ID A0A0R3RFF3_9BILA Unreviewed; 1074 AA.
AC A0A0R3RFF3;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=6-phosphofructokinase {ECO:0000256|ARBA:ARBA00012055};
DE EC=2.7.1.11 {ECO:0000256|ARBA:ARBA00012055};
OS Elaeophora elaphi.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Elaeophora.
OX NCBI_TaxID=1147741 {ECO:0000313|Proteomes:UP000050640, ECO:0000313|WBParaSite:EEL_0000008701-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:EEL_0000008701-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
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}.
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DR AlphaFoldDB; A0A0R3RFF3; -.
DR STRING; 1147741.A0A0R3RFF3; -.
DR WBParaSite; EEL_0000008701-mRNA-1; EEL_0000008701-mRNA-1; EEL_0000008701.
DR UniPathway; UPA00109; UER00182.
DR Proteomes; UP000050640; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; 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:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.40.50.460; Phosphofructokinase domain; 2.
DR InterPro; IPR009161; 6-Pfructokinase_euk.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR022953; ATP_PFK.
DR InterPro; IPR027417; P-loop_NTPase.
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; PF00005; ABC_tran; 1.
DR Pfam; PF00365; PFK; 2.
DR PRINTS; PR00476; PHFRCTKINASE.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF53784; Phosphofructokinase; 2.
DR PROSITE; PS00433; PHOSPHOFRUCTOKINASE; 2.
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};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 91..109
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 181..296
FT /note="ABC transporter"
FT /evidence="ECO:0000259|Pfam:PF00005"
FT DOMAIN 338..640
FT /note="Phosphofructokinase"
FT /evidence="ECO:0000259|Pfam:PF00365"
FT DOMAIN 721..1005
FT /note="Phosphofructokinase"
FT /evidence="ECO:0000259|Pfam:PF00365"
SQ SEQUENCE 1074 AA; 119099 MW; 54E6BE9C24B9CEEA CRC64;
MIGAVAVSIV EKASGRDTAN TLSIIWSLFF PTYNLSLCFS KAYTNEHTRE ACTIVDCSIE
EMHKIAKECC GNNDERLYID NMLLNTGKMG MALMVVFLLL HSIIFWFAIA ASEANFVRII
KRWLQKDAKA NRKIASIETF ESCCEDTDVL MEKEKVSKMK NSDSLVVARN LEKWYGKLNA
VKKINFHVAK GECFGLLGVN GAGKTTTFQM LTGESVSCAG DVYIHGFNIQ TEWRKAYDHI
GYCPQFDAII GEMTGQETLQ LFARLRGIRE CDVTRVTDSM IHAVALDKYK NNLIKTYSEL
PDLLASDFDS EIQFQIKSVN GHEGSVMKKG KYKGQIMGLF TSGGDAPGMN SAVRAIVRVG
LYLGARVFCI HEGYQGMVDG GKFIREATWE TVSDIIQKGG TLIGSARCKD FRERSGRLKA
AQNLIQHGIT SLVCIGGDGS LTGANTFRNE WPGLVTELLN AKVISKEDAE KCKSIQIVGI
VGSIDNDFCG TDMTIGTDTA LHRITEAVDS VRSTAHSHQR CFVIEVMGRN CGYLAVAASL
ALDADFCFIP EWPPPTHWQD VLCKKLKQMR EDGNRVNIVI VAEGAIDHNG SAITSNMIQD
VIKKNMKYDT RITILGHIQR GGSPSVFDRL LGCRMGAEAT IALMEMNDES EPCVVSIDGN
QMVRIPLMKC VQRTKAVKTA MDKKDWAMAL RLRGRSFRRN VEMYRTLSKI RRHEAASEGF
NIAIMNVGSP CAGCNAAVMS CVRTAILQGC IPYCIYNSNE GLASGQIQRM EWNDVALWSA
EGGSFLGSQP ALPNDDTLPL MAKNLLRFNI NSLIIIGGFN AYHTCLIFAQ NRAKFPPFRI
PMCVIPSTIN NNVPGTAFTI GADTSLNEIC KMIDKIKQSA TGSKRRVFVI ETMGNYCGYL
ATLSAMASGA DAAYIYEEIF NVHELINDIR VIAEKMKTGA QRYLIVRNEK ASENYTSEFI
RQLFTEEGKG IFTTRTNVLG HTQQGGNPSP FDRLFAAKMG ARAVVHLLGQ MKEFKKTNLC
HPGTATLQGL IGKYVCLTPV EELMKDADFA HRLPVEQWWM KLRPLLRILA KHDF
//
