ID A0A077Z464_TRITR Unreviewed; 767 AA.
AC A0A077Z464;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=6-phosphofructokinase {ECO:0000256|ARBA:ARBA00012055, ECO:0000256|PIRNR:PIRNR000533};
DE EC=2.7.1.11 {ECO:0000256|ARBA:ARBA00012055, ECO:0000256|PIRNR:PIRNR000533};
DE AltName: Full=Phosphohexokinase {ECO:0000256|PIRNR:PIRNR000533};
GN ORFNames=TTRE_0000311601 {ECO:0000313|EMBL:CDW54846.1};
OS Trichuris trichiura (Whipworm) (Trichocephalus trichiurus).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichuridae; Trichuris.
OX NCBI_TaxID=36087 {ECO:0000313|EMBL:CDW54846.1};
RN [1] {ECO:0000313|EMBL:CDW54846.1}
RP NUCLEOTIDE SEQUENCE.
RA Aslett M.;
RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CDW54846.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Foth B.J., Tsai I.J., Reid A.J., Bancroft A.J., Nichol S., Tracey A.,
RA Holroyd N., Cotton J.A., Stanley E.J., Zarowiecki M., Liu J.Z.,
RA Huckvale T., Cooper P.J., Grencis R.K., Berriman M.;
RT "The whipworm genome and dual-species transcriptomics of an intimate host-
RT pathogen interaction.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000256|ARBA:ARBA00002659}.
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 ECO:0000256|PIRNR:PIRNR000533};
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, ECO:0000256|PIRNR:PIRNR000533}.
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:0000256|PIRNR:PIRNR000533}.
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DR EMBL; HG805919; CDW54846.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A077Z464; -.
DR STRING; 36087.A0A077Z464; -.
DR UniPathway; UPA00109; UER00182.
DR GO; GO:0005737; C:cytoplasm; 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: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; 3.40.50.460; Phosphofructokinase domain; 2.
DR InterPro; IPR009161; 6-Pfructokinase_euk.
DR InterPro; IPR022953; ATP_PFK.
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, MUSCLE TYPE; 1.
DR PANTHER; PTHR13697; PHOSPHOFRUCTOKINASE; 1.
DR Pfam; PF00365; PFK; 2.
DR PIRSF; PIRSF000533; ATP_PFK_euk; 1.
DR PRINTS; PR00476; PHFRCTKINASE.
DR SUPFAM; SSF53784; Phosphofructokinase; 2.
DR PROSITE; PS00433; PHOSPHOFRUCTOKINASE; 2.
PE 3: Inferred from homology;
KW Allosteric enzyme {ECO:0000256|ARBA:ARBA00022533};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR000533};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|PIRNR:PIRNR000533};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR000533};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR000533};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000533}.
FT DOMAIN 13..318
FT /note="Phosphofructokinase"
FT /evidence="ECO:0000259|Pfam:PF00365"
FT DOMAIN 406..689
FT /note="Phosphofructokinase"
FT /evidence="ECO:0000259|Pfam:PF00365"
SQ SEQUENCE 767 AA; 84520 MW; 0CD551FE4C16C727 CRC64;
MENGEEKVRE RSMGVFTSGG DAAGMNAALR AVTRVGISNG YRVFLIHEGY QGMVDGGDYF
EEASWNSVSD VIQYSGTIIG SARCKAFMTV EGRQKAVENL VIHGITDLVC IGGDGSLTGL
NILRQEWAGH LKKLIELKRL EKAQVDLLGE LRIVGLVGSI DNDFCGTDMT IGVDSALNRI
VESIDAVAST AQSHQRTFVI EVMGRRCGYL ALIASIVSEA DWVFTPEWPV PENWPDLLCK
KLKESRDYGQ RVNIIICSEG ATDQTGKAIS SEQVRQVVHD RLRYDTRVTV LGHVQRGGVP
SAFDRLLASR MGADAVLALM DAKKATDENE PVVITLDGNV LVRRSLTKCV EQTLEVKAAL
DAKDWKRAIE LRGKTFQRNF EAYNLLSKMH PPVDKQNLSG GLKFNLAVMN VGSPSCGMNA
AVRCFVRMGL YHGCKVYAIK DSFQGLIKGK LTEMSWHSVI DWTRYGGSFL GSQKSLPSMN
MPAVAEQLGR YKINALLLVG GFEAYHACIE LTENRHQFKE FCIPMAVIPC TISNNVPGAN
YSIGSDTALN VICSMVDKLK QSARGTKHRV FIVETMGGYC GYLATLAGLA SGADNAYIFE
QTFGVDDIKN DVKAIAQKMD KGVQRYIVTR CENANMHYTT EFMRQLFSEE GKGQFSTRIN
VLGHAQQGGN ASPFDRLMAT RMAIHVAQVL VSMAREVAAE DGSVYTDNPN TALLLGVLHR
HAQLTPVLEL KERTDFAHRL PMDQWWLKLH PLLRLLAAYK STYATSA
//