ID   A0A2G5ZJ77_9BACL        Unreviewed;       319 AA.
AC   A0A2G5ZJ77;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   29-SEP-2021, entry version 16.
DE   RecName: Full=ATP-dependent 6-phosphofructokinase {ECO:0000256|HAMAP-Rule:MF_00339};
DE            Short=ATP-PFK {ECO:0000256|HAMAP-Rule:MF_00339};
DE            Short=Phosphofructokinase {ECO:0000256|HAMAP-Rule:MF_00339};
DE            EC=2.7.1.11 {ECO:0000256|HAMAP-Rule:MF_00339};
DE   AltName: Full=Phosphohexokinase {ECO:0000256|HAMAP-Rule:MF_00339};
GN   Name=pfkA {ECO:0000256|HAMAP-Rule:MF_00339,
GN   ECO:0000313|EMBL:PID00772.1};
GN   ORFNames=CSV68_00695 {ECO:0000313|EMBL:PID00772.1};
OS   Sporosarcina sp. P29.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Planococcaceae; Sporosarcina;
OC   unclassified Sporosarcina.
OX   NCBI_TaxID=2048252 {ECO:0000313|EMBL:PID00772.1, ECO:0000313|Proteomes:UP000229790};
RN   [1] {ECO:0000313|EMBL:PID00772.1, ECO:0000313|Proteomes:UP000229790}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P29 {ECO:0000313|EMBL:PID00772.1,
RC   ECO:0000313|Proteomes:UP000229790};
RA   Oliver A., Kay M., Cooper K.;
RT   "Comparative genomics and methylomics between geographically and
RT   phenotypically diverse Sporosarcina species.";
RL   Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00002659, ECO:0000256|HAMAP-
CC       Rule:MF_00339}.
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_00339};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946,
CC         ECO:0000256|HAMAP-Rule:MF_00339};
CC   -!- ACTIVITY REGULATION: Allosterically activated by ADP and other
CC       diphosphonucleosides, and allosterically inhibited by
CC       phosphoenolpyruvate. {ECO:0000256|HAMAP-Rule:MF_00339}.
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_00339}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00339}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|HAMAP-Rule:MF_00339}.
CC   -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) family.
CC       ATP-dependent PFK group I subfamily. Prokaryotic clade 'B1' sub-
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_00339}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00339}.
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:PID00772.1}.
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DR   EMBL; PDYX01000001; PID00772.1; -; Genomic_DNA.
DR   EnsemblBacteria; PID00772; PID00772; CSV68_00695.
DR   UniPathway; UPA00109; UER00182.
DR   Proteomes; UP000229790; 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: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; 3.40.50.460; -; 1.
DR   HAMAP; MF_00339; Phosphofructokinase_I_B1; 1.
DR   InterPro; IPR022953; ATP_PFK.
DR   InterPro; IPR012003; ATP_PFK_prok-type.
DR   InterPro; IPR012828; PFKA_ATP_prok.
DR   InterPro; IPR015912; Phosphofructokinase_CS.
DR   InterPro; IPR000023; Phosphofructokinase_dom.
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; TIGR02482; PFKA_ATP; 1.
DR   PROSITE; PS00433; PHOSPHOFRUCTOKINASE; 1.
PE   3: Inferred from homology;
KW   Allosteric enzyme {ECO:0000256|ARBA:ARBA00022533, ECO:0000256|HAMAP-
KW   Rule:MF_00339};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00339};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00339};
KW   Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|HAMAP-
KW   Rule:MF_00339};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_00339};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00339};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_00339};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00339};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00339}.
FT   DOMAIN          3..274
FT                   /note="PFK"
FT                   /evidence="ECO:0000259|Pfam:PF00365"
FT   NP_BIND         72..73
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00339"
FT   NP_BIND         102..105
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00339"
FT   REGION          21..25
FT                   /note="ADP binding; allosteric activator; shared with
FT                   dimeric partner"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00339"
FT   REGION          125..127
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00339"
FT   REGION          169..171
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00339"
FT   REGION          185..187
FT                   /note="ADP binding; allosteric activator"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00339"
FT   REGION          213..215
FT                   /note="ADP binding; allosteric activator"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00339"
FT   REGION          249..252
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00339"
FT   ACT_SITE        127
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00339"
FT   METAL           103
FT                   /note="Magnesium; catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00339"
FT   BINDING         11
FT                   /note="ATP; via amide nitrogen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00339"
FT   BINDING         154
FT                   /note="ADP; allosteric activator"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00339"
FT   BINDING         162
FT                   /note="Substrate; shared with dimeric partner"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00339"
FT   BINDING         211
FT                   /note="ADP; allosteric activator"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00339"
FT   BINDING         222
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00339"
FT   BINDING         243
FT                   /note="Substrate; shared with dimeric partner"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00339"
SQ   SEQUENCE   319 AA;  34012 MW;  624832D78EBC7E0A CRC64;
     MKKIAVLTSG GDAPGMNAAI RSVVRKALFE GVEVSGVFNG YQGLIDGRIE QFQLGSVGDI
     IQRGGTILRS ARCPEFMTEE GRAKAMEQIK LHAIEGLVVI GGDGSFKGAN ELVKLGVPCA
     CVPATIDNDI TGTEFTIGFD TALNTVVEVI DKIRDTATSH ERSFIIEVMG RDAGDLALWA
     GLGGGAESII LPEKPFDVNS IVDRLKSSTS RGKKHSIIVL AEGMMSATQL AAILKEEAGV
     ETRVSILGHM QRGGSPSARD RVIASQYGAR AVETLLSGKK SSAVGMRNHK VVDYNLEEVF
     IKREQLDLSL LDLAETLSI
//