ID A0A3Q1IQS3_ANATE Unreviewed; 455 AA.
AC A0A3Q1IQS3;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 2.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 4a {ECO:0000313|Ensembl:ENSATEP00000024237.2};
OS Anabas testudineus (Climbing perch) (Anthias testudineus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Anabantaria; Anabantiformes; Anabantoidei; Anabantidae; Anabas.
OX NCBI_TaxID=64144 {ECO:0000313|Ensembl:ENSATEP00000024237.2, ECO:0000313|Proteomes:UP000265040};
RN [1] {ECO:0000313|Ensembl:ENSATEP00000024237.2}
RP IDENTIFICATION.
RG Ensembl;
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 AlphaFoldDB; A0A3Q1IQS3; -.
DR Ensembl; ENSATET00000024625.2; ENSATEP00000024237.2; ENSATEG00000016787.2.
DR GeneTree; ENSGT00950000182835; -.
DR Proteomes; UP000265040; Unplaced.
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 InterPro; IPR001345; PG/BPGM_mutase_AS.
DR PANTHER; PTHR10606; 6-PHOSPHOFRUCTO-2-KINASE/FRUCTOSE-2,6-BISPHOSPHATASE; 1.
DR PANTHER; PTHR10606:SF14; 6-PHOSPHOFRUCTO-2-KINASE_FRUCTOSE-2,6-BISPHOSPHATASE 4; 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.
DR PROSITE; PS00175; PG_MUTASE; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
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:UP000265040};
KW Transferase {ECO:0000256|ARBA:ARBA00022777}.
FT DOMAIN 21..235
FT /note="6-phosphofructo-2-kinase"
FT /evidence="ECO:0000259|Pfam:PF01591"
FT ACT_SITE 243
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT ACT_SITE 312
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT BINDING 242..249
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT BINDING 292
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
SQ SEQUENCE 455 AA; 52689 MW; 946668EE61B59FEA CRC64;
MMRGCSSRAK LTQNQGRAVC MTNCPTLIVT VGLPARGKTY ISKKLTRYLN WIGVPTREFN
VGQYRREFVK IYKSFEFFSP DNEEGLKIRR QCASAALNDV RQYLTEDGGQ VAVFDATNTT
RERRETIIQF AEQNGFKVFF VESVCEDPDV IQENIVQVKL GSPDYTNCNT EEAVEDFMKR
IKCYENSYET LDEVLDRDLS YIKIMDVGQR YLVNRVLDHI QSRIVYYLMN IHITPRSIYL
CRHGESELNV KGRIGGDSGL TARGKEFAKK LSQFIQEQGI SDLKVWTSQM KRTIQTAEAL
SVPYEQWKVL NEIDAGVCEE MMYEEIQENY PLEFALRDQD KYRYRYPKGE SYEDLVQRLE
PVIMELERQE NVLVICHQAV MRCLLAYFLD KPAEELPYLK CPLHTVLKLT PVAYGCKVES
ISLNVEAVNT HRERPENVEV TRMSEEALLT VPAHQ
//
