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Database: UniProt/TrEMBL
Entry: L0IFX7_THETR
LinkDB: L0IFX7_THETR
Original site: L0IFX7_THETR 
ID   L0IFX7_THETR            Unreviewed;       321 AA.
AC   L0IFX7;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   07-JUN-2017, entry version 36.
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   ORFNames=Thethe_00748 {ECO:0000313|EMBL:AGB18435.1};
OS   Thermoanaerobacterium thermosaccharolyticum M0795.
OC   Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacterales Family III. Incertae Sedis;
OC   Thermoanaerobacterium.
OX   NCBI_TaxID=698948 {ECO:0000313|EMBL:AGB18435.1, ECO:0000313|Proteomes:UP000010845};
RN   [1] {ECO:0000313|EMBL:AGB18435.1, ECO:0000313|Proteomes:UP000010845}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M0795 {ECO:0000313|EMBL:AGB18435.1,
RC   ECO:0000313|Proteomes:UP000010845};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Teshima H., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Kyrpides N., Ivanova N., Pagani I., Feinberg L., Folden J.,
RA   Hogsett D., Shaw J., Woyke T.;
RT   "Complete sequence of chromosome of Thermoanaerobacterium
RT   thermosaccharolyticum M0795.";
RL   Submitted (MAR-2012) 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; CP003066; AGB18435.1; -; Genomic_DNA.
DR   RefSeq; WP_015311153.1; NC_019970.1.
DR   EnsemblBacteria; AGB18435; AGB18435; Thethe_00748.
DR   KEGG; tto:Thethe_00748; -.
DR   PATRIC; fig|698948.3.peg.733; -.
DR   KO; K00850; -.
DR   OrthoDB; POG091H01AC; -.
DR   UniPathway; UPA00109; UER00182.
DR   Proteomes; UP000010845; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003872; F:6-phosphofructokinase activity; IEA:UniProtKB-HAMAP.
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   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:UP000010845};
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:AGB18435.1};
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;  34714 MW;  B4021CB13DFD7BBB CRC64;
     MKTIGVLTSG GDAPGMNAAI RAVVRCGIYN GLTVKGIMRG YQGLIDDEIE DMTLSSVGDI
     IQRGGTILRT ARSAEFKTKE GRAKAAEVLK KHGIEGLIII GGDGSFRGAQ LLSNEHGVNT
     IGIPGTIDND IPCTDYTIGF DTACNTAIDA INKIRDTATS HERANIIEVM GRNAGYIALY
     AGLAGGAEII IIPEVKFDID EVCDKISYGI KRGKLHHIIV LAEGVMSGLE LSKMIQERLP
     KLDLRHTTLG HIQRGGAPSV MDRIIASQMG ARAVELLLEN KSQRIISIRN NQIVDDDIDT
     ALAMRKEFNF KLYELSKILS I
//
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