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Database: UniProt
Entry: A0A077Z464_TRITR
LinkDB: A0A077Z464_TRITR
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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
//
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