ID A0A183QNA4_9TREM Unreviewed; 443 AA.
AC A0A183QNA4;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=6-phosphofructokinase {ECO:0000256|ARBA:ARBA00012055};
DE EC=2.7.1.11 {ECO:0000256|ARBA:ARBA00012055};
OS Schistosoma rodhaini.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX NCBI_TaxID=6188 {ECO:0000313|WBParaSite:SROB_0000513901-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:SROB_0000513901-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (JUN-2016) 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 STRING; 6188.A0A183QNA4; -.
DR WBParaSite; SROB_0000513901-mRNA-1; SROB_0000513901-mRNA-1; SROB_0000513901.
DR UniPathway; UPA00109; UER00182.
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; -; 1.
DR Gene3D; 3.40.50.460; Phosphofructokinase domain; 1.
DR InterPro; IPR022953; ATP_PFK.
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; 1.
DR PRINTS; PR00476; PHFRCTKINASE.
DR SUPFAM; SSF53784; Phosphofructokinase; 1.
PE 4: Predicted;
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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 40..342
FT /note="Phosphofructokinase"
FT /evidence="ECO:0000259|Pfam:PF00365"
SQ SEQUENCE 443 AA; 49776 MW; F032D36CDD112CD7 CRC64;
MVFKXXXXXX XXXXXXIHHT QLFQVYESIV RFLTFQNNLR IGIVNVGAPA CGINAVIRGF
TRLGITKGYK IIGIHEGFSG LVKGDASEIQ WADVRGWVGM GGSMLGTRRY VIFCFHFYTL
FQLSRDTPNG LGIDKVAAKF KEFKLSGLLI IGGFEAYECM IELVEGREKY PELCIPMAMV
PATISNNVPG TDFSLGCDTA LNEITSVLDK IKQSALGTKR RVFVVETMGG YCGYLATMSA
LAGGADAAYI FEEPFTIDDL REDVVHLRAK IDDNVKRGLV LRAEYANKYY TSEFIHQLYA
QEGQGIFDCR CNVLGHMQQG DRPSPFDRSL GTKFASKAID WLDEQINANI RSDCKLHIVF
YTPGHLCCTL IGIVRRQTTY SNIMELREHT DFVHRLPKEE WWLSLRPLMR IMAKHDSLYE
SESIMSGESS LSLSNCSHIA TRI
//
