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Database: UniProt
Entry: O34529
LinkDB: O34529
Original site: O34529 
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   07-NOV-2018, entry version 134.
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
RT   in the 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.,
RA   Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S.,
RA   Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S.,
RA   Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M.,
RA   Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A.,
RA   Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T.,
RA   Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D.,
RA   Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N.,
RA   Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G.,
RA   Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A.,
RA   Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M.,
RA   Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M.,
RA   Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S.,
RA   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.,
RA   Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B.,
RA   Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R.,
RA   Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P.,
RA   Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H.,
RA   Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P.,
RA   Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F.,
RA   Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H.,
RA   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:
RT   interactions 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.,
RA   Rodrigues C., Herzberg C., Commichau F.M., Lewis R.J., Stulke J.;
RT   "RNase Y in Bacillus subtilis: a natively disordered protein that is
RT   the functional equivalent of RNase E from Escherichia coli.";
RL   J. Bacteriol. 193:5431-5441(2011).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS), INTERACTION WITH ENO, AND
RP   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
RT   with glycolysis in the Bacillus subtilis degradosome.";
RL   J. Mol. Biol. 416:121-136(2012).
CC   -!- FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate
CC       to fructose 1,6-bisphosphate by ATP, the first committing step of
CC       glycolysis. {ECO:0000255|HAMAP-Rule:MF_00339}.
CC   -!- CATALYTIC ACTIVITY: ATP + D-fructose 6-phosphate = ADP + D-
CC       fructose 1,6-bisphosphate. {ECO:0000255|HAMAP-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
CC       complex composed of rny, rnjA, rnjB, pnp, pfkA and eno
CC       (PubMed:19193632) (although rnjA and rnjB's presence is unclear).
CC       Specifically interacts with RNase Y (rny, PubMed:21803996) and
CC       enolase (eno, PubMed:22198292). {ECO:0000255|HAMAP-Rule:MF_00339,
CC       ECO:0000269|PubMed:19193632, ECO:0000269|PubMed:21803996,
CC       ECO:0000269|PubMed:22198292}.
CC   -!- INTERACTION:
CC       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)
CC       family. ATP-dependent PFK group I subfamily. Prokaryotic clade
CC       "B1" sub-subfamily. {ECO:0000255|HAMAP-Rule:MF_00339}.
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   ProteinModelPortal; O34529; -.
DR   SMR; O34529; -.
DR   IntAct; O34529; 4.
DR   MINT; O34529; -.
DR   STRING; 224308.Bsubs1_010100015926; -.
DR   PaxDb; O34529; -.
DR   PRIDE; O34529; -.
DR   EnsemblBacteria; CAB14879; CAB14879; BSU29190.
DR   GeneID; 937376; -.
DR   KEGG; bsu:BSU29190; -.
DR   PATRIC; fig|224308.179.peg.3169; -.
DR   eggNOG; ENOG4105CTQ; Bacteria.
DR   eggNOG; COG0205; LUCA.
DR   HOGENOM; HOG000248870; -.
DR   InParanoid; O34529; -.
DR   KO; K00850; -.
DR   OMA; GKLHSII; -.
DR   PhylomeDB; O34529; -.
DR   BioCyc; BSUB:BSU29190-MONOMER; -.
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   GO; GO:0006007; P:glucose catabolic process; IBA:GO_Central.
DR   GO; GO:0051259; P:protein complex oligomerization; IBA:GO_Central.
DR   CDD; cd00763; Bacterial_PFK; 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; Complete proteome;
KW   Cytoplasm; Glycolysis; Kinase; Magnesium; Metal-binding;
KW   Nucleotide-binding; Reference proteome; Transferase.
FT   CHAIN         1    319       ATP-dependent 6-phosphofructokinase.
FT                                /FTId=PRO_0000111936.
FT   NP_BIND      72     73       ATP. {ECO:0000255|HAMAP-Rule:MF_00339}.
FT   NP_BIND     102    105       ATP. {ECO:0000255|HAMAP-Rule:MF_00339}.
FT   REGION       21     25       Allosteric activator ADP binding; shared
FT                                with dimeric partner. {ECO:0000255|HAMAP-
FT                                Rule:MF_00339}.
FT   REGION      125    127       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00339}.
FT   REGION      169    171       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00339}.
FT   REGION      185    187       Allosteric activator ADP binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_00339}.
FT   REGION      213    215       Allosteric activator ADP binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_00339}.
FT   REGION      249    252       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00339}.
FT   ACT_SITE    127    127       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00339}.
FT   METAL       103    103       Magnesium; catalytic. {ECO:0000255|HAMAP-
FT                                Rule:MF_00339}.
FT   BINDING      11     11       ATP; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00339}.
FT   BINDING     154    154       Allosteric activator ADP.
FT                                {ECO:0000255|HAMAP-Rule:MF_00339}.
FT   BINDING     162    162       Substrate; shared with dimeric partner.
FT                                {ECO:0000255|HAMAP-Rule:MF_00339}.
FT   BINDING     211    211       Allosteric activator ADP.
FT                                {ECO:0000255|HAMAP-Rule:MF_00339}.
FT   BINDING     222    222       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00339}.
FT   BINDING     243    243       Substrate; shared with dimeric partner.
FT                                {ECO:0000255|HAMAP-Rule:MF_00339}.
FT   STRAND        3     11       {ECO:0000244|PDB:4A3S}.
FT   HELIX        16     29       {ECO:0000244|PDB:4A3S}.
FT   STRAND       33     37       {ECO:0000244|PDB:4A3S}.
FT   HELIX        42     46       {ECO:0000244|PDB:4A3S}.
FT   STRAND       49     52       {ECO:0000244|PDB:4A3S}.
FT   HELIX        54     57       {ECO:0000244|PDB:4A3S}.
FT   HELIX        74     77       {ECO:0000244|PDB:4A3S}.
FT   HELIX        79     91       {ECO:0000244|PDB:4A3S}.
FT   STRAND       96    101       {ECO:0000244|PDB:4A3S}.
FT   HELIX       105    114       {ECO:0000244|PDB:4A3S}.
FT   STRAND      119    125       {ECO:0000244|PDB:4A3S}.
FT   HELIX       139    160       {ECO:0000244|PDB:4A3S}.
FT   STRAND      163    168       {ECO:0000244|PDB:4A3S}.
FT   HELIX       175    184       {ECO:0000244|PDB:4A3S}.
FT   STRAND      187    191       {ECO:0000244|PDB:4A3S}.
FT   HELIX       198    209       {ECO:0000244|PDB:4A3S}.
FT   TURN        210    212       {ECO:0000244|PDB:4A3S}.
FT   STRAND      216    221       {ECO:0000244|PDB:4A3S}.
FT   TURN        222    224       {ECO:0000244|PDB:4A3S}.
FT   HELIX       227    238       {ECO:0000244|PDB:4A3S}.
FT   STRAND      242    246       {ECO:0000244|PDB:4A3S}.
FT   HELIX       248    252       {ECO:0000244|PDB:4A3S}.
FT   HELIX       258    275       {ECO:0000244|PDB:4A3S}.
FT   TURN        276    278       {ECO:0000244|PDB:4A3S}.
FT   STRAND      281    287       {ECO:0000244|PDB:4A3S}.
FT   STRAND      290    295       {ECO:0000244|PDB:4A3S}.
FT   HELIX       296    299       {ECO:0000244|PDB:4A3S}.
FT   STRAND      300    302       {ECO:0000244|PDB:4A3S}.
FT   HELIX       308    318       {ECO:0000244|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
//
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