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Database: UniProt/TrEMBL
Entry: E8UWL3_THEBF
LinkDB: E8UWL3_THEBF
Original site: E8UWL3_THEBF 
ID   E8UWL3_THEBF            Unreviewed;       321 AA.
AC   E8UWL3;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   25-OCT-2017, entry version 51.
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   OrderedLocusNames=Thebr_0701 {ECO:0000313|EMBL:ADV79295.1};
OS   Thermoanaerobacter brockii subsp. finnii (strain ATCC 43586 / DSM 3389
OS   / AKO-1) (Thermoanaerobacter finnii).
OC   Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Thermoanaerobacter.
OX   NCBI_TaxID=509193 {ECO:0000313|EMBL:ADV79295.1, ECO:0000313|Proteomes:UP000002062};
RN   [1] {ECO:0000313|EMBL:ADV79295.1, ECO:0000313|Proteomes:UP000002062}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43586 / DSM 3389 / AKO-1
RC   {ECO:0000313|Proteomes:UP000002062};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L.,
RA   Pitluck S., Chertkov O., Munk C., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Mikhailova N., Pagani I.,
RA   Hemme C.L., Woyke T.;
RT   "Complete sequence of Thermoanaerobacter brockii finnii Ako-1.";
RL   Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases.
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:0000256|HAMAP-Rule:MF_00339,
CC       ECO:0000256|SAAS:SAAS00729178}.
CC   -!- CATALYTIC ACTIVITY: ATP + D-fructose 6-phosphate = ADP + D-
CC       fructose 1,6-bisphosphate. {ECO:0000256|HAMAP-Rule:MF_00339,
CC       ECO:0000256|SAAS:SAAS00728855}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00339, ECO:0000256|SAAS:SAAS00640094};
CC   -!- ENZYME 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|HAMAP-Rule:MF_00339, ECO:0000256|SAAS:SAAS00640117}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00339,
CC       ECO:0000256|SAAS:SAAS00643582}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00339,
CC       ECO:0000256|SAAS:SAAS00640112}.
CC   -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA)
CC       family. ATP-dependent PFK group I subfamily. Prokaryotic clade
CC       "B1" sub-subfamily. {ECO:0000256|HAMAP-Rule:MF_00339,
CC       ECO:0000256|SAAS:SAAS00634686}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00339}.
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DR   EMBL; CP002466; ADV79295.1; -; Genomic_DNA.
DR   RefSeq; WP_003868325.1; NC_014964.1.
DR   ProteinModelPortal; E8UWL3; -.
DR   SMR; E8UWL3; -.
DR   EnsemblBacteria; ADV79295; ADV79295; Thebr_0701.
DR   GeneID; 11083396; -.
DR   KEGG; tbo:Thebr_0701; -.
DR   HOGENOM; HOG000248870; -.
DR   KO; K00850; -.
DR   UniPathway; UPA00109; UER00182.
DR   Proteomes; UP000002062; Chromosome.
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   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|HAMAP-Rule:MF_00339};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00339,
KW   ECO:0000256|SAAS:SAAS00728960};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002062};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00339,
KW   ECO:0000256|SAAS:SAAS00640104};
KW   Glycolysis {ECO:0000256|HAMAP-Rule:MF_00339,
KW   ECO:0000256|SAAS:SAAS00640111};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00339,
KW   ECO:0000256|SAAS:SAAS00640102, ECO:0000313|EMBL:ADV79295.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00339,
KW   ECO:0000256|SAAS:SAAS00640121};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00339,
KW   ECO:0000256|SAAS:SAAS00640110};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00339,
KW   ECO:0000256|SAAS:SAAS00728832};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00339,
KW   ECO:0000256|SAAS:SAAS00640113}.
FT   DOMAIN        4    277       PFK. {ECO:0000259|Pfam:PF00365}.
FT   NP_BIND      72     73       ATP. {ECO:0000256|HAMAP-Rule:MF_00339}.
FT   NP_BIND     102    105       ATP. {ECO:0000256|HAMAP-Rule:MF_00339}.
FT   REGION       21     25       Allosteric activator ADP binding; shared
FT                                with dimeric partner. {ECO:0000256|HAMAP-
FT                                Rule:MF_00339}.
FT   REGION      126    128       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00339}.
FT   REGION      170    172       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00339}.
FT   REGION      186    188       Allosteric activator ADP binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00339}.
FT   REGION      214    216       Allosteric activator ADP binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00339}.
FT   REGION      251    254       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00339}.
FT   ACT_SITE    128    128       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00339}.
FT   METAL       103    103       Magnesium; catalytic. {ECO:0000256|HAMAP-
FT                                Rule:MF_00339}.
FT   BINDING      11     11       ATP; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00339}.
FT   BINDING     155    155       Allosteric activator ADP.
FT                                {ECO:0000256|HAMAP-Rule:MF_00339}.
FT   BINDING     163    163       Substrate; shared with dimeric partner.
FT                                {ECO:0000256|HAMAP-Rule:MF_00339}.
FT   BINDING     212    212       Allosteric activator ADP.
FT                                {ECO:0000256|HAMAP-Rule:MF_00339}.
FT   BINDING     223    223       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00339}.
FT   BINDING     245    245       Substrate; shared with dimeric partner.
FT                                {ECO:0000256|HAMAP-Rule:MF_00339}.
SQ   SEQUENCE   321 AA;  35215 MW;  595F90D4BF423E29 CRC64;
     MKTIGILTSG GDAPGMNAAI RAVVRTGIYY GLKVKGIMRG YAGLVEDEVI DLNLSSVGDI
     LQKGGTILRT ARCEEFKKKE VRKKAYETLQ KHGIEGLVVI GGDGSFRGAQ LLSEEWNVNT
     IGIPGTIDND IPCTDYTIGF DTACNTVIDA INKIRDTATS HERANIIEVM GRNAGYIALY
     AGLAGGAEMI ILPEVEWSID ELCDKITYGI KRGKLHHIIV LAEGVMSAPE LAKMIKERLP
     KLDLRYTILG HIQRGGAPTV MDRVLASQMG ARAVELLLEN KTKRIISIRN NQIVDDDIDE
     ALSMKKEFNR KLYELSKILS I
//
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