ID W5K0G2_ASTMX Unreviewed; 537 AA.
AC W5K0G2;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 2.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 2 {ECO:0000256|ARBA:ARBA00040487};
DE EC=2.7.1.105 {ECO:0000256|ARBA:ARBA00012130};
DE EC=3.1.3.46 {ECO:0000256|ARBA:ARBA00013067};
DE AltName: Full=6PF-2-K/Fru-2,6-P2ase heart-type isozyme {ECO:0000256|ARBA:ARBA00041796};
OS Astyanax mexicanus (Blind cave fish) (Astyanax fasciatus mexicanus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC Characoidei; Characidae; Astyanax.
OX NCBI_TaxID=7994 {ECO:0000313|Ensembl:ENSAMXP00000001072.2, ECO:0000313|Proteomes:UP000018467};
RN [1] {ECO:0000313|Proteomes:UP000018467}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RA Jeffery W., Warren W., Wilson R.K.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000018467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RX PubMed=25329095; DOI=10.1038/ncomms6307;
RA McGaugh S.E., Gross J.B., Aken B., Blin M., Borowsky R., Chalopin D.,
RA Hinaux H., Jeffery W.R., Keene A., Ma L., Minx P., Murphy D., O'Quin K.E.,
RA Retaux S., Rohner N., Searle S.M., Stahl B.A., Tabin C., Volff J.N.,
RA Yoshizawa M., Warren W.C.;
RT "The cavefish genome reveals candidate genes for eye loss.";
RL Nat. Commun. 5:5307-5307(2014).
RN [3] {ECO:0000313|Ensembl:ENSAMXP00000001072.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Synthesis and degradation of fructose 2,6-bisphosphate.
CC {ECO:0000256|ARBA:ARBA00003771}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the phosphoglycerate
CC mutase family. {ECO:0000256|ARBA:ARBA00008408}.
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DR STRING; 7994.ENSAMXP00000028990; -.
DR Ensembl; ENSAMXT00000001072.2; ENSAMXP00000001072.2; ENSAMXG00000001046.2.
DR Ensembl; ENSAMXT00000045169.1; ENSAMXP00000028990.1; ENSAMXG00000001046.2.
DR eggNOG; KOG0234; Eukaryota.
DR GeneTree; ENSGT00950000182835; -.
DR HOGENOM; CLU_006383_1_1_1; -.
DR Proteomes; UP000018467; Unassembled WGS sequence.
DR Bgee; ENSAMXG00000001046; Expressed in mesonephros and 14 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 InterPro; IPR001345; PG/BPGM_mutase_AS.
DR PANTHER; PTHR10606; 6-PHOSPHOFRUCTO-2-KINASE/FRUCTOSE-2,6-BISPHOSPHATASE; 1.
DR PANTHER; PTHR10606:SF48; 6-PHOSPHOFRUCTO-2-KINASE_FRUCTOSE-2,6-BISPHOSPHATASE 2; 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 Acetylation {ECO:0000256|ARBA:ARBA00022990};
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:UP000018467};
KW Transferase {ECO:0000256|ARBA:ARBA00022777}.
FT DOMAIN 38..259
FT /note="6-phosphofructo-2-kinase"
FT /evidence="ECO:0000259|Pfam:PF01591"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 474..537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..38
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 268
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT ACT_SITE 337
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT BINDING 267..274
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT BINDING 317
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
SQ SEQUENCE 537 AA; 61751 MW; A5802E4DD60B9B90 CRC64;
MSSLAGDGDL SKGEGDPPKA MEKPTDSRKT ESRTTEKKCS WASHMTNSST LIVMIGLPAR
GKTYMSKKLT RYLNWIGVPT KVFNLGEYRR EAVQSYKSYD FFRHDNAEAM KIRKQCAIIA
LQDVKTYLNE EGGQIAVFDA TNTTRERRDL ILEFAQENSH RVFFVESICD DPDVIAENIM
DVKVSSPDYP ERHRERVMED FLKRIECYKV TYQPLDPDQH DRDRSFIQVI NVGQRFLVNR
VQDYIQSKIV YYLMNIHVHT HSIYLCRHGE SEHNIQGLIG GDSGLSNRGK EFARALRGFV
ESHKLVDLKV WTSQLKRTIQ TAEALGVPYE QWKILNEIDA GVCEEMSYDM IKHMYPDEYA
MRDQDKYHYR YPGGESYQDL VQRLEPVIME LERQGNVLVI CHQAVMRCLL AYFLDKSADD
LPYLKCPLHV VLKLTPVAYG CKVDMFDLKV EAVNTHRNRP LGCEKQDVPP ALLRRNSFTP
MSSRDQVKRP RLFSVGNPPH TPLPPALDST QEADELAEKP ETLNCFSATD SDDNVQK
//
