ID S7WAX1_SPRLO Unreviewed; 1000 AA.
AC S7WAX1;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=6-phosphofructokinase {ECO:0000256|ARBA:ARBA00012055};
DE EC=2.7.1.11 {ECO:0000256|ARBA:ARBA00012055};
GN ORFNames=SLOPH_1429 {ECO:0000313|EMBL:EPR80071.1};
OS Spraguea lophii (strain 42_110) (Microsporidian parasite).
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Spraguidae;
OC Spraguea.
OX NCBI_TaxID=1358809 {ECO:0000313|EMBL:EPR80071.1, ECO:0000313|Proteomes:UP000014978};
RN [1] {ECO:0000313|Proteomes:UP000014978}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=42_110 {ECO:0000313|Proteomes:UP000014978};
RX PubMed=23990793; DOI=10.1371/journal.pgen.1003676;
RA Campbell S.E., Williams T.A., Yousuf A., Soanes D.M., Paszkiewicz K.H.,
RA Williams B.A.P.;
RT "The genome of Spraguea lophii and the basis of host-microsporidian
RT interactions.";
RL PLoS Genet. 9:E1003676-E1003676(2013).
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 -!- 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}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EPR80071.1}.
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DR EMBL; ATCN01000021; EPR80071.1; -; Genomic_DNA.
DR AlphaFoldDB; S7WAX1; -.
DR STRING; 1358809.S7WAX1; -.
DR VEuPathDB; MicrosporidiaDB:SLOPH_1429; -.
DR HOGENOM; CLU_011053_2_0_1; -.
DR InParanoid; S7WAX1; -.
DR OMA; EWQDQMC; -.
DR OrthoDB; 374214at2759; -.
DR UniPathway; UPA00109; UER00182.
DR Proteomes; UP000014978; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0003872; F:6-phosphofructokinase activity; IEA:InterPro.
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; -; 3.
DR Gene3D; 3.40.50.460; Phosphofructokinase domain; 3.
DR InterPro; IPR022953; ATP_PFK.
DR InterPro; IPR015912; Phosphofructokinase_CS.
DR InterPro; IPR000023; Phosphofructokinase_dom.
DR InterPro; IPR035966; PKF_sf.
DR PANTHER; PTHR13697:SF4; ATP-DEPENDENT 6-PHOSPHOFRUCTOKINASE; 1.
DR PANTHER; PTHR13697; PHOSPHOFRUCTOKINASE; 1.
DR Pfam; PF00365; PFK; 2.
DR PRINTS; PR00476; PHFRCTKINASE.
DR SUPFAM; SSF53784; Phosphofructokinase; 2.
DR PROSITE; PS00433; PHOSPHOFRUCTOKINASE; 1.
PE 4: Predicted;
KW Allosteric enzyme {ECO:0000256|ARBA:ARBA00022533};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Glycolysis {ECO:0000256|ARBA:ARBA00023152};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EPR80071.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000014978};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 104..404
FT /note="Phosphofructokinase"
FT /evidence="ECO:0000259|Pfam:PF00365"
FT DOMAIN 557..904
FT /note="Phosphofructokinase"
FT /evidence="ECO:0000259|Pfam:PF00365"
SQ SEQUENCE 1000 AA; 112297 MW; 7BEDD553D1779D94 CRC64;
MYVSVKELIL KSEKATLNSC LLYERLGLIA TFDPSDPSIK VSSCEDAAII SVDTSINIEI
YSKKHLNQLI EDGFFKADDD KVTILDDVGN KLLVSFNPKK SLKRIAVLTS GGDAPGMNSA
IRAIIRTGIK WGSKVYGVFC GYEGLIEDMI EELEWDRLNK HACDGGTFLQ SARSKRFMAR
EGRKQAVFNL VKRNIGGLIV IGGDGSLTGA LILKNEFKGF VNELIAEGKL EKDSVDEDLS
IITIPASIDN DIPLADTTIG SDSALHRVIE SVDTLTTTME SHRRAIVIEV MGRHCGWIAL
MSAVATAADY VFLPERPADW KTESVNAIKK ARKFGKRGVF LVLSEGAVDI NGEIIKPEEV
KSLLEKNDIE TRILRLGHLQ RGGAPSAFDR IQATLLGCKA VEILLTRYNI EPIMMADQKG
EIKAVPLIEV IKKCEEQDKK RLSKSFDFLF DSRNSFFKKT YQLSEKLRKG SKAQFQLDSK
IPQSSSSHYA QDMGEDRKTE ILQNNTKDKE CTGIENININ EINANNKDIE KQENNEFTTK
TDNEPFTTQS NIYKKKRIAI LHEGKRAGGM NVALNAIVQY GLSCDQEIIV ITDGFDGLVN
NQIVESHQYE FISGIHDGGS LIGSSPSNID SIENIYYKLI EHRIDSLIVV GGYESLVALY
NIQKIMENKF KDENEKDENY TPKGNNTKHN KALKNDKDLH LKKMIDLILI PSTTDNNIPL
TDITIGSDTA LNTIMRSCDY LKLSTISMKQ SVFIVEVGGE NCGYLSLMSG IASGALEAFI
PERKYMISHL SEIAQRLRHR FKNKKDLNVC NIKNDENTEK KNEELVNKKT NINSLKRNGV
LLIRNENTFN KIDTKSLGKI LSTDSSDRFN TKFCVLGYLQ RGGNPSPIDR VFSTIFGVEA
IDLLLEKEEY QNVESIEKEK NIREIETMNG NRKHNDKDVK NNDGYNNSLG IKNINGMVGI
NQQDITFSSL EKVMERFDIK KKRDKNPKWL VYSNICRSWE
//
