ID A0A089RVF0_9LACO Unreviewed; 320 AA.
AC A0A089RVF0;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 59.
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:AIR10567.1};
GN ORFNames=A8C52_07545 {ECO:0000313|EMBL:PAY46762.1}, B5G36_08105
GN {ECO:0000313|EMBL:OUN17926.1}, B6U37_04700
GN {ECO:0000313|EMBL:OQR25487.1}, B6U60_03850
GN {ECO:0000313|EMBL:OQQ84443.1}, B7R82_04650
GN {ECO:0000313|EMBL:ARU19315.1}, DB362_03635
GN {ECO:0000313|EMBL:PWG53017.1}, FGO86_01985
GN {ECO:0000313|EMBL:TXJ84743.1}, FYL24_08645
GN {ECO:0000313|EMBL:MYY75602.1}, GKC33_09455
GN {ECO:0000313|EMBL:MSE08909.1}, HRD59_01920
GN {ECO:0000313|EMBL:NRD04208.1}, LSJ_0886 {ECO:0000313|EMBL:AIR10567.1};
OS Ligilactobacillus salivarius.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Ligilactobacillus.
OX NCBI_TaxID=1624 {ECO:0000313|EMBL:AIR10567.1, ECO:0000313|Proteomes:UP000029488};
RN [1] {ECO:0000313|EMBL:AIR10567.1, ECO:0000313|Proteomes:UP000029488}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM1046 {ECO:0000313|EMBL:AIR10567.1,
RC ECO:0000313|Proteomes:UP000029488};
RX PubMed=25201645; DOI=10.1186/1471-2164-15-771;
RA Raftis E.J., Forde B.M., Claesson M.J., O'Toole P.W.;
RT "Unusual genome complexity in Lactobacillus salivarius JCM1046.";
RL BMC Genomics 15:771-771(2014).
RN [2] {ECO:0000313|EMBL:PAY46762.1, ECO:0000313|Proteomes:UP000218139}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KLA006 {ECO:0000313|EMBL:PAY46762.1,
RC ECO:0000313|Proteomes:UP000218139};
RA Lee J.-Y., Kim E.B., Choi Y.-J.;
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000192353, ECO:0000313|Proteomes:UP000192638}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AH4231 {ECO:0000313|EMBL:OQR25487.1,
RC ECO:0000313|Proteomes:UP000192353}, and LMG 14477
RC {ECO:0000313|EMBL:OQQ84443.1, ECO:0000313|Proteomes:UP000192638};
RA Harris H.M.;
RT "Phylogenomics and comparative genomics of Lactobacillus salivarius, a
RT mammalian gut commensal.";
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:ARU19315.1, ECO:0000313|Proteomes:UP000195378}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZLS006 {ECO:0000313|EMBL:ARU19315.1,
RC ECO:0000313|Proteomes:UP000195378};
RA Zhang D.;
RT "Complete genome sequence of Lactobacillus salivarius ZLS006, a probiotic
RT strain isolated from healthy piglet.";
RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000313|Proteomes:UP000196255}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=An84 {ECO:0000313|Proteomes:UP000196255};
RA Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA Rychlik I.;
RT "Function of individual gut microbiota members based on whole genome
RT sequencing of pure cultures obtained from chicken caecum.";
RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
RN [6] {ECO:0000313|EMBL:OUN17926.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=An84 {ECO:0000313|EMBL:OUN17926.1};
RX PubMed=30064352;
RA Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA Rychlik I.;
RT "Whole genome sequencing and function prediction of 133 gut anaerobes
RT isolated from chicken caecum in pure cultures.";
RL BMC Genomics 19:0-561(2018).
RN [7] {ECO:0000313|EMBL:PWG53017.1, ECO:0000313|Proteomes:UP000245607}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A3iob {ECO:0000313|EMBL:PWG53017.1,
RC ECO:0000313|Proteomes:UP000245607};
RA Audisio C., Albarracin L., Torres M.J., Hebert E.M., Saavedra L.;
RT "Lactobacillus salivarius genome sequencing and assembly.";
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
RN [8] {ECO:0000313|EMBL:TXJ84743.1, ECO:0000313|Proteomes:UP000321271}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C2 {ECO:0000313|EMBL:TXJ84743.1,
RC ECO:0000313|Proteomes:UP000321271};
RX PubMed=31417502; DOI=.3389/fmicb.2019.01663;
RA Bravo M., Combes T., Martinez F.O., Cerrato R., Rey J., Garcia-Jimenez W.,
RA Fernandez-Llario P., Risco D., Gutierrez-Merino J.;
RT "Lactobacilli Isolated From Wild Boar (Sus scrofa) Antagonize Mycobacterium
RT bovis Bacille Calmette-Guerin (BCG) in a Species-Dependent Manner.";
RL Front. Microbiol. 10:1663-1663(2019).
RN [9] {ECO:0000313|EMBL:MSE08909.1, ECO:0000313|Proteomes:UP000467635}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VRA_01-1sq_f {ECO:0000313|EMBL:MSE08909.1,
RC ECO:0000313|Proteomes:UP000467635};
RA Vasilyev I.Y., Radchenko V., Ilnitskaya E.V.;
RT "Draft Genome Sequence of Plant Growth-Promoting Rhizosphere-Associated
RT Bacteria.";
RL Submitted (NOV-2019) to the EMBL/GenBank/DDBJ databases.
RN [10] {ECO:0000313|EMBL:MYY75602.1, ECO:0000313|Proteomes:UP000471466}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FZJTZ69_1 {ECO:0000313|EMBL:MYY75602.1,
RC ECO:0000313|Proteomes:UP000471466};
RX PubMed=31915776; DOI=10.1039/c9fo02116g;
RA Zhai Q., Shen X., Cen S., Zhang C., Tian F., Zhao J., Zhang H., Xue Y.,
RA Chen W.;
RT "Screening of Lactobacillus salivarius strains from the feces of Chinese
RT populations and the evaluation of their effects against intestinal
RT inflammation in mice.";
RL Food Funct. 11:221-235(2020).
RN [11] {ECO:0000313|EMBL:NRD04208.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=BIO6313 {ECO:0000313|EMBL:NRD04208.1};
RA Jaomanjaka F.;
RT "Investigation of probiotic properties of different lactic acid bacteria.";
RL Submitted (MAY-2020) 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|HAMAP-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}.
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DR EMBL; CP007646; AIR10567.1; -; Genomic_DNA.
DR EMBL; CP020858; ARU19315.1; -; Genomic_DNA.
DR EMBL; WKKX01000498; MSE08909.1; -; Genomic_DNA.
DR EMBL; VSTS01000010; MYY75602.1; -; Genomic_DNA.
DR EMBL; JABRBP010000001; NRD04208.1; -; Genomic_DNA.
DR EMBL; NBEB01000040; OQQ84443.1; -; Genomic_DNA.
DR EMBL; NBEY01000039; OQR25487.1; -; Genomic_DNA.
DR EMBL; NFHF01000020; OUN17926.1; -; Genomic_DNA.
DR EMBL; LXZO01000087; PAY46762.1; -; Genomic_DNA.
DR EMBL; QFAS01000005; PWG53017.1; -; Genomic_DNA.
DR EMBL; VCMO01000001; TXJ84743.1; -; Genomic_DNA.
DR RefSeq; WP_003700206.1; NZ_VSWB01000001.1.
DR SMR; A0A089RVF0; -.
DR GeneID; 69724054; -.
DR KEGG; lsj:LSJ_0886; -.
DR OMA; KFAVICV; -.
DR UniPathway; UPA00109; UER00182.
DR Proteomes; UP000029488; Chromosome.
DR Proteomes; UP000192353; Unassembled WGS sequence.
DR Proteomes; UP000192638; Unassembled WGS sequence.
DR Proteomes; UP000195378; Chromosome.
DR Proteomes; UP000196255; Unassembled WGS sequence.
DR Proteomes; UP000218139; Unassembled WGS sequence.
DR Proteomes; UP000245607; Unassembled WGS sequence.
DR Proteomes; UP000321271; Unassembled WGS sequence.
DR Proteomes; UP000467635; Unassembled WGS sequence.
DR Proteomes; UP000471466; Unassembled WGS sequence.
DR Proteomes; UP000606766; 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; 3.40.50.450; -; 1.
DR Gene3D; 3.40.50.460; Phosphofructokinase domain; 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 NCBIfam; TIGR02482; PFKA_ATP; 1.
DR PANTHER; PTHR13697:SF4; ATP-DEPENDENT 6-PHOSPHOFRUCTOKINASE; 1.
DR PANTHER; PTHR13697; PHOSPHOFRUCTOKINASE; 1.
DR Pfam; PF00365; PFK; 1.
DR PIRSF; PIRSF000532; ATP_PFK_prok; 1.
DR PRINTS; PR00476; PHFRCTKINASE.
DR SUPFAM; SSF53784; Phosphofructokinase; 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="Phosphofructokinase"
FT /evidence="ECO:0000259|Pfam:PF00365"
FT ACT_SITE 127
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00339"
FT BINDING 11
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00339"
FT BINDING 21..25
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /ligand_note="allosteric activator; ligand shared between
FT dimeric partners"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00339"
FT BINDING 72..73
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00339"
FT BINDING 102..105
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00339"
FT BINDING 103
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00339"
FT BINDING 125..127
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00339"
FT BINDING 162
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00339"
FT BINDING 169..171
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00339"
FT BINDING 185..187
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /ligand_note="allosteric activator; ligand shared between
FT dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00339"
FT BINDING 213..215
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /ligand_note="allosteric activator; ligand shared between
FT dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00339"
FT BINDING 222
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00339"
FT BINDING 243
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00339"
FT BINDING 249..252
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00339"
SQ SEQUENCE 320 AA; 34435 MW; 27F4CDEADB2E191C CRC64;
MKRIGILTSG GDAAGMNAAV RAIARSAMNA GLEAYGINYG YKGLVEGNIF KMESTKLDEI
INRGGTILYS ARFPEFAETE TQLKGIEQLK KFGIEALVVI GGDGSYHGAE KLTMHGYNSI
GVPGTIDNDI PGTDFTIGFD TAANVAMEAL DRINDTATSH QRVFVVEVMG RGAGDIALWS
GIATGADAIV IPEREYDIEA IANKISENRK NGKDHGLIVL AEGVMGAAEF KEKLDQYGDF
DSRAITLGHI QRGGNPTVKD RVLATRLGDY AIRLLLEGKG GLAIGIHDNQ LVATDIIDTL
ENHKHQTDVS LQDLNDRVRF
//
