosphate 1-phosphotransferase {ECO:0000256|HAMAP-Rule:MF_01976};
DE            EC=2.7.1.90 {ECO:0000256|HAMAP-Rule:MF_01976};
DE   AltName: Full=6-phosphofructokinase, pyrophosphate dependent {ECO:0000256|HAMAP-Rule:MF_01976};
DE   AltName: Full=PPi-dependent phosphofructokinase {ECO:0000256|HAMAP-Rule:MF_01976};
DE            Short=PPi-PFK {ECO:0000256|HAMAP-Rule:MF_01976};
DE   AltName: Full=Pyrophosphate-dependent 6-phosphofructose-1-kinase {ECO:0000256|HAMAP-Rule:MF_01976};
GN   Name=pfp {ECO:0000256|HAMAP-Rule:MF_01976};
GN   ORFNames=ESP62_010005 {ECO:0000313|EMBL:KAA1378662.1};
OS   Aeromicrobium fastidiosum.
OC   Bacteria; Actinobacteria; Propionibacteriales; Nocardioidaceae;
OC   Aeromicrobium.
OX   NCBI_TaxID=52699 {ECO:0000313|EMBL:KAA1378662.1};
RN   [1] {ECO:0000313|EMBL:KAA1378662.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NRBC 14897 {ECO:0000313|EMBL:KAA1378662.1};
RA   Li J.;
RL   Submitted (SEP-2019) 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|HAMAP-Rule:MF_01976}.
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|HAMAP-Rule:MF_01976};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946,
CC         ECO:0000256|HAMAP-Rule:MF_01976};
CC   -!- ACTIVITY REGULATION: Non-allosteric. {ECO:0000256|HAMAP-Rule:MF_01976}.
CC   -!- PATHWAY: Carbohydrate degradation. {ECO:0000256|ARBA:ARBA00004921}.
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC       phosphate and glycerone phosphate from D-glucose: step 3/4.
CC       {ECO:0000256|ARBA:ARBA00004679, ECO:0000256|HAMAP-Rule:MF_01976}.
CC   -!- SUBUNIT: Homodimer or homotetramer. {ECO:0000256|HAMAP-Rule:MF_01976}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|HAMAP-Rule:MF_01976}.
CC   -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) family.
CC       Mixed-substrate PFK group III subfamily. {ECO:0000256|HAMAP-
CC       Rule:MF_01976}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_01976}.
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:KAA1378662.1}.
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DR   EMBL; SDPP02000002; KAA1378662.1; -; Genomic_DNA.
DR   UniPathway; UPA00109; UER00182.
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   HAMAP; MF_01976; Phosphofructokinase_III; 1.
DR   InterPro; IPR022953; ATP_PFK.
DR   InterPro; IPR012003; ATP_PFK_prok-type.
DR   InterPro; IPR000023; Phosphofructokinase_dom.
DR   InterPro; IPR012829; Phosphofructokinase_III.
DR   InterPro; IPR035966; PKF_sf.
DR   Pfam; PF00365; PFK; 1.
DR   PIRSF; PIRSF000532; ATP_PFK_prok; 1.
DR   PRINTS; PR00476; PHFRCTKINASE.
DR   SUPFAM; SSF53784; SSF53784; 1.
DR   TIGRFAMs; TIGR02483; PFK_mixed; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01976};
KW   Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|HAMAP-
KW   Rule:MF_01976};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_01976};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01976};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_01976};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_01976}.
FT   DOMAIN          2..297
FT                   /note="PFK"
FT                   /evidence="ECO:0000259|Pfam:PF00365"
FT   REGION          125..127
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01976"
FT   REGION          169..171
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01976"
FT   REGION          272..275
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01976"
FT   ACT_SITE        127
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01976"
FT   METAL           103
FT                   /note="Magnesium; catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01976"
FT   BINDING         10
FT                   /note="Diphosphate; via amide nitrogen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01976"
FT   BINDING         162
FT                   /note="Substrate; shared with dimeric partner"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01976"
FT   BINDING         221
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01976"
FT   BINDING         266
FT                   /note="Substrate; shared with dimeric partner"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01976"
FT   SITE            104
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_01976"
FT   SITE            124
FT                   /note="Important for catalytic activity; stabilizes the
FT                   transition state when the phosphoryl donor is PPi"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01976"
SQ   SEQUENCE   342 AA;  36468 MW;  B1DCACDBA0250605 CRC64;
     MRVGMLTGGG DCPGLNAVIR AAVRKGVQQY RHEFIGFRDG WRGPLEDDTM TLGVDEVRGI
     LPRGGTILGS SRTNPFAIDD GVQRIKDNLD RNGCDALIAI GGEDTLGVAT KLADLGVAVV
     GVPKTIDNDL SGTDFTFGFD TAVNIATEAI DRLHTTAESH HRVLVVEVMG RHAGWIALHS
     GLAGGANIIL IPERPFDIEQ VCAQVESRFA THYAPIIVVS EGAVPAEGGD MSLVSGQKDA
     FGHVRLGGIG DRLASEIEHR TGKEARAVVL GHVQRGGSPT AFDRWLATRF GLHAITAVHE
     GDFGTMMSLR GTEIARVPLA DGTEKLKTVR ADLYEEAEVF FG
//