ID L9JBT2_TUPCH Unreviewed; 1319 AA.
AC L9JBT2;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
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};
GN ORFNames=TREES_T100003445 {ECO:0000313|EMBL:ELW47759.1};
OS Tupaia chinensis (Chinese tree shrew).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Scandentia; Tupaiidae; Tupaia.
OX NCBI_TaxID=246437 {ECO:0000313|EMBL:ELW47759.1, ECO:0000313|Proteomes:UP000011518};
RN [1] {ECO:0000313|Proteomes:UP000011518}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Zhang G., Fan Y., Yao Y., Huang Z.;
RT "Genome of the Chinese tree shrew, a rising model animal genetically
RT related to primates.";
RL Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000011518}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23385571; DOI=10.1038/ncomms2416;
RA Fan Y., Huang Z.Y., Cao C.C., Chen C.S., Chen Y.X., Fan D.D., He J.,
RA Hou H.L., Hu L., Hu X.T., Jiang X.T., Lai R., Lang Y.S., Liang B.,
RA Liao S.G., Mu D., Ma Y.Y., Niu Y.Y., Sun X.Q., Xia J.Q., Xiao J.,
RA Xiong Z.Q., Xu L., Yang L., Zhang Y., Zhao W., Zhao X.D., Zheng Y.T.,
RA Zhou J.M., Zhu Y.B., Zhang G.J., Wang J., Yao Y.G.;
RT "Genome of the Chinese tree shrew.";
RL Nat. Commun. 4:1426-1426(2013).
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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00302}.
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DR EMBL; KB321094; ELW47759.1; -; Genomic_DNA.
DR STRING; 246437.L9JBT2; -.
DR eggNOG; ENOG502SHRK; Eukaryota.
DR InParanoid; L9JBT2; -.
DR Proteomes; UP000011518; Unassembled WGS sequence.
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; cd00033; CCP; 11.
DR CDD; cd07067; HP_PGM_like; 1.
DR Gene3D; 1.20.5.3730; -; 1.
DR Gene3D; 2.20.28.230; -; 1.
DR Gene3D; 2.10.70.10; Complement Module, domain 1; 10.
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; IPR040514; C4bp_oligo.
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 InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR InterPro; IPR000436; Sushi_SCR_CCP_dom.
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; PF18453; C4bp_oligo; 1.
DR Pfam; PF00300; His_Phos_1; 1.
DR Pfam; PF00084; Sushi; 10.
DR PRINTS; PR00991; 6PFRUCTKNASE.
DR SMART; SM00032; CCP; 11.
DR SMART; SM00855; PGAM; 1.
DR SUPFAM; SSF57535; Complement control module/SCR domain; 11.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
DR PROSITE; PS00175; PG_MUTASE; 1.
DR PROSITE; PS50923; SUSHI; 10.
PE 3: Inferred from homology;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00302}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ELW47759.1};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000011518};
KW Sushi {ECO:0000256|PROSITE-ProRule:PRU00302};
KW Transferase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ELW47759.1}.
FT DOMAIN 510..567
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 568..625
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 626..682
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 755..816
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 817..878
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 879..943
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 944..1003
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 1004..1069
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 1070..1130
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 1188..1246
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DISULFID 538..565
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT DISULFID 596..623
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT DISULFID 787..814
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT DISULFID 881..924
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT DISULFID 974..1001
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT DISULFID 1072..1115
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT DISULFID 1217..1244
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
SQ SEQUENCE 1319 AA; 149675 MW; CB1C81E3EB8A2D23 CRC64;
MSENFASCSE PNNNSYKIKA SNPRMSEKKC SWASYMTNSP TLIVMIGLPA RGKTYVSKKL
TRYLNWIGVP TKVFNLGVYR REAVKSYKSY DFFRHDNEEA MKIRRRCALV ALQDVKAYLS
EENGQIAVFD ATNTTRERRD MILNFAKQNS YKVFFVESVC DDPDVIAANI LEVKVSSPDY
PERNRENVME DFLKRIECYK VTYQPLDPDN YDKDRSFIKV INVGQRFLVN RVQDYIQSKI
VYYLMNIHVQ PRTIYLCRHG ESEFNLLGKI GGDSGLSVRG KQFSQALRTF LEEQKIADLK
VWTSQLKRTI QTAESLGVTY EQWKILNEID AGVCEEMTYA EIEKQYPDEF ALRDQEKYLY
RYPGGESYQD LVQRLEPVIM ELERQGNVLV ISHQAVMRCL LAYFLDKGAD ELPYLKCPLH
TIFKLTPVAY GNYELRDWQE VGIEEGCKVE TIKLNVEAVN THRDKPTLLG NVYSVSSQGF
GLGKGNGEGP TGVKEKIHNP KQVMQADRTE RCSKPPQVDN SIFIAMKEEG QISGIYSCIK
GYHLVGKGTL FCNAFDEWTV PTATCHLGHC PNPVLSNGKF NYSWPVKVSD KVTFMCNDYY
ILKGSSWSQC LENHTWAPPF PICKSRDCDP PENPAHGYFK GRNFTSGSNI TYYCEEGYRL
MGTPDQQCID GEWNSDLPSC ELIQEAPKPT APTKYGKALL AFQENKDLCK AIQDFIKRLT
ETGLTMEELK HTLEMKKAEL KGKKCCPNIV AKKTGDCGPP PILSFASPVN ELNDTEFKTG
DVLRYTCRPG FSKTISNPTL ICRSKGSWSY VTFCTRKRCR NPGDLPNGQV EVKTDFLFGS
HIEFSCLEGY ILVGSTTSYC EIQEKGVDWS DPLPECVIAQ CESPPDISNG RHNGGDRDTY
TFGSSVTYSC DPHFSLLGKA SVSCTVENKT KGVWSPSPPV CKKITCSQPD IAHSKIVSGF
GPVYTYKDSI VFNCQRGYIL RGNSVIRCEV DNNWNPSPPY CELNGCIGLP DIPHAILEEY
YRASGEEAYE IGTEFKYSCY SGYKPVTREP TTVVCQKNFR WNIHNKCEET CCPEPKLKNG
VIIRHKKKYV GSKCTYFYGD EVSYSCSNKN YEASCRSDGT WYPEAPSCDK NCEFPPTIAH
GHHRDVPRYI FGTKEYAYEC DEGYTLVGES RISCSSSVWS ALPPKCKAIC HKPEIENGKP
SVDKNQYVES ENITVECNSG YDVVGSQSIT CSEDRTWYPE VPKCEWVFPE GCEQVLAGRK
LMQCLPNPED VKMALEVYKL SLEIERLEQE RGMARETRPT LESVPQSFFR EWGKDVLLS
//
