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Database: UniProt/TrEMBL
Entry: K4LGF9_THEPS
LinkDB: K4LGF9_THEPS
Original site: K4LGF9_THEPS 
ID   K4LGF9_THEPS            Unreviewed;       323 AA.
AC   K4LGF9;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   27-SEP-2017, entry version 35.
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   ECO:0000313|EMBL:AFV11167.1};
GN   OrderedLocusNames=Tph_c09380 {ECO:0000313|EMBL:AFV11167.1};
OS   Thermacetogenium phaeum (strain ATCC BAA-254 / DSM 12270 / PB).
OC   Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Thermacetogenium.
OX   NCBI_TaxID=1089553 {ECO:0000313|EMBL:AFV11167.1, ECO:0000313|Proteomes:UP000000467};
RN   [1] {ECO:0000313|EMBL:AFV11167.1, ECO:0000313|Proteomes:UP000000467}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-254 / DSM 12270 / PB
RC   {ECO:0000313|Proteomes:UP000000467};
RX   PubMed=23259483; DOI=10.1186/1471-2164-13-723;
RA   Oehler D., Poehlein A., Leimbach A., Muller N., Daniel R.,
RA   Gottschalk G., Schink B.;
RT   "Genome-guided analysis of physiological and morphological traits of
RT   the fermentative acetate oxidizer Thermacetogenium phaeum.";
RL   BMC Genomics 13:723-723(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: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; CP003732; AFV11167.1; -; Genomic_DNA.
DR   EnsemblBacteria; AFV11167; AFV11167; Tph_c09380.
DR   KEGG; tpz:Tph_c09380; -.
DR   KO; K00850; -.
DR   OrthoDB; POG091H01AC; -.
DR   UniPathway; UPA00109; UER00182.
DR   Proteomes; UP000000467; 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   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:UP000000467};
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:AFV11167.1};
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:UP000000467};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00339,
KW   ECO:0000256|SAAS:SAAS00640113, ECO:0000313|EMBL:AFV11167.1}.
FT   DOMAIN        7    279       PFK. {ECO:0000259|Pfam:PF00365}.
FT   NP_BIND      76     77       ATP. {ECO:0000256|HAMAP-Rule:MF_00339}.
FT   NP_BIND     106    109       ATP. {ECO:0000256|HAMAP-Rule:MF_00339}.
FT   REGION       25     29       Allosteric activator ADP binding; shared
FT                                with dimeric partner. {ECO:0000256|HAMAP-
FT                                Rule:MF_00339}.
FT   REGION      129    131       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00339}.
FT   REGION      173    175       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00339}.
FT   REGION      189    191       Allosteric activator ADP binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00339}.
FT   REGION      217    219       Allosteric activator ADP binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00339}.
FT   REGION      253    256       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00339}.
FT   ACT_SITE    131    131       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00339}.
FT   METAL       107    107       Magnesium; catalytic. {ECO:0000256|HAMAP-
FT                                Rule:MF_00339}.
FT   BINDING      15     15       ATP; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00339}.
FT   BINDING     158    158       Allosteric activator ADP.
FT                                {ECO:0000256|HAMAP-Rule:MF_00339}.
FT   BINDING     166    166       Substrate; shared with dimeric partner.
FT                                {ECO:0000256|HAMAP-Rule:MF_00339}.
FT   BINDING     215    215       Allosteric activator ADP.
FT                                {ECO:0000256|HAMAP-Rule:MF_00339}.
FT   BINDING     226    226       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00339}.
FT   BINDING     247    247       Substrate; shared with dimeric partner.
FT                                {ECO:0000256|HAMAP-Rule:MF_00339}.
SQ   SEQUENCE   323 AA;  34308 MW;  2F404F7EAF3384B2 CRC64;
     MKRQVNRIGM LTSGGDAPGM NAAIRAVVRK SIYHGLEVVG IKRGFDGLLK KEFVKLQLGS
     VADIIHRGGT ILHTARSEEF KTEEGQRKGV NNLRDGGIDG LVVIGGDGSF KGALALAKLG
     VPVIGVPATI DNDVGGTDLT IGFDTAVNNV VDAINKIRDT ATSHERIFII EVMGRHAGHI
     ALYAGLSGGA ESILVPEIPV DIDEVIFKLQ RGINRGKLHS IIIVAEGAAS GLTIGEEIKK
     RMGQETRVTI LGHLQRGGTP TALDRMLASC MGAKAVDLLL EGESRKMVGI VNGQLVAVDI
     EDALSRKRAL NRELWELAAI LAI
//
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