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Database: UniProt/TrEMBL
Entry: C5CF49_KOSOT
LinkDB: C5CF49_KOSOT
Original site: C5CF49_KOSOT 
ID   C5CF49_KOSOT            Unreviewed;       320 AA.
AC   C5CF49;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   25-OCT-2017, entry version 64.
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=Kole_1624 {ECO:0000313|EMBL:ACR80314.1};
OS   Kosmotoga olearia (strain TBF 19.5.1).
OC   Bacteria; Thermotogae; Kosmotogales; Kosmotogaceae; Kosmotoga.
OX   NCBI_TaxID=521045 {ECO:0000313|EMBL:ACR80314.1, ECO:0000313|Proteomes:UP000002382};
RN   [1] {ECO:0000313|EMBL:ACR80314.1, ECO:0000313|Proteomes:UP000002382}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TBF 19.5.1 {ECO:0000313|EMBL:ACR80314.1,
RC   ECO:0000313|Proteomes:UP000002382};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T.,
RA   Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Ovchinnikova G., Noll K.;
RT   "Complete sequence of Thermotogales bacterium TBF 19.5.1.";
RL   Submitted (JUN-2009) 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; CP001634; ACR80314.1; -; Genomic_DNA.
DR   STRING; 521045.Kole_1624; -.
DR   EnsemblBacteria; ACR80314; ACR80314; Kole_1624.
DR   KEGG; kol:Kole_1624; -.
DR   eggNOG; ENOG4105CTQ; Bacteria.
DR   eggNOG; COG0205; LUCA.
DR   HOGENOM; HOG000248870; -.
DR   KO; K00850; -.
DR   OMA; GKLHSII; -.
DR   OrthoDB; POG091H01AC; -.
DR   UniPathway; UPA00109; UER00182.
DR   Proteomes; UP000002382; 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:UP000002382};
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:ACR80314.1};
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   Reference proteome {ECO:0000313|Proteomes:UP000002382};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00339,
KW   ECO:0000256|SAAS:SAAS00640113, ECO:0000313|EMBL:ACR80314.1}.
FT   DOMAIN        4    277       PFK. {ECO:0000259|Pfam:PF00365}.
FT   NP_BIND      73     74       ATP. {ECO:0000256|HAMAP-Rule:MF_00339}.
FT   NP_BIND     103    106       ATP. {ECO:0000256|HAMAP-Rule:MF_00339}.
FT   REGION       22     26       Allosteric activator ADP binding; shared
FT                                with dimeric partner. {ECO:0000256|HAMAP-
FT                                Rule:MF_00339}.
FT   REGION      127    129       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00339}.
FT   REGION      171    173       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00339}.
FT   REGION      187    189       Allosteric activator ADP binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00339}.
FT   REGION      215    217       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    129    129       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00339}.
FT   METAL       104    104       Magnesium; catalytic. {ECO:0000256|HAMAP-
FT                                Rule:MF_00339}.
FT   BINDING      12     12       ATP; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00339}.
FT   BINDING     156    156       Allosteric activator ADP.
FT                                {ECO:0000256|HAMAP-Rule:MF_00339}.
FT   BINDING     164    164       Substrate; shared with dimeric partner.
FT                                {ECO:0000256|HAMAP-Rule:MF_00339}.
FT   BINDING     213    213       Allosteric activator ADP.
FT                                {ECO:0000256|HAMAP-Rule:MF_00339}.
FT   BINDING     224    224       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   320 AA;  34581 MW;  A88C4CC60CFC158E CRC64;
     MIKKIAVMTS GGDAPGMNAA IRAAVRTAVT ENIEIVGIKR GYSGLLDEDF IEMSYASVGG
     IMEKGGTILR SSRCEEFQTT EGRKRAAEIL KKYGIEALVV IGGEGSLTGA MLLSEENDIP
     VIGIPGTIDN DIAHTDMCIG VDTCLNTVIG NIQKLKDTAS SHERAFIVEV MGRHSGYIAL
     ASGLATGAEA ILIPEIPVDY DAIAEKLWNE RKRGKINCIV VVAEGVASAY TVARHMEHRI
     GYETRITILG HVQRGGSPTA FDRILASRMG YEAIKALQEE DFGTMIALQS GKMVRIPLKK
     VLSEKKKIDE KLIEMSKILS
//
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