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Database: UniProt
Entry: P0A796
LinkDB: P0A796
Original site: P0A796 
ID   PFKA_ECOLI              Reviewed;         320 AA.
AC   P0A796; P06998; Q2M8L2;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2005, sequence version 1.
DT   12-SEP-2018, entry version 118.
DE   RecName: Full=ATP-dependent 6-phosphofructokinase isozyme 1 {ECO:0000255|HAMAP-Rule:MF_00339};
DE            Short=ATP-PFK 1 {ECO:0000255|HAMAP-Rule:MF_00339};
DE            Short=Phosphofructokinase 1 {ECO:0000255|HAMAP-Rule:MF_00339};
DE            EC=2.7.1.11 {ECO:0000255|HAMAP-Rule:MF_00339};
DE   AltName: Full=6-phosphofructokinase isozyme I;
DE   AltName: Full=Phosphohexokinase 1 {ECO:0000255|HAMAP-Rule:MF_00339};
GN   Name=pfkA {ECO:0000255|HAMAP-Rule:MF_00339};
GN   OrderedLocusNames=b3916, JW3887;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3158524; DOI=10.1111/j.1432-1033.1985.tb08934.x;
RA   Hellinga H.W., Evans P.R.;
RT   "Nucleotide sequence and high-level expression of the major
RT   Escherichia coli phosphofructokinase.";
RL   Eur. J. Biochem. 149:363-373(1985).
RN   [2]
RP   SEQUENCE REVISION, ACTIVE SITE, AND MUTAGENESIS OF ASP-128 AND
RP   ARG-172.
RX   PubMed=2953977; DOI=10.1038/327437a0;
RA   Hellinga H.W., Evans P.R.;
RT   "Mutations in the active site of Escherichia coli
RT   phosphofructokinase.";
RL   Nature 327:437-439(1987).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=8346018; DOI=10.1093/nar/21.15.3391;
RA   Plunkett G. III, Burland V., Daniels D.L., Blattner F.R.;
RT   "Analysis of the Escherichia coli genome. III. DNA sequence of the
RT   region from 87.2 to 89.2 minutes.";
RL   Nucleic Acids Res. 21:3391-3398(1993).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
RA   Mau B., Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains
RT   MG1655 and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [6]
RP   PROTEIN SEQUENCE OF 1-8.
RC   STRAIN=K12;
RX   PubMed=17895580; DOI=10.1266/ggs.82.291;
RA   Otsuka Y., Koga M., Iwamoto A., Yonesaki T.;
RT   "A role of RnlA in the RNase LS activity from Escherichia coli.";
RL   Genes Genet. Syst. 82:291-299(2007).
RN   [7]
RP   IDENTIFICATION BY 2D-GEL.
RX   PubMed=9298644; DOI=10.1002/elps.1150180805;
RA   VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R.,
RA   Neidhardt F.C.;
RT   "Escherichia coli proteome analysis using the gene-protein database.";
RL   Electrophoresis 18:1243-1251(1997).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) IN COMPLEX WITH MAGNESIUM; ADP;
RP   FRUCTOSE 1,6-BISPHOSPHATE AND ALLOSTERIC ACTIVATOR, AND ACTIVE SITE.
RX   PubMed=2975709; DOI=10.1016/0022-2836(88)90056-3;
RA   Shirakihara Y., Evans P.R.;
RT   "Crystal structure of the complex of phosphofructokinase from
RT   Escherichia coli with its reaction products.";
RL   J. Mol. Biol. 204:973-994(1988).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
RX   PubMed=2527305; DOI=10.1016/0022-2836(89)90246-5;
RA   Rypniewski W.R., Evans P.R.;
RT   "Crystal structure of unliganded phosphofructokinase from Escherichia
RT   coli.";
RL   J. Mol. Biol. 207:805-821(1989).
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         ECO:0000269|PubMed:2975709};
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. {ECO:0000255|HAMAP-Rule:MF_00339,
CC       ECO:0000269|PubMed:2975709}.
CC   -!- INTERACTION:
CC       P12281:moeA; NbExp=2; IntAct=EBI-554405, EBI-554393;
CC       P0A7I4:prfC; NbExp=2; IntAct=EBI-554405, EBI-556252;
CC       P37440:ucpA; NbExp=2; IntAct=EBI-554405, EBI-559387;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00339,
CC       ECO:0000305|PubMed:17895580}.
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; X02519; CAA26356.1; -; Genomic_DNA.
DR   EMBL; L19201; AAB03048.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC76898.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE77394.1; -; Genomic_DNA.
DR   PIR; G65197; KIECFA.
DR   RefSeq; NP_418351.1; NC_000913.3.
DR   RefSeq; WP_000591795.1; NZ_LN832404.1.
DR   PDB; 1PFK; X-ray; 2.40 A; A/B=1-320.
DR   PDB; 2PFK; X-ray; 2.40 A; A/B/C/D=1-320.
DR   PDBsum; 1PFK; -.
DR   PDBsum; 2PFK; -.
DR   ProteinModelPortal; P0A796; -.
DR   SMR; P0A796; -.
DR   BioGrid; 4261224; 17.
DR   DIP; DIP-35841N; -.
DR   IntAct; P0A796; 7.
DR   STRING; 316385.ECDH10B_4105; -.
DR   SWISS-2DPAGE; P0A796; -.
DR   EPD; P0A796; -.
DR   PaxDb; P0A796; -.
DR   PRIDE; P0A796; -.
DR   EnsemblBacteria; AAC76898; AAC76898; b3916.
DR   EnsemblBacteria; BAE77394; BAE77394; BAE77394.
DR   GeneID; 948412; -.
DR   KEGG; ecj:JW3887; -.
DR   KEGG; eco:b3916; -.
DR   PATRIC; fig|1411691.4.peg.2789; -.
DR   EchoBASE; EB0693; -.
DR   EcoGene; EG10699; pfkA.
DR   eggNOG; ENOG4105CTQ; Bacteria.
DR   eggNOG; COG0205; LUCA.
DR   HOGENOM; HOG000248870; -.
DR   InParanoid; P0A796; -.
DR   KO; K00850; -.
DR   OMA; GKLHSII; -.
DR   PhylomeDB; P0A796; -.
DR   BioCyc; EcoCyc:6PFK-1-MONOMER; -.
DR   BioCyc; MetaCyc:6PFK-1-MONOMER; -.
DR   BRENDA; 2.7.1.11; 2026.
DR   SABIO-RK; P0A796; -.
DR   UniPathway; UPA00109; UER00182.
DR   EvolutionaryTrace; P0A796; -.
DR   PRO; PR:P0A796; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005945; C:6-phosphofructokinase complex; IDA:EcoliWiki.
DR   GO; GO:0005737; C:cytoplasm; IDA:EcoliWiki.
DR   GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR   GO; GO:0003872; F:6-phosphofructokinase activity; IDA:EcoCyc.
DR   GO; GO:0005524; F:ATP binding; IMP:EcoliWiki.
DR   GO; GO:0019003; F:GDP binding; IDA:EcoCyc.
DR   GO; GO:0042802; F:identical protein binding; IDA:EcoliWiki.
DR   GO; GO:0000287; F:magnesium ion binding; IDA:EcoliWiki.
DR   GO; GO:0032553; F:ribonucleotide binding; IDA:EcoliWiki.
DR   GO; GO:0044275; P:cellular carbohydrate catabolic process; IMP:EcoliWiki.
DR   GO; GO:0006002; P:fructose 6-phosphate metabolic process; IEA:InterPro.
DR   GO; GO:0006007; P:glucose catabolic process; IMP:EcoliWiki.
DR   GO; GO:0006096; P:glycolytic process; IDA:EcoliWiki.
DR   GO; GO:0051289; P:protein homotetramerization; IPI:EcoCyc.
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; Direct protein sequencing; Glycolysis; Kinase; Magnesium;
KW   Metal-binding; Nucleotide-binding; Reference proteome; Transferase.
FT   CHAIN         1    320       ATP-dependent 6-phosphofructokinase
FT                                isozyme 1.
FT                                /FTId=PRO_0000111950.
FT   NP_BIND      73     74       ATP. {ECO:0000255|HAMAP-Rule:MF_00339,
FT                                ECO:0000269|PubMed:2975709}.
FT   NP_BIND     103    106       ATP. {ECO:0000255|HAMAP-Rule:MF_00339,
FT                                ECO:0000269|PubMed:2975709}.
FT   REGION       22     26       Allosteric activator ADP binding; shared
FT                                with dimeric partner. {ECO:0000255|HAMAP-
FT                                Rule:MF_00339,
FT                                ECO:0000269|PubMed:2975709}.
FT   REGION       55     60       Allosteric activator ADP binding; shared
FT                                with dimeric partner. {ECO:0000255|HAMAP-
FT                                Rule:MF_00339,
FT                                ECO:0000269|PubMed:2975709}.
FT   REGION      126    128       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00339,
FT                                ECO:0000269|PubMed:2975709}.
FT   REGION      170    172       Substrate binding.
FT                                {ECO:0000250|UniProtKB:P00512,
FT                                ECO:0000255|HAMAP-Rule:MF_00339}.
FT   REGION      186    188       Allosteric activator ADP binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_00339,
FT                                ECO:0000269|PubMed:2975709}.
FT   REGION      214    216       Allosteric activator ADP binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_00339,
FT                                ECO:0000269|PubMed:2975709}.
FT   REGION      250    253       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00339,
FT                                ECO:0000269|PubMed:2975709}.
FT   ACT_SITE    128    128       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00339,
FT                                ECO:0000269|PubMed:2953977,
FT                                ECO:0000269|PubMed:2975709}.
FT   METAL       104    104       Magnesium; catalytic. {ECO:0000255|HAMAP-
FT                                Rule:MF_00339,
FT                                ECO:0000269|PubMed:2975709}.
FT   BINDING      12     12       ATP; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00339,
FT                                ECO:0000269|PubMed:2975709}.
FT   BINDING     155    155       Allosteric activator ADP.
FT                                {ECO:0000255|HAMAP-Rule:MF_00339,
FT                                ECO:0000269|PubMed:2975709}.
FT   BINDING     163    163       Substrate; shared with dimeric partner.
FT                                {ECO:0000255|HAMAP-Rule:MF_00339,
FT                                ECO:0000269|PubMed:2975709}.
FT   BINDING     212    212       Allosteric activator ADP.
FT                                {ECO:0000250|UniProtKB:P00512,
FT                                ECO:0000255|HAMAP-Rule:MF_00339}.
FT   BINDING     223    223       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00339,
FT                                ECO:0000269|PubMed:2975709}.
FT   BINDING     244    244       Substrate; shared with dimeric partner.
FT                                {ECO:0000255|HAMAP-Rule:MF_00339,
FT                                ECO:0000269|PubMed:2975709}.
FT   MUTAGEN     128    128       D->S: 18000-fold reduction of catalytic
FT                                rate. {ECO:0000269|PubMed:2953977}.
FT   MUTAGEN     172    172       R->S: 3.4-fold reduction in turnover
FT                                numbers. {ECO:0000269|PubMed:2953977}.
FT   CONFLICT     74     74       F -> C (in Ref. 1; CAA26356).
FT                                {ECO:0000305}.
FT   CONFLICT    103    104       GD -> DG (in Ref. 1; CAA26356).
FT                                {ECO:0000305}.
FT   CONFLICT    163    163       R -> P (in Ref. 1; CAA26356).
FT                                {ECO:0000305}.
FT   CONFLICT    317    319       KKL -> EKM (in Ref. 1; CAA26356).
FT                                {ECO:0000305}.
FT   STRAND        4      9       {ECO:0000244|PDB:1PFK}.
FT   HELIX        17     30       {ECO:0000244|PDB:1PFK}.
FT   STRAND       34     39       {ECO:0000244|PDB:1PFK}.
FT   HELIX        41     46       {ECO:0000244|PDB:1PFK}.
FT   STRAND       50     53       {ECO:0000244|PDB:1PFK}.
FT   HELIX        56     58       {ECO:0000244|PDB:1PFK}.
FT   HELIX        75     78       {ECO:0000244|PDB:1PFK}.
FT   HELIX        80     92       {ECO:0000244|PDB:1PFK}.
FT   STRAND       97    102       {ECO:0000244|PDB:1PFK}.
FT   HELIX       104    115       {ECO:0000244|PDB:1PFK}.
FT   STRAND      120    125       {ECO:0000244|PDB:1PFK}.
FT   HELIX       140    161       {ECO:0000244|PDB:1PFK}.
FT   STRAND      164    169       {ECO:0000244|PDB:1PFK}.
FT   HELIX       176    184       {ECO:0000244|PDB:1PFK}.
FT   STRAND      188    191       {ECO:0000244|PDB:1PFK}.
FT   HELIX       199    211       {ECO:0000244|PDB:1PFK}.
FT   STRAND      217    226       {ECO:0000244|PDB:1PFK}.
FT   HELIX       228    239       {ECO:0000244|PDB:1PFK}.
FT   STRAND      243    247       {ECO:0000244|PDB:1PFK}.
FT   HELIX       249    253       {ECO:0000244|PDB:1PFK}.
FT   HELIX       259    277       {ECO:0000244|PDB:1PFK}.
FT   STRAND      282    288       {ECO:0000244|PDB:1PFK}.
FT   STRAND      291    296       {ECO:0000244|PDB:1PFK}.
FT   HELIX       297    303       {ECO:0000244|PDB:1PFK}.
FT   HELIX       310    319       {ECO:0000244|PDB:1PFK}.
SQ   SEQUENCE   320 AA;  34842 MW;  D03D79F6A5536A41 CRC64;
     MIKKIGVLTS GGDAPGMNAA IRGVVRSALT EGLEVMGIYD GYLGLYEDRM VQLDRYSVSD
     MINRGGTFLG SARFPEFRDE NIRAVAIENL KKRGIDALVV IGGDGSYMGA MRLTEMGFPC
     IGLPGTIDND IKGTDYTIGF FTALSTVVEA IDRLRDTSSS HQRISVVEVM GRYCGDLTLA
     AAIAGGCEFV VVPEVEFSRE DLVNEIKAGI AKGKKHAIVA ITEHMCDVDE LAHFIEKETG
     RETRATVLGH IQRGGSPVPY DRILASRMGA YAIDLLLAGY GGRCVGIQNE QLVHHDIIDA
     IENMKRPFKG DWLDCAKKLY
//
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