PFKA2_CANAX
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 03-AUG-2022, entry version 98.
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;
CC Evidence={ECO:0000255|HAMAP-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 PRIDE; 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:0003872; F:6-phosphofructokinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0070095; F:fructose-6-phosphate binding; IEA:EnsemblFungi.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030388; P:fructose 1,6-bisphosphate metabolic process; IEA:EnsemblFungi.
DR GO; GO:0006002; P:fructose 6-phosphate metabolic process; IEA:EnsemblFungi.
DR Gene3D; 3.10.180.10; -; 1.
DR Gene3D; 3.40.50.460; -; 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 Pfam; PF00365; PFK; 2.
DR PIRSF; PIRSF000533; ATP_PFK_euk; 1.
DR PRINTS; PR00476; PHFRCTKINASE.
DR SUPFAM; SSF53784; SSF53784; 2.
DR SUPFAM; SSF54593; SSF54593; 1.
DR TIGRFAMs; TIGR02478; 6PF1K_euk; 1.
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
