(data stored in SCRATCH zone)

SWISSPROT: E6S6R7_INTC7

ID   E6S6R7_INTC7            Unreviewed;       362 AA.
AC   E6S6R7;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   08-MAY-2019, entry version 53.
DE   RecName: Full=ATP-dependent 6-phosphofructokinase {ECO:0000256|HAMAP-Rule:MF_01976};
DE            Short=ATP-PFK {ECO:0000256|HAMAP-Rule:MF_01976};
DE            Short=Phosphofructokinase {ECO:0000256|HAMAP-Rule:MF_01976};
DE            EC=2.7.1.11 {ECO:0000256|HAMAP-Rule:MF_01976};
DE   AltName: Full=Phosphohexokinase {ECO:0000256|HAMAP-Rule:MF_01976};
GN   Name=pfkA {ECO:0000256|HAMAP-Rule:MF_01976};
GN   OrderedLocusNames=Intca_0246 {ECO:0000313|EMBL:ADU46803.1};
OS   Intrasporangium calvum (strain ATCC 23552 / DSM 43043 / JCM 3097 /
OS   NBRC 12989 / 7 KIP).
OC   Bacteria; Actinobacteria; Micrococcales; Intrasporangiaceae;
OC   Intrasporangium.
OX   NCBI_TaxID=710696 {ECO:0000313|EMBL:ADU46803.1, ECO:0000313|Proteomes:UP000008914};
RN   [1] {ECO:0000313|EMBL:ADU46803.1, ECO:0000313|Proteomes:UP000008914}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23552 / DSM 43043 / JCM 3097 / NBRC 12989 / 7 KIP
RC   {ECO:0000313|Proteomes:UP000008914};
RX   PubMed=21304734; DOI=10.4056/sigs.1263355;
RA   Del Rio T.G., Chertkov O., Yasawong M., Lucas S., Deshpande S.,
RA   Cheng J.F., Detter C., Tapia R., Han C., Goodwin L., Pitluck S.,
RA   Liolios K., Ivanova N., Mavromatis K., Pati A., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA   Rohde M., Pukall R., Sikorski J., Goker M., Woyke T., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.,
RA   Lapidus A.;
RT   "Complete genome sequence of Intrasporangium calvum type strain (7
RT   KIP).";
RL   Stand. Genomic Sci. 3:294-303(2010).
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_01976}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose
CC         1,6-bisphosphate + H(+); Xref=Rhea:RHEA:16109,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:32966,
CC         ChEBI:CHEBI:57634, ChEBI:CHEBI:456216; EC=2.7.1.11;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01976};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01976, ECO:0000256|SAAS:SAAS00609123};
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_01976, ECO:0000256|SAAS:SAAS00041065}.
CC   -!- SUBUNIT: Homodimer or homotetramer. {ECO:0000256|HAMAP-
CC       Rule:MF_01976}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01976,
CC       ECO:0000256|SAAS:SAAS00551378}.
CC   -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA)
CC       family. Mixed-substrate PFK group III subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_01976}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01976}.
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DR   EMBL; CP002343; ADU46803.1; -; Genomic_DNA.
DR   RefSeq; WP_013491125.1; NC_014830.1.
DR   STRING; 710696.Intca_0246; -.
DR   EnsemblBacteria; ADU46803; ADU46803; Intca_0246.
DR   KEGG; ica:Intca_0246; -.
DR   eggNOG; ENOG4105CTQ; Bacteria.
DR   eggNOG; COG0205; LUCA.
DR   HOGENOM; HOG000248869; -.
DR   KO; K21071; -.
DR   OrthoDB; 1421302at2; -.
DR   UniPathway; UPA00109; UER00182.
DR   Proteomes; UP000008914; 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:0047334; F:diphosphate-fructose-6-phosphate 1-phosphotransferase activity; IEA:InterPro.
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_01976; Phosphofructokinase_III; 1.
DR   InterPro; IPR022953; ATP_PFK.
DR   InterPro; IPR012003; ATP_PFK_prok-type.
DR   InterPro; IPR015912; Phosphofructokinase_CS.
DR   InterPro; IPR000023; Phosphofructokinase_dom.
DR   InterPro; IPR012829; Phosphofructokinase_III.
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; TIGR02483; PFK_mixed; 1.
DR   PROSITE; PS00433; PHOSPHOFRUCTOKINASE; 1.
PE   3: Inferred from homology;
DR   PRODOM; E6S6R7.
DR   SWISS-2DPAGE; E6S6R7.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01976};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008914};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01976,
KW   ECO:0000256|SAAS:SAAS00436108};
KW   Glycolysis {ECO:0000256|HAMAP-Rule:MF_01976,
KW   ECO:0000256|SAAS:SAAS00436111};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_01976,
KW   ECO:0000256|SAAS:SAAS00436062, ECO:0000313|EMBL:ADU46803.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01976,
KW   ECO:0000256|SAAS:SAAS00436079};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01976,
KW   ECO:0000256|SAAS:SAAS00436116};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01976};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008914};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01976,
KW   ECO:0000256|SAAS:SAAS00436075, ECO:0000313|EMBL:ADU46803.1}.
FT   DOMAIN        2    297       PFK. {ECO:0000259|Pfam:PF00365}.
FT   NP_BIND      72     73       ATP. {ECO:0000256|HAMAP-Rule:MF_01976}.
FT   NP_BIND     102    105       ATP. {ECO:0000256|HAMAP-Rule:MF_01976}.
FT   REGION      125    127       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01976}.
FT   REGION      169    171       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01976}.
FT   REGION      272    275       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01976}.
FT   ACT_SITE    127    127       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01976}.
FT   METAL       103    103       Magnesium; catalytic. {ECO:0000256|HAMAP-
FT                                Rule:MF_01976}.
FT   BINDING      10     10       ATP; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01976}.
FT   BINDING     162    162       Substrate; shared with dimeric partner.
FT                                {ECO:0000256|HAMAP-Rule:MF_01976}.
FT   BINDING     222    222       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01976}.
FT   BINDING     266    266       Substrate; shared with dimeric partner.
FT                                {ECO:0000256|HAMAP-Rule:MF_01976}.
FT   SITE        104    104       Important for substrate specificity;
FT                                cannot use PPi as phosphoryl donor.
FT                                {ECO:0000256|HAMAP-Rule:MF_01976}.
SQ   SEQUENCE   362 AA;  38986 MW;  1B798FAB56A1BAA0 CRC64;
     MRIGILTGGG DCPGLNAVIR GAVRAAEVTY DSTVVGFRNA WRGVMDNDFE LLDVDRCRGI
     LPLGGTILGT SRDQPFAFED GLKKVRKAYD RHGLDAIIGV GGEGSMSVLA RLHENGFPIV
     GVPKTIDNDI SLTEMTFGFQ TAVQICTDAI DRLHTTAESH HRVLVVEVMG RHVGHIATWS
     GIAGGAAITL VPEEPFDIGE VCERIVHRHR KGRFATIIVV AEGALPQPGT MELPEPEMDK
     YGHQILGGIG SILAREIQGR TGIESRMTAL GHIQRGGSPV AFDRVLGTRF GVAAVEAALD
     GAWGQMVALQ QGHIVRVPIS DAVGQLKMVD ADLLRLNTMF QPRIPGDEYP GIPADRLERV
     ED
//

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