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Database: UniProt
Entry: A0A3Q1BP49_AMPOC
LinkDB: A0A3Q1BP49_AMPOC
Original site: A0A3Q1BP49_AMPOC 
ID   A0A3Q1BP49_AMPOC        Unreviewed;       526 AA.
AC   A0A3Q1BP49;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 3 {ECO:0000313|Ensembl:ENSAOCP00000010721.1};
OS   Amphiprion ocellaris (Clown anemonefish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Pomacentridae; Amphiprion.
OX   NCBI_TaxID=80972 {ECO:0000313|Ensembl:ENSAOCP00000010721.1, ECO:0000313|Proteomes:UP000257160};
RN   [1] {ECO:0000313|Ensembl:ENSAOCP00000010721.1}
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; A0A3Q1BP49; -.
DR   STRING; 80972.ENSAOCP00000010721; -.
DR   Ensembl; ENSAOCT00000017869.1; ENSAOCP00000010721.1; ENSAOCG00000001041.1.
DR   GeneTree; ENSGT00950000182835; -.
DR   OrthoDB; 2013830at2759; -.
DR   Proteomes; UP000257160; 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: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.
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:UP000257160};
KW   Transferase {ECO:0000256|ARBA:ARBA00022777}.
FT   DOMAIN          27..245
FT                   /note="6-phosphofructo-2-kinase"
FT                   /evidence="ECO:0000259|Pfam:PF01591"
FT   REGION          442..476
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        253
FT                   /note="Tele-phosphohistidine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT   ACT_SITE        322
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT   BINDING         252..259
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT   BINDING         302
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
SQ   SEQUENCE   526 AA;  60367 MW;  9B3BEEE3CAB765BA CRC64;
     MPRELTQNRI QKIWVPTKDD RRRAAGAPNF ANPPTVIVMV GLPARGKTYM SKKLTRYLNW
     IGMPTKVFNV GEYRREAVKN YSSYDFFKPD NEYAVKIRQQ CALAALRDVK SYLKDEGGQV
     AVFDATNTTR DRRDMILKFG SENSFKVFFI ESVCDDPNVI ASNIMEVKVS CPDYRDCNKT
     EAMLDFHRRI ECYKTSYQPL DPDQHDRDLS FIKVIDVGRR FLVNRIQDHI QSKIVYYLMN
     IHVQPRTIYL CRHGESTDNL EGRLGGDSGL SPRGKQFSAA LARFVEEQQL KNLKVWTSQL
     CRSIQTAEHL GVPYEQWKAL NEIDAGLCEE MTYDEVKEKF PEEFALRDED KYYYRYPAGE
     SYQDLVQRVE PVIMELERQE NVLVICHQAV MRCLLAYFLD KSADEMPYLK CPLHTVLKLT
     PVAYGCKVES ISLNVEAVNT HRDRPEEVKR GPGTLIRRNS VTPLTSPESN IKKPRIDDLD
     EAPIQELPPS VASLALCSPS HLPLALAGQD LRRSSSGCHD FLQPCQ
//
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