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Database: UniProt
Entry: Q8A624
LinkDB: Q8A624
Original site: Q8A624 
ID   PFKA2_BACTN             Reviewed;         326 AA.
AC   Q8A624;
DT   16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2003, sequence version 1.
DT   07-NOV-2018, entry version 99.
DE   RecName: Full=ATP-dependent 6-phosphofructokinase 2 {ECO:0000255|HAMAP-Rule:MF_00339};
DE            Short=ATP-PFK 2 {ECO:0000255|HAMAP-Rule:MF_00339};
DE            Short=Phosphofructokinase 2 {ECO:0000255|HAMAP-Rule:MF_00339};
DE            EC=2.7.1.11 {ECO:0000255|HAMAP-Rule:MF_00339};
DE   AltName: Full=Phosphohexokinase 2 {ECO:0000255|HAMAP-Rule:MF_00339};
GN   Name=pfkA2 {ECO:0000255|HAMAP-Rule:MF_00339};
GN   OrderedLocusNames=BT_2062;
OS   Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / NCTC
OS   10582 / E50 / VPI-5482).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=226186;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482;
RX   PubMed=12663928; DOI=10.1126/science.1080029;
RA   Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K.,
RA   Chiang H.C., Hooper L.V., Gordon J.I.;
RT   "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis.";
RL   Science 299:2074-2076(2003).
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   -!- 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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00339}.
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; AE015928; AAO77169.1; -; Genomic_DNA.
DR   RefSeq; NP_810975.1; NC_004663.1.
DR   RefSeq; WP_008761048.1; NC_004663.1.
DR   ProteinModelPortal; Q8A624; -.
DR   SMR; Q8A624; -.
DR   STRING; 226186.BT_2062; -.
DR   PaxDb; Q8A624; -.
DR   PRIDE; Q8A624; -.
DR   EnsemblBacteria; AAO77169; AAO77169; BT_2062.
DR   GeneID; 1071883; -.
DR   GeneID; 31615509; -.
DR   KEGG; bth:BT_2062; -.
DR   PATRIC; fig|226186.12.peg.2120; -.
DR   eggNOG; ENOG4105CTQ; Bacteria.
DR   eggNOG; COG0205; LUCA.
DR   InParanoid; Q8A624; -.
DR   KO; K00850; -.
DR   OMA; GKLHSII; -.
DR   OrthoDB; POG091H01AC; -.
DR   BioCyc; BTHE:G13PU-7004-MONOMER; -.
DR   UniPathway; UPA00109; UER00182.
DR   Proteomes; UP000001414; Chromosome.
DR   GO; GO:0005945; C:6-phosphofructokinase complex; IBA:GO_Central.
DR   GO; GO:0003872; F:6-phosphofructokinase activity; IBA:GO_Central.
DR   GO; GO:0016208; F:AMP binding; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR   GO; GO:0070095; F:fructose-6-phosphate binding; IBA:GO_Central.
DR   GO; GO:0042802; F:identical protein binding; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0048029; F:monosaccharide binding; IBA:GO_Central.
DR   GO; GO:0061621; P:canonical glycolysis; IBA:GO_Central.
DR   GO; GO:0030388; P:fructose 1,6-bisphosphate metabolic process; IBA:GO_Central.
DR   GO; GO:0006002; P:fructose 6-phosphate metabolic process; IBA:GO_Central.
DR   GO; GO:0006007; P:glucose catabolic process; IBA:GO_Central.
DR   GO; GO:0051259; P:protein complex oligomerization; IBA:GO_Central.
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; ATP-binding; Complete proteome; Cytoplasm;
KW   Glycolysis; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
KW   Reference proteome; Transferase.
FT   CHAIN         1    326       ATP-dependent 6-phosphofructokinase 2.
FT                                /FTId=PRO_0000111938.
FT   NP_BIND      75     76       ATP. {ECO:0000255|HAMAP-Rule:MF_00339}.
FT   NP_BIND     105    108       ATP. {ECO:0000255|HAMAP-Rule:MF_00339}.
FT   REGION       24     28       Allosteric activator ADP binding; shared
FT                                with dimeric partner. {ECO:0000255|HAMAP-
FT                                Rule:MF_00339}.
FT   REGION      129    131       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00339}.
FT   REGION      173    175       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00339}.
FT   REGION      189    191       Allosteric activator ADP binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_00339}.
FT   REGION      217    219       Allosteric activator ADP binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_00339}.
FT   REGION      256    259       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00339}.
FT   ACT_SITE    131    131       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00339}.
FT   METAL       106    106       Magnesium; catalytic. {ECO:0000255|HAMAP-
FT                                Rule:MF_00339}.
FT   BINDING      14     14       ATP; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00339}.
FT   BINDING     158    158       Allosteric activator ADP.
FT                                {ECO:0000255|HAMAP-Rule:MF_00339}.
FT   BINDING     166    166       Substrate; shared with dimeric partner.
FT                                {ECO:0000255|HAMAP-Rule:MF_00339}.
FT   BINDING     215    215       Allosteric activator ADP.
FT                                {ECO:0000255|HAMAP-Rule:MF_00339}.
FT   BINDING     226    226       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00339}.
FT   BINDING     250    250       Substrate; shared with dimeric partner.
FT                                {ECO:0000255|HAMAP-Rule:MF_00339}.
SQ   SEQUENCE   326 AA;  35257 MW;  EEF46D4915E7A082 CRC64;
     MGTVKCIGIL TSGGDAPGMN AAIRAVTRAA IYNGLQVKGI YRGYKGLVTG EIKEFKSQNV
     SNIIQLGGTI LKTARCKEFT TPEGRQLAYD NMKREGIDAL VIIGGDGSLT GARIFAQEFD
     VPCIGLPGTI DNDLYGTDTT IGYDTALNTI LDAVDKIRDT ATSHERLFFV EVMGRDAGFL
     ALNGAIASGA EAAIIPEFST EVDQLEEFIK NGFRKSKNSS IVLVAESELT GGAMHYAERV
     KNEYPQYDVR VTILGHLQRG GSPTAHDRIL ASRLGAAAID AIMEDQRNVM IGIEHDEIVY
     VPFSKAIKND KPVKRDLVNV LKELSI
//
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