ID   PFKA2_CANAX             Reviewed;         946 AA.
AC   O94200;
DT   16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   27-MAR-2024, entry version 102.
DE   RecName: Full=ATP-dependent 6-phosphofructokinase subunit beta {ECO:0000255|HAMAP-Rule:MF_03184};
DE            EC=2.7.1.11 {ECO:0000255|HAMAP-Rule:MF_03184};
DE   AltName: Full=ATP-dependent 6-phosphofructokinase 2 {ECO:0000255|HAMAP-Rule:MF_03184};
DE            Short=ATP-PFK 2 {ECO:0000255|HAMAP-Rule:MF_03184};
DE            Short=Phosphofructokinase 2 {ECO:0000255|HAMAP-Rule:MF_03184};
DE   AltName: Full=Phosphohexokinase 2 {ECO:0000255|HAMAP-Rule:MF_03184};
GN   Name=PFK2;
OS   Candida albicans (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=5476;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RC   STRAIN=ATCC 10231 / CBS 6431 / CIP 48.72 / DSM 1386 / NBRC 1594;
RX   PubMed=10091602; DOI=10.1046/j.1432-1327.1999.00132.x;
RA   Lorberg A., Kirchrath L., Ernst J.F., Heinisch J.J.;
RT   "Genetic and biochemical characterization of phosphofructokinase from the
RT   opportunistic pathogenic yeast Candida albicans.";
RL   Eur. J. Biochem. 260:217-226(1999).
CC   -!- FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate to
CC       fructose 1,6-bisphosphate by ATP, the first committing step of
CC       glycolysis.
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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_03184};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_03184};
CC   -!- ACTIVITY REGULATION: Allosterically activated by ADP, AMP, or fructose
CC       2,6-bisphosphate, and allosterically inhibited by ATP or citrate.
CC       {ECO:0000255|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:0000255|HAMAP-Rule:MF_03184}.
CC   -!- SUBUNIT: Heterooctamer of 4 alpha and 4 beta chains.
CC       {ECO:0000255|HAMAP-Rule:MF_03184}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03184}.
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:0000255|HAMAP-Rule:MF_03184}.
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DR   EMBL; AJ007637; CAB38867.1; -; Genomic_DNA.
DR   AlphaFoldDB; O94200; -.
DR   SMR; O94200; -.
DR   VEuPathDB; FungiDB:C7_01800C_A; -.
DR   VEuPathDB; FungiDB:CAWG_05531; -.
DR   UniPathway; UPA00109; UER00182.
DR   GO; GO:0005945; C:6-phosphofructokinase complex; IEA:EnsemblFungi.
DR   GO; GO:0005739; C:mitochondrion; IEA:EnsemblFungi.
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:0003729; F:mRNA binding; IEA:EnsemblFungi.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:EnsemblFungi.
DR   GO; GO:0006002; P:fructose 6-phosphate metabolic process; IEA:EnsemblFungi.
DR   GO; GO:0007035; P:vacuolar acidification; IEA:EnsemblFungi.
DR   GO; GO:0070072; P:vacuolar proton-transporting V-type ATPase complex assembly; IEA:EnsemblFungi.
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   HAMAP; MF_03184; Phosphofructokinase_I_E; 1.
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   1: Evidence at protein level;
KW   Allosteric enzyme; ATP-binding; Cytoplasm; Glycolysis; Kinase; Magnesium;
KW   Metal-binding; Nucleotide-binding; Transferase.
FT   CHAIN           1..946
FT                   /note="ATP-dependent 6-phosphofructokinase subunit beta"
FT                   /id="PRO_0000112039"
FT   REGION          1..559
FT                   /note="N-terminal catalytic PFK domain 1"
FT   REGION          560..573
FT                   /note="Interdomain linker"
FT   REGION          574..946
FT                   /note="C-terminal regulatory PFK domain 2"
FT   ACT_SITE        334
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT   BINDING         192
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT   BINDING         256..257
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT   BINDING         286..289
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT   BINDING         287
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT   BINDING         332..334
FT                   /ligand="beta-D-fructose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57634"
FT                   /ligand_label="2"
FT                   /ligand_note="ligand shared with subunit alpha"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT   BINDING         369
FT                   /ligand="beta-D-fructose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57634"
FT                   /ligand_label="1"
FT                   /ligand_note="ligand shared with subunit alpha"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT   BINDING         376..378
FT                   /ligand="beta-D-fructose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57634"
FT                   /ligand_label="2"
FT                   /ligand_note="ligand shared with subunit alpha"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT   BINDING         433
FT                   /ligand="beta-D-fructose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57634"
FT                   /ligand_label="2"
FT                   /ligand_note="ligand shared with subunit alpha"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT   BINDING         461
FT                   /ligand="beta-D-fructose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57634"
FT                   /ligand_label="1"
FT                   /ligand_note="ligand shared with subunit alpha"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT   BINDING         467..470
FT                   /ligand="beta-D-fructose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57634"
FT                   /ligand_label="2"
FT                   /ligand_note="ligand shared with subunit alpha"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT   BINDING         644
FT                   /ligand="beta-D-fructose 2,6-bisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58579"
FT                   /ligand_label="2"
FT                   /ligand_note="allosteric activator; ligand shared with
FT                   subunit alpha"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT   BINDING         702..706
FT                   /ligand="beta-D-fructose 2,6-bisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58579"
FT                   /ligand_label="2"
FT                   /ligand_note="allosteric activator; ligand shared with
FT                   subunit alpha"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT   BINDING         747..749
FT                   /ligand="beta-D-fructose 2,6-bisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58579"
FT                   /ligand_label="2"
FT                   /ligand_note="allosteric activator; ligand shared with
FT                   subunit alpha"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT   BINDING         833
FT                   /ligand="beta-D-fructose 2,6-bisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58579"
FT                   /ligand_label="1"
FT                   /ligand_note="allosteric activator; ligand shared with
FT                   subunit alpha"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT   BINDING         839..842
FT                   /ligand="beta-D-fructose 2,6-bisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58579"
FT                   /ligand_label="2"
FT                   /ligand_note="allosteric activator; ligand shared with
FT                   subunit alpha"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT   BINDING         920
FT                   /ligand="beta-D-fructose 2,6-bisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58579"
FT                   /ligand_label="2"
FT                   /ligand_note="allosteric activator; ligand shared with
FT                   subunit alpha"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
SQ   SEQUENCE   946 AA;  104046 MW;  AEF6167A741D8672 CRC64;
     MISIVNGTST LSLVAGSVET LNQAINFYTN ILGLSVHSEQ NDWTYLSNDD NKMIVKIQLD
     TKSGLSLDQV NDRRTEIIAK LNVTDWRSLD TTSVLKVQNL VALIETLTTF NYTLQITPNE
     LYPNEVYCVG PIGYIIGFTA CDEPLTLVPP LQKSHPKPGL VSNLMSKSGS QSRNIEETKA
     VRRNIAVMTS GGDSQGMNAA VRAVVRATIF HGSKAFAVQE GYAGLVKGGP EYIKEMKWQD
     VRGFLSEGGT NIGTARCMEF KERWGRLKGC KNLIDAGIDG LIVCGGDGSL TGADLFRHEW
     PSLIQELKDK GEITNEQFER HKHLYICGMV GSIDNDMAMT DATIGGYSAL ERICRAIDYI
     DATANSHSRA FVVEVMGRHC GWLALMAGIA TSADYIFIPE KPASSKDWQD QMCDIVGKHR
     AQGKRKTIVI VAEGAITSDL KPITSDEVKD VLVDRLGLDT RITVLGHVQR GGTAVAFDRT
     LATLQGVEAV KAILELTPDV PSPLIAIDEN KICRRPLVEA VRITKSVASA IEAKDFEKAM
     SLRDHEFKEH LANFMAMNTA NHEKPTLPRE KRKKIAIINI GAPAGGMNSA VYAMATYCMS
     RGHTPYAIHN GFAGLSRHES VKSIEWIDIE GWNSIGGSEI GTNRQTPEET DIGMIAHYFE
     KYQFDGLIIV GGFEAFVSLE QLERSRAMYP SFRIPMVLIP ATISNNVPGT EYSLGADTCL
     NSLMEYCDIV KQSASATRGT AFIIDVQGGN SGYIATFASL ISGAQASYVP EEGISLQQLE
     MDINSLREAF AVEQGMTKSG KLIIKSSNAS KVLTPHTLAD IFNDECHGDF DTKTAIPGHV
     QQGGLPSPID RSRGDRFAIR AVQFIEDHCD VLAPYRYELD FPIDDKKILN TAAVLGIKSS
     RLRFTSIRHL FDFETELGRR MPKTIYWNTI RDISDQLVGR TRLDKP
//