(data stored in SCRATCH zone)

SWISSPROT: C5DCN7_LACTC

ID   C5DCN7_LACTC            Unreviewed;       975 AA.
AC   C5DCN7;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   08-MAY-2019, entry version 69.
DE   RecName: Full=ATP-dependent 6-phosphofructokinase {ECO:0000256|HAMAP-Rule:MF_03184};
DE            Short=ATP-PFK {ECO:0000256|HAMAP-Rule:MF_03184};
DE            Short=Phosphofructokinase {ECO:0000256|HAMAP-Rule:MF_03184};
DE            EC=2.7.1.11 {ECO:0000256|HAMAP-Rule:MF_03184};
DE   AltName: Full=Phosphohexokinase {ECO:0000256|HAMAP-Rule:MF_03184};
GN   OrderedLocusNames=KLTH0B04576g {ECO:0000313|EMBL:CAR21548.1};
OS   Lachancea thermotolerans (strain ATCC 56472 / CBS 6340 / NRRL Y-8284)
OS   (Yeast) (Kluyveromyces thermotolerans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Lachancea.
OX   NCBI_TaxID=559295 {ECO:0000313|EMBL:CAR21548.1, ECO:0000313|Proteomes:UP000002036};
RN   [1] {ECO:0000313|EMBL:CAR21548.1, ECO:0000313|Proteomes:UP000002036}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 56472 / CBS 6340 / NRRL Y-8284
RC   {ECO:0000313|Proteomes:UP000002036};
RX   PubMed=19525356; DOI=10.1101/gr.091546.109;
RG   The Genolevures Consortium;
RA   Souciet J.-L., Dujon B., Gaillardin C., Johnston M., Baret P.V.,
RA   Cliften P., Sherman D.J., Weissenbach J., Westhof E., Wincker P.,
RA   Jubin C., Poulain J., Barbe V., Segurens B., Artiguenave F.,
RA   Anthouard V., Vacherie B., Val M.-E., Fulton R.S., Minx P., Wilson R.,
RA   Durrens P., Jean G., Marck C., Martin T., Nikolski M., Rolland T.,
RA   Seret M.-L., Casaregola S., Despons L., Fairhead C., Fischer G.,
RA   Lafontaine I., Leh V., Lemaire M., de Montigny J., Neuveglise C.,
RA   Thierry A., Blanc-Lenfle I., Bleykasten C., Diffels J., Fritsch E.,
RA   Frangeul L., Goeffon A., Jauniaux N., Kachouri-Lafond R., Payen C.,
RA   Potier S., Pribylova L., Ozanne C., Richard G.-F., Sacerdot C.,
RA   Straub M.-L., Talla E.;
RT   "Comparative genomics of protoploid Saccharomycetaceae.";
RL   Genome Res. 19:1696-1709(2009).
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_03184}.
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_03184,
CC         ECO:0000256|PIRNR:PIRNR000533};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_03184};
CC   -!- ACTIVITY REGULATION: Allosterically activated by ADP, AMP, or
CC       fructose 2,6-bisphosphate, and allosterically inhibited by ATP or
CC       citrate. {ECO:0000256|HAMAP-Rule:MF_03184}.
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_03184, ECO:0000256|PIRNR:PIRNR000533}.
CC   -!- SUBUNIT: Heterooctamer of 4 alpha and 4 beta chains.
CC       {ECO:0000256|HAMAP-Rule:MF_03184}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03184}.
CC   -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA)
CC       family. ATP-dependent PFK group I subfamily. Eukaryotic two domain
CC       clade "E" sub-subfamily. {ECO:0000256|HAMAP-Rule:MF_03184,
CC       ECO:0000256|PIRNR:PIRNR000533}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; CU928166; CAR21548.1; -; Genomic_DNA.
DR   RefSeq; XP_002551986.1; XM_002551940.1.
DR   STRING; 381046.XP_002551986.1; -.
DR   EnsemblFungi; CAR21548; CAR21548; KLTH0B04576g.
DR   GeneID; 8290823; -.
DR   KEGG; lth:KLTH0B04576g; -.
DR   HOGENOM; HOG000200154; -.
DR   InParanoid; C5DCN7; -.
DR   KO; K00850; -.
DR   OMA; GCKAYFI; -.
DR   OrthoDB; 172878at2759; -.
DR   UniPathway; UPA00109; UER00182.
DR   Proteomes; UP000002036; Chromosome B.
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_03184; Phosphofructokinase_I_E; 1.
DR   InterPro; IPR009161; 6-Pfructokinase_euk.
DR   InterPro; IPR022953; ATP_PFK.
DR   InterPro; IPR040712; Pfk_N.
DR   InterPro; IPR015912; Phosphofructokinase_CS.
DR   InterPro; IPR000023; Phosphofructokinase_dom.
DR   InterPro; IPR035966; PKF_sf.
DR   Pfam; PF00365; PFK; 2.
DR   Pfam; PF18468; Pfk_N; 1.
DR   PIRSF; PIRSF000533; ATP_PFK_euk; 1.
DR   PRINTS; PR00476; PHFRCTKINASE.
DR   SUPFAM; SSF53784; SSF53784; 2.
DR   TIGRFAMs; TIGR02478; 6PF1K_euk; 1.
DR   PROSITE; PS00433; PHOSPHOFRUCTOKINASE; 2.
PE   3: Inferred from homology;
DR   PRODOM; C5DCN7.
DR   SWISS-2DPAGE; C5DCN7.
KW   Allosteric enzyme {ECO:0000256|HAMAP-Rule:MF_03184};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_03184,
KW   ECO:0000256|PIRNR:PIRNR000533};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002036};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03184};
KW   Glycolysis {ECO:0000256|HAMAP-Rule:MF_03184,
KW   ECO:0000256|PIRNR:PIRNR000533};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_03184,
KW   ECO:0000256|PIRNR:PIRNR000533};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_03184};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_03184};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03184,
KW   ECO:0000256|PIRNR:PIRNR000533};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002036};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_03184,
KW   ECO:0000256|PIRNR:PIRNR000533}.
FT   DOMAIN        8     99       Pfk_N. {ECO:0000259|Pfam:PF18468}.
FT   DOMAIN      198    504       PFK. {ECO:0000259|Pfam:PF00365}.
FT   DOMAIN      586    876       PFK. {ECO:0000259|Pfam:PF00365}.
FT   NP_BIND     269    270       ATP. {ECO:0000256|HAMAP-Rule:MF_03184}.
FT   NP_BIND     299    302       ATP. {ECO:0000256|HAMAP-Rule:MF_03184}.
FT   REGION        1    571       N-terminal catalytic PFK domain 1.
FT                                {ECO:0000256|HAMAP-Rule:MF_03184}.
FT   REGION      345    347       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_03184}.
FT   REGION      389    391       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_03184}.
FT   REGION      479    482       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_03184}.
FT   REGION      572    585       Interdomain linker. {ECO:0000256|HAMAP-
FT                                Rule:MF_03184}.
FT   REGION      586    975       C-terminal regulatory PFK domain 2.
FT                                {ECO:0000256|HAMAP-Rule:MF_03184}.
FT   REGION      713    717       Allosteric activator fructose 2,6-
FT                                bisphosphate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_03184}.
FT   REGION      758    760       Allosteric activator fructose 2,6-
FT                                bisphosphate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_03184}.
FT   REGION      850    853       Allosteric activator fructose 2,6-
FT                                bisphosphate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_03184}.
FT   ACT_SITE    347    347       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_03184}.
FT   METAL       300    300       Magnesium; catalytic. {ECO:0000256|HAMAP-
FT                                Rule:MF_03184}.
FT   BINDING     206    206       ATP; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_03184}.
FT   BINDING     382    382       Substrate; shared with dimeric partner.
FT                                {ECO:0000256|HAMAP-Rule:MF_03184}.
FT   BINDING     446    446       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_03184}.
FT   BINDING     473    473       Substrate; shared with dimeric partner.
FT                                {ECO:0000256|HAMAP-Rule:MF_03184}.
FT   BINDING     656    656       Allosteric activator fructose 2,6-
FT                                bisphosphate. {ECO:0000256|HAMAP-Rule:
FT                                MF_03184}.
FT   BINDING     751    751       Allosteric activator fructose 2,6-
FT                                bisphosphate; shared with dimeric
FT                                partner. {ECO:0000256|HAMAP-Rule:
FT                                MF_03184}.
FT   BINDING     818    818       Allosteric activator fructose 2,6-
FT                                bisphosphate. {ECO:0000256|HAMAP-Rule:
FT                                MF_03184}.
FT   BINDING     844    844       Allosteric activator fructose 2,6-
FT                                bisphosphate; shared with dimeric
FT                                partner. {ECO:0000256|HAMAP-Rule:
FT                                MF_03184}.
FT   BINDING     942    942       Allosteric activator fructose 2,6-
FT                                bisphosphate. {ECO:0000256|HAMAP-Rule:
FT                                MF_03184}.
SQ   SEQUENCE   975 AA;  106984 MW;  651B00410A95AB3C CRC64;
     MTQETVYGVA FRSVATADES AYRSAIKFYH KLGFSTVKTY DKFRGNKEAA TSGTAQGSVK
     ETWLESFKLS EVDSNGFRIP QQEATNHEQS DGALLKIRLV AHQPLEAKNS RVTYYSASID
     EVSKAFPDAK KLENGEYALN DPLGYELRLS GYVRAGDKKT VDKEFFLDES KTPADYLKGQ
     NLSPNQIPGA TSTGIKKKIA VMTSGGDSPG MNSAVRAVVR AGIYYGCDVF AVYEGYEGLL
     KGGDLLKKME WKDVRGWLSE GGTLIGTARC MEFRERWGRK QAAGNLISEG IDALVVCGGD
     GSLTGADLFR SEWPSLVEEL VKDGKFTEKQ VEPYRNLKIV GLVGSIDNDM SGTDSTIGAY
     SALERICEMV DYIDATAKSH SRAFVVEVMG RHCGWLALMA GIATGADYIF VPERAAPAGK
     WQEELKKVCQ AHREKGRRNN TVIVAEGALD NNLKPITSEQ VKDALVELGL DTKITTLGHV
     QRGGTAVAHD RWLATLQGVD AVKAVLEMTP ETPSPLIGIL ENKIIRMPLM ESVKLTKSVA
     EAIENKDFDK AISLRDTEFI ELYENFISTT VKDDGSERLP EDQRLNIAIV HVGAPSAALN
     AATRAATLYC LSRGHKPSAI LNGFSGLIQT GEIKELSWID VENWHNLGGS EIGTNRSVAS
     EDMGSIAYHF QKNKFDGVII LGGFEGFKSL KELRDARAQY PIFNIPMVLI PSTVSNNVPG
     TEYSLGVDTC LNTLVNYTDA IKQSASATRR RVFVVEVQGG HSGYIASFTG LVTGAVSVYT
     PEDQIDLKSI REDLALLKEN FRHDQGETRN GKLVIRNEQA SSIYTTDLLA DIIAEASSGK
     FGVRTAIPGH VQQGGVPSSK DRVTGSRYAV KCVKFIEAWN RKNSDEQNED FKILRFKYVN
     GVKEYTIQDE DASAAIIAVN GSHISFKPIA RLWEEETNVE LRKGQEVHWE EFNKIGDILS
     GRLNLRKEVD AGKSA
//

If you have problems or comments...

PBIL Back to PBIL home page