PFKA_BACSU
ID PFKA_BACSU Reviewed; 319 AA.
AC O34529;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=ATP-dependent 6-phosphofructokinase {ECO:0000255|HAMAP-Rule:MF_00339};
DE Short=ATP-PFK {ECO:0000255|HAMAP-Rule:MF_00339};
DE Short=Phosphofructokinase {ECO:0000255|HAMAP-Rule:MF_00339};
DE EC=2.7.1.11 {ECO:0000255|HAMAP-Rule:MF_00339};
DE AltName: Full=Phosphohexokinase {ECO:0000255|HAMAP-Rule:MF_00339};
GN Name=pfkA {ECO:0000255|HAMAP-Rule:MF_00339}; Synonyms=pfk;
GN OrderedLocusNames=BSU29190;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9387221; DOI=10.1099/00221287-143-11-3431;
RA Lapidus A., Galleron N., Sorokin A., Ehrlich S.D.;
RT "Sequencing and functional annotation of the Bacillus subtilis genes in the
RT 200 kb rrnB-dnaB region.";
RL Microbiology 143:3431-3441(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP SUBUNIT.
RC STRAIN=168;
RX PubMed=19193632; DOI=10.1074/mcp.m800546-mcp200;
RA Commichau F.M., Rothe F.M., Herzberg C., Wagner E., Hellwig D.,
RA Lehnik-Habrink M., Hammer E., Volker U., Stulke J.;
RT "Novel activities of glycolytic enzymes in Bacillus subtilis: interactions
RT with essential proteins involved in mRNA processing.";
RL Mol. Cell. Proteomics 8:1350-1360(2009).
RN [4]
RP INTERACTION WITH RNY, AND SUBUNIT.
RC STRAIN=168;
RX PubMed=21803996; DOI=10.1128/jb.05500-11;
RA Lehnik-Habrink M., Newman J., Rothe F.M., Solovyova A.S., Rodrigues C.,
RA Herzberg C., Commichau F.M., Lewis R.J., Stulke J.;
RT "RNase Y in Bacillus subtilis: a natively disordered protein that is the
RT functional equivalent of RNase E from Escherichia coli.";
RL J. Bacteriol. 193:5431-5441(2011).
RN [5]
RP INTERACTION WITH BRXC, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=168 / CU1065 {ECO:0000303|PubMed:33722570};
RX PubMed=33722570; DOI=10.1016/j.redox.2021.101935;
RA Gaballa A., Su T.T., Helmann J.D.;
RT "The Bacillus subtilis monothiol bacilliredoxin BrxC (YtxJ) and the Bdr
RT (YpdA) disulfide reductase reduce S-bacillithiolated proteins.";
RL Redox Biol. 42:101935-101935(2021).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS), INTERACTION WITH ENO, AND SUBUNIT.
RC STRAIN=168;
RX PubMed=22198292; DOI=10.1016/j.jmb.2011.12.024;
RA Newman J.A., Hewitt L., Rodrigues C., Solovyova A.S., Harwood C.R.,
RA Lewis R.J.;
RT "Dissection of the network of interactions that links RNA processing with
RT glycolysis in the Bacillus subtilis degradosome.";
RL J. Mol. Biol. 416:121-136(2012).
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:0000255|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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00339};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00339};
CC -!- ACTIVITY REGULATION: Allosterically activated by ADP and other
CC diphosphonucleosides, and allosterically inhibited by
CC phosphoenolpyruvate. {ECO:0000255|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:0000255|HAMAP-Rule:MF_00339}.
CC -!- SUBUNIT: Homotetramer. Component of a possible RNA degradosome complex
CC composed of rny, rnjA, rnjB, pnp, pfkA and eno (PubMed:19193632)
CC (although rnjA and rnjB's presence is unclear). Specifically interacts
CC with RNase Y (rny, PubMed:21803996) and enolase (eno, PubMed:22198292).
CC Interacts with BrxC (PubMed:33722570). {ECO:0000255|HAMAP-
CC Rule:MF_00339, ECO:0000269|PubMed:19193632,
CC ECO:0000269|PubMed:21803996, ECO:0000269|PubMed:22198292,
CC ECO:0000269|PubMed:33722570}.
CC -!- INTERACTION:
CC O34529; O31774: rny; NbExp=2; IntAct=EBI-5250040, EBI-6415578;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|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:0000255|HAMAP-Rule:MF_00339}.
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DR EMBL; AF008220; AAC00342.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14879.1; -; Genomic_DNA.
DR PIR; A69675; A69675.
DR RefSeq; NP_390797.1; NC_000964.3.
DR RefSeq; WP_003229420.1; NZ_JNCM01000036.1.
DR PDB; 4A3S; X-ray; 2.30 A; A/B=1-319.
DR PDBsum; 4A3S; -.
DR AlphaFoldDB; O34529; -.
DR SMR; O34529; -.
DR IntAct; O34529; 4.
DR MINT; O34529; -.
DR STRING; 224308.BSU29190; -.
DR jPOST; O34529; -.
DR PaxDb; O34529; -.
DR PRIDE; O34529; -.
DR EnsemblBacteria; CAB14879; CAB14879; BSU_29190.
DR GeneID; 937376; -.
DR KEGG; bsu:BSU29190; -.
DR PATRIC; fig|224308.179.peg.3169; -.
DR eggNOG; COG0205; Bacteria.
DR InParanoid; O34529; -.
DR OMA; KFAVICV; -.
DR PhylomeDB; O34529; -.
DR BioCyc; BSUB:BSU29190-MON; -.
DR SABIO-RK; O34529; -.
DR UniPathway; UPA00109; UER00182.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005945; C:6-phosphofructokinase complex; IBA:GO_Central.
DR GO; GO:0003872; F:6-phosphofructokinase activity; IBA:GO_Central.
DR GO; GO:0016208; F:AMP binding; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0070095; F:fructose-6-phosphate binding; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0048029; F:monosaccharide binding; IBA:GO_Central.
DR GO; GO:0061621; P:canonical glycolysis; IBA:GO_Central.
DR GO; GO:0030388; P:fructose 1,6-bisphosphate metabolic process; IBA:GO_Central.
DR GO; GO:0006002; P:fructose 6-phosphate metabolic process; IBA:GO_Central.
DR CDD; cd00763; Bacterial_PFK; 1.
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 1: Evidence at protein level;
KW 3D-structure; Allosteric enzyme; ATP-binding; Cytoplasm; Glycolysis;
KW Kinase; Magnesium; Metal-binding; Nucleotide-binding; Reference proteome;
KW Transferase.
FT CHAIN 1..319
FT /note="ATP-dependent 6-phosphofructokinase"
FT /id="PRO_0000111936"
FT ACT_SITE 127
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00339"
FT BINDING 11
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|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:0000255|HAMAP-Rule:MF_00339"
FT BINDING 72..73
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00339"
FT BINDING 102..105
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00339"
FT BINDING 103
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|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:0000255|HAMAP-Rule:MF_00339"
FT BINDING 154
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:0000255|HAMAP-Rule:MF_00339"
FT BINDING 162
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255|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:0000255|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:0000255|HAMAP-Rule:MF_00339"
FT BINDING 211
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:0000255|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:0000255|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:0000255|HAMAP-Rule:MF_00339"
FT BINDING 243
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255|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:0000255|HAMAP-Rule:MF_00339"
FT STRAND 3..11
FT /evidence="ECO:0007829|PDB:4A3S"
FT HELIX 16..29
FT /evidence="ECO:0007829|PDB:4A3S"
FT STRAND 33..37
FT /evidence="ECO:0007829|PDB:4A3S"
FT HELIX 42..46
FT /evidence="ECO:0007829|PDB:4A3S"
FT STRAND 49..52
FT /evidence="ECO:0007829|PDB:4A3S"
FT HELIX 54..57
FT /evidence="ECO:0007829|PDB:4A3S"
FT HELIX 74..77
FT /evidence="ECO:0007829|PDB:4A3S"
FT HELIX 79..91
FT /evidence="ECO:0007829|PDB:4A3S"
FT STRAND 96..101
FT /evidence="ECO:0007829|PDB:4A3S"
FT HELIX 105..114
FT /evidence="ECO:0007829|PDB:4A3S"
FT STRAND 119..125
FT /evidence="ECO:0007829|PDB:4A3S"
FT HELIX 139..160
FT /evidence="ECO:0007829|PDB:4A3S"
FT STRAND 163..168
FT /evidence="ECO:0007829|PDB:4A3S"
FT HELIX 175..184
FT /evidence="ECO:0007829|PDB:4A3S"
FT STRAND 187..191
FT /evidence="ECO:0007829|PDB:4A3S"
FT HELIX 198..209
FT /evidence="ECO:0007829|PDB:4A3S"
FT TURN 210..212
FT /evidence="ECO:0007829|PDB:4A3S"
FT STRAND 216..221
FT /evidence="ECO:0007829|PDB:4A3S"
FT TURN 222..224
FT /evidence="ECO:0007829|PDB:4A3S"
FT HELIX 227..238
FT /evidence="ECO:0007829|PDB:4A3S"
FT STRAND 242..246
FT /evidence="ECO:0007829|PDB:4A3S"
FT HELIX 248..252
FT /evidence="ECO:0007829|PDB:4A3S"
FT HELIX 258..275
FT /evidence="ECO:0007829|PDB:4A3S"
FT TURN 276..278
FT /evidence="ECO:0007829|PDB:4A3S"
FT STRAND 281..287
FT /evidence="ECO:0007829|PDB:4A3S"
FT STRAND 290..295
FT /evidence="ECO:0007829|PDB:4A3S"
FT HELIX 296..299
FT /evidence="ECO:0007829|PDB:4A3S"
FT STRAND 300..302
FT /evidence="ECO:0007829|PDB:4A3S"
FT HELIX 308..318
FT /evidence="ECO:0007829|PDB:4A3S"
SQ SEQUENCE 319 AA; 34254 MW; 706CBC7F9BCFCDFC CRC64;
MKRIGVLTSG GDSPGMNAAV RAVVRKAIYH DVEVYGIYNG YAGLISGKIE KLELGSVGDI
IHRGGTKLYT ARCPEFKTVE GREKGIANLK KLGIEGLVVI GGDGSYMGAK KLTEHGFPCV
GVPGTIDNDI PGTDFTIGFD TALNTVIDAI DKIRDTATSH ERTYVIEVMG RHAGDIALWA
GLAGGAESIL IPEADYDMHE IIARLKRGHE RGKKHSIIIV AEGVGSGVEF GKRIEEETNL
ETRVSVLGHI QRGGSPSAAD RVLASRLGAY AVELLLEGKG GRCVGIQNNK LVDHDIIEIL
ETKHTVEQNM YQLSKELSI
