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Database: UniProt
Entry: A0A1L8GZG6_XENLA
LinkDB: A0A1L8GZG6_XENLA
Original site: A0A1L8GZG6_XENLA 
ID   A0A1L8GZG6_XENLA        Unreviewed;       510 AA.
AC   A0A1L8GZG6;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=6-phosphofructo-2-kinase/fructose-2, 6-bisphosphatase 3 isoform X3 {ECO:0000313|RefSeq:XP_018108242.1};
GN   Name=pfkfb3.L {ECO:0000313|RefSeq:XP_018108242.1,
GN   ECO:0000313|Xenbase:XB-GENE-17340406};
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355 {ECO:0000313|Proteomes:UP000186698, ECO:0000313|RefSeq:XP_018108242.1};
RN   [1] {ECO:0000313|RefSeq:XP_018108242.1}
RP   IDENTIFICATION.
RC   STRAIN=J_2021 {ECO:0000313|RefSeq:XP_018108242.1};
RC   TISSUE=Erythrocytes {ECO:0000313|RefSeq:XP_018108242.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the phosphoglycerate
CC       mutase family. {ECO:0000256|ARBA:ARBA00008408}.
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DR   RefSeq; XP_018108242.1; XM_018252753.2.
DR   AlphaFoldDB; A0A1L8GZG6; -.
DR   STRING; 8355.A0A1L8GZG6; -.
DR   PaxDb; 8355-A0A1L8GZG6; -.
DR   GeneID; 108711232; -.
DR   KEGG; xla:108711232; -.
DR   AGR; Xenbase:XB-GENE-17340406; -.
DR   CTD; 108711232; -.
DR   Xenbase; XB-GENE-17340406; pfkfb3.L.
DR   OMA; PRCIYLT; -.
DR   OrthoDB; 2013830at2759; -.
DR   Proteomes; UP000186698; Chromosome 3L.
DR   Bgee; 108711232; Expressed in egg cell and 19 other cell types or tissues.
DR   GO; GO:0003873; F:6-phosphofructo-2-kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004331; F:fructose-2,6-bisphosphate 2-phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006003; P:fructose 2,6-bisphosphate metabolic process; IEA:InterPro.
DR   GO; GO:0006000; P:fructose metabolic process; IEA:InterPro.
DR   CDD; cd07067; HP_PGM_like; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
DR   InterPro; IPR003094; 6Pfruct_kin.
DR   InterPro; IPR013079; 6Phosfructo_kin.
DR   InterPro; IPR013078; His_Pase_superF_clade-1.
DR   InterPro; IPR029033; His_PPase_superfam.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR10606; 6-PHOSPHOFRUCTO-2-KINASE/FRUCTOSE-2,6-BISPHOSPHATASE; 1.
DR   PANTHER; PTHR10606:SF41; 6-PHOSPHOFRUCTO-2-KINASE_FRUCTOSE-2,6-BISPHOSPHATASE 3; 1.
DR   Pfam; PF01591; 6PF2K; 1.
DR   Pfam; PF00300; His_Phos_1; 1.
DR   PIRSF; PIRSF000709; 6PFK_2-Ptase; 1.
DR   PRINTS; PR00991; 6PFRUCTKNASE.
DR   SMART; SM00855; PGAM; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
PE   3: Inferred from homology;
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000186698};
KW   Transferase {ECO:0000256|ARBA:ARBA00022777}.
FT   DOMAIN          29..247
FT                   /note="6-phosphofructo-2-kinase"
FT                   /evidence="ECO:0000259|Pfam:PF01591"
FT   BINDING         254..261
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT   BINDING         304
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
SQ   SEQUENCE   510 AA;  58129 MW;  C49ABF91E83838D1 CRC64;
     MPMELTQNRI QKIWLPRDEL PQLPINVGGP QFANSPTVIV MVGLPARGKT YISKKLTRYL
     NWSGVPTKVF NVGEYRREAV KDFSSHDFFR ADNTEAMKIR RHCALAALAD VKSYLTKEGG
     QIAVFDATNT TRERRSMVVD FAKENEFKVF FIESVCDDPS VVASNVLEVK LSSPDYKGCT
     SNVALEDFMK RINCYKNSYE PLDPDHHDRD LSMIIVIDVG RRFLVNRVQD HIQSKIVYYL
     MNIHVQPRCI YLCRAGESES NLNGKIGGDS GLSHRGKKFA ITLKKYIEDQ NLKELKVWTS
     QLKRSIQTAE ALKLPYEQWK ALNELDAGVC EEKTYEEIKE LYPEEYALRA QDKYHYRYPS
     GESYQDLVQR LEPVIMELER QGNVLVICHQ AVLRCLLSYF LDKPADEMPY LKCPLHSMLK
     LTPFAYGCHV ETVPFSVDAV NTHRDRIIED CKKCPTPLMR RNSVTPLASP EPTKKARINS
     FEEFAACSSV GCASQEPQSG QPLLGKACLA
//
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