ID A0A2K5NZX4_CERAT Unreviewed; 717 AA.
AC A0A2K5NZX4;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 3 {ECO:0000313|Ensembl:ENSCATP00000043084.1};
GN Name=PFKFB3 {ECO:0000313|Ensembl:ENSCATP00000043084.1};
OS Cercocebus atys (Sooty mangabey) (Cercocebus torquatus atys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Cercocebus.
OX NCBI_TaxID=9531 {ECO:0000313|Ensembl:ENSCATP00000043084.1, ECO:0000313|Proteomes:UP000233060};
RN [1] {ECO:0000313|Ensembl:ENSCATP00000043084.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SIMILARITY: In the C-terminal section; belongs to the phosphoglycerate
CC mutase family. {ECO:0000256|ARBA:ARBA00008408}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; A0A2K5NZX4; -.
DR STRING; 9531.ENSCATP00000043084; -.
DR Ensembl; ENSCATT00000067521.1; ENSCATP00000043084.1; ENSCATG00000044099.1.
DR GeneTree; ENSGT00950000182835; -.
DR Proteomes; UP000233060; Unplaced.
DR Bgee; ENSCATG00000044099; Expressed in skeletal muscle tissue and 12 other cell types or tissues.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
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 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:UP000233060};
KW Transferase {ECO:0000256|ARBA:ARBA00022777}.
FT DOMAIN 223..443
FT /note="6-phosphofructo-2-kinase"
FT /evidence="ECO:0000259|Pfam:PF01591"
FT REGION 1..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 103..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 637..717
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..141
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 637..651
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 451
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT ACT_SITE 520
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT BINDING 450..457
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
SQ SEQUENCE 717 AA; 79719 MW; 95EF99ECC6874752 CRC64;
MGRGDNSSQD LQQGWAAGAG APPSPARRGS PQAASRLAHP PPHVEGGWDP RNAARPEADV
RVCGQPGFFK SRRCVGHPSR TGEEASGRAW WRECGCHCAR ASQSFPSGRA GGAGHPQPRT
PRSTRRAPHP SQHTSSPAPT RVRNLAQSTF PQAAQGTPGR APAHAPLSSF VPGVGGPSPA
SVGISALGSG PSGTAAKMPL ELTQSRVQKI WVPVDHRPSL PRSCGPKLTN SPTVIVMVGL
PARGKTYISK KLTRYLNWIG VPTKVFNVGE YRREAVKQYS SYNFFRPDNE EAMKVRKQCA
LAALRDVKSY LAKEGGQIAV FDATNTTRER RHMILHFAKE NDFKAFFIES VCDDPTVVAS
NIMEVKISSP DYKDCNSAEA MDDFMKRISC YEASYQPLDP DKCDRDLSLI KVIDVGRRFL
VNRVQDHIQS RIVYYLMNIH VQPRTIYLCR HGENEHNLQG RIGGDSGLSS RGKKFASALS
KFVEEQNLKD LRVWTSQLKS TIQTAEALRL PYEQWKALNE IDAGVCEELT YEEIRDTYPE
EYALREQDKY YYRYPTGESY QDLVQRLEPV IMELERQENV LVICHQAVLR CLLAYFLDKS
AEEMPYLKCP LHTVLKLTPV AYGCRVESIY LNVESVSTHR ERSEDAKKGP NPLMRRNSVT
PLASPEPTKK PRINSFEEHV ASTSAALPSC LPPEVPTQLP GQNMKGSRSS ADSSRKH
//
