ID   Q6FQJ7_CANGA            Unreviewed;       957 AA.
AC   Q6FQJ7;
DT   19-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   19-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 116.
DE   RecName: Full=6-phosphofructokinase {ECO:0000256|ARBA:ARBA00012055, ECO:0000256|PIRNR:PIRNR000533};
DE            EC=2.7.1.11 {ECO:0000256|ARBA:ARBA00012055, ECO:0000256|PIRNR:PIRNR000533};
DE   AltName: Full=Phosphohexokinase {ECO:0000256|PIRNR:PIRNR000533};
GN   OrderedLocusNames=CAGL0I05698g {ECO:0000313|EMBL:CAG60434.1};
OS   Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 /
OS   NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces.
OX   NCBI_TaxID=284593 {ECO:0000313|EMBL:CAG60434.1, ECO:0000313|Proteomes:UP000002428};
RN   [1] {ECO:0000313|EMBL:CAG60434.1, ECO:0000313|Proteomes:UP000002428}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65
RC   {ECO:0000313|Proteomes:UP000002428};
RX   PubMed=15229592; DOI=10.1038/nature02579;
RG   Genolevures;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.F., Straub M.L.,
RA   Suleau A., Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E.,
RA   Wirth B., Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   Wincker P., Souciet J.L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 1,6-
CC         bisphosphate + H(+); Xref=Rhea:RHEA:16109, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:32966, ChEBI:CHEBI:57634,
CC         ChEBI:CHEBI:456216; EC=2.7.1.11;
CC         Evidence={ECO:0000256|ARBA:ARBA00000432,
CC         ECO:0000256|PIRNR:PIRNR000533};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC       phosphate and glycerone phosphate from D-glucose: step 3/4.
CC       {ECO:0000256|ARBA:ARBA00004679, ECO:0000256|PIRNR:PIRNR000533}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) family.
CC       ATP-dependent PFK group I subfamily. Eukaryotic two domain clade "E"
CC       sub-subfamily. {ECO:0000256|PIRNR:PIRNR000533}.
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DR   EMBL; CR380955; CAG60434.1; -; Genomic_DNA.
DR   RefSeq; XP_447497.1; XM_447497.1.
DR   AlphaFoldDB; Q6FQJ7; -.
DR   STRING; 284593.Q6FQJ7; -.
DR   GeneID; 2889342; -.
DR   KEGG; cgr:CAGL0I05698g; -.
DR   eggNOG; KOG2440; Eukaryota.
DR   HOGENOM; CLU_011053_0_0_1; -.
DR   InParanoid; Q6FQJ7; -.
DR   OMA; CIATRES; -.
DR   UniPathway; UPA00109; UER00182.
DR   Proteomes; UP000002428; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0003872; F:6-phosphofructokinase activity; IEA:UniProtKB-EC.
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   Gene3D; 3.40.50.450; -; 2.
DR   Gene3D; 3.10.180.10; 2,3-Dihydroxybiphenyl 1,2-Dioxygenase, domain 1; 1.
DR   Gene3D; 3.40.50.460; Phosphofructokinase domain; 2.
DR   InterPro; IPR009161; 6-Pfructokinase_euk.
DR   InterPro; IPR022953; ATP_PFK.
DR   InterPro; IPR029068; Glyas_Bleomycin-R_OHBP_Dase.
DR   InterPro; IPR015912; Phosphofructokinase_CS.
DR   InterPro; IPR000023; Phosphofructokinase_dom.
DR   InterPro; IPR035966; PKF_sf.
DR   NCBIfam; TIGR02478; 6PF1K_euk; 1.
DR   PANTHER; PTHR13697:SF4; ATP-DEPENDENT 6-PHOSPHOFRUCTOKINASE; 1.
DR   PANTHER; PTHR13697; PHOSPHOFRUCTOKINASE; 1.
DR   Pfam; PF00365; PFK; 2.
DR   PIRSF; PIRSF000533; ATP_PFK_euk; 1.
DR   PRINTS; PR00476; PHFRCTKINASE.
DR   SUPFAM; SSF54593; Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase; 1.
DR   SUPFAM; SSF53784; Phosphofructokinase; 2.
DR   PROSITE; PS00433; PHOSPHOFRUCTOKINASE; 2.
PE   3: Inferred from homology;
KW   Allosteric enzyme {ECO:0000256|ARBA:ARBA00022533};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR000533};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|PIRNR:PIRNR000533};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR000533};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|PIRNR:PIRNR000533};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002428};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000533}.
FT   DOMAIN          197..503
FT                   /note="Phosphofructokinase"
FT                   /evidence="ECO:0000259|Pfam:PF00365"
FT   DOMAIN          584..875
FT                   /note="Phosphofructokinase"
FT                   /evidence="ECO:0000259|Pfam:PF00365"
SQ   SEQUENCE   957 AA;  105268 MW;  D8063D838A39D772 CRC64;
     MVKNSMVHGV TRVDLTAYSA ESFENAIQFY LAFLVLDELD QNEDGGVVLA NSHVYIKISY
     KEDGEMERKV NDRLMNLIEK TTSGDWRAVS SNVLVYTVDD IGLVKETLKR IGLPHQAYPT
     ELTPAQIYTL DPLGNVVGFT GNKLAIATEI PFVLPTEEDD ESELSSKESS YTNLTSLMRT
     TSGYPSLPFG HSRTHRNIAI LTSGGDAPGM NSVIRAVVRT ALFKGCRVYI VREGLEGLVK
     GYIEEFFWED VGGWNSQGGT NIGTAKSNAF LQRRGRLLAA RNLIIHDIDS LIVCGGDGSL
     AAADIFKHEW HSLISELLSS HLIKIEQLHS HKHLTICGIS ASIDNDIPVT DASIGAYSAL
     DRICKALDYI QVTAESTSRA YVVEIMGGNC GWLTLLAGIA TAADYIFLPE CPQQKEDWRT
     HLQRIVKRNR RNGRRNTLVL LCEGAVAADS TPITSRDVHQ VLSEELDIDT RITVLGHVQR
     GGAPVAYDRI LATLQGVEAV SVILESTPDT PSYLIAVKEN KILRKDLQDA VRQTFKISTS
     LKDREFEKAF RAKEAEFIEH YHNFLAINAA DQDKKLVKSA SLLNIAIINI GAPAGGMNSA
     VYAMASYCMW KGHRPIAIYN GWSGLARHES IRSLKWSEIV GWQSRGGSEI GTNRETPNEA
     DVGMIAYYFQ KYKIDGLIIV GGFEGFESLR QLEKARELFP AFRIPMVLIP ATLSNNVPGT
     EYSLGSDTAL NSLTEFCDNI GISSAATKDK AYVVEVQGGN SGYLATLTSI AIGACATYVP
     EEGISLVQLS EDIETISKSF DCVQTGDHAG KIILKSQNAS KAMSAEKLAN IITEEAAGKF
     EAKSVIPGHL QQGGTPSPID RTRATKLAIR AVDFILEKSK VLKSQDDVIY EHTKELTESA
     VVLGVKGSNI LFTSVKQLYL FETNVRDRMP KVIHWDGIRT LSDHMAGRRR IYEDEDN
//