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F16P1_SPIOL
ID   F16P1_SPIOL             Reviewed;         415 AA.
AC   P22418; O20251;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-1998, sequence version 2.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Fructose-1,6-bisphosphatase, chloroplastic;
DE            Short=FBPase;
DE            EC=3.1.3.11;
DE   AltName: Full=D-fructose-1,6-bisphosphate 1-phosphohydrolase;
DE   Flags: Precursor;
OS   Spinacia oleracea (Spinach).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   Caryophyllales; Chenopodiaceae; Chenopodioideae; Anserineae; Spinacia.
OX   NCBI_TaxID=3562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Seedling;
RX   PubMed=8980497; DOI=10.1007/bf00019100;
RA   Martin W., Mustafa A.Z., Henze K., Schnarrenberger C.;
RT   "Higher-plant chloroplast and cytosolic fructose-1,6-bisphosphatase
RT   isoenzymes: origins via duplication rather than prokaryote-eukaryote
RT   divergence.";
RL   Plant Mol. Biol. 32:485-491(1996).
RN   [2]
RP   PROTEIN SEQUENCE OF 58-415.
RX   PubMed=2159755; DOI=10.1016/0003-9861(90)90475-e;
RA   Marcus F., Harrsch P.B.;
RT   "Amino acid sequence of spinach chloroplast fructose-1,6-bisphosphatase.";
RL   Arch. Biochem. Biophys. 279:151-157(1990).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
RX   PubMed=7703244; DOI=10.1021/bi00013a020;
RA   Villeret V., Huang S., Zhang Y., Lipscomb W.N.;
RT   "Structural aspects of the allosteric inhibition of fructose-1,6-
RT   bisphosphatase by AMP: the binding of both the substrate analogue 2,5-
RT   anhydro-D-glucitol 1,6-bisphosphate and catalytic metal ions monitored by
RT   X-ray crystallography.";
RL   Biochemistry 34:4307-4315(1995).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=beta-D-fructose 1,6-bisphosphate + H2O = beta-D-fructose 6-
CC         phosphate + phosphate; Xref=Rhea:RHEA:11064, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:32966, ChEBI:CHEBI:43474, ChEBI:CHEBI:57634; EC=3.1.3.11;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250};
CC   -!- PATHWAY: Carbohydrate biosynthesis; Calvin cycle.
CC   -!- SUBUNIT: Homotetramer.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- INDUCTION: Light activation through pH changes, Mg(2+) levels and also
CC       by light-modulated reduction of essential disulfide groups via the
CC       ferredoxin-thioredoxin f system.
CC   -!- MISCELLANEOUS: In plants there are two FBPase isozymes: one in the
CC       cytosol and the other in the chloroplast.
CC   -!- SIMILARITY: Belongs to the FBPase class 1 family. {ECO:0000305}.
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DR   EMBL; L76555; AAD10207.1; -; mRNA.
DR   PIR; T09085; T09085.
DR   PDB; 1SPI; X-ray; 2.80 A; A/B/C/D=58-415.
DR   PDBsum; 1SPI; -.
DR   AlphaFoldDB; P22418; -.
DR   SMR; P22418; -.
DR   PRIDE; P22418; -.
DR   OrthoDB; 1381522at2759; -.
DR   BRENDA; 3.1.3.11; 5812.
DR   SABIO-RK; P22418; -.
DR   UniPathway; UPA00116; -.
DR   EvolutionaryTrace; P22418; -.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0042132; F:fructose 1,6-bisphosphate 1-phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-UniPathway.
DR   CDD; cd00354; FBPase; 1.
DR   HAMAP; MF_01855; FBPase_class1; 1.
DR   InterPro; IPR044015; FBPase_C_dom.
DR   InterPro; IPR000146; FBPase_class-1.
DR   InterPro; IPR033391; FBPase_N.
DR   InterPro; IPR028343; FBPtase.
DR   InterPro; IPR020548; Fructose_bisphosphatase_AS.
DR   PANTHER; PTHR11556; PTHR11556; 1.
DR   Pfam; PF00316; FBPase; 1.
DR   Pfam; PF18913; FBPase_C; 1.
DR   PIRSF; PIRSF500210; FBPtase; 1.
DR   PIRSF; PIRSF000904; FBPtase_SBPase; 1.
DR   PRINTS; PR00115; F16BPHPHTASE.
DR   PROSITE; PS00124; FBPASE; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Calvin cycle; Carbohydrate metabolism; Chloroplast;
KW   Direct protein sequencing; Disulfide bond; Hydrolase; Magnesium;
KW   Metal-binding; Plastid; Transit peptide.
FT   TRANSIT         1..57
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000269|PubMed:2159755"
FT   CHAIN           58..415
FT                   /note="Fructose-1,6-bisphosphatase, chloroplastic"
FT                   /id="PRO_0000008818"
FT   REGION          207..232
FT                   /note="Involved in light regulation"
FT                   /evidence="ECO:0000255"
FT   BINDING         135
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         164
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         164
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         185
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         185
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         187
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         188..191
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         188
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         295
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         327
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         345
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         347
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         357
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         363
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   DISULFID        231..236
FT                   /note="Redox-active (light-modulated)"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        66
FT                   /note="E -> Q (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        88
FT                   /note="E -> P (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        303
FT                   /note="D -> P (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   HELIX           80..86
FT                   /evidence="ECO:0007829|PDB:1SPI"
FT   HELIX           96..116
FT                   /evidence="ECO:0007829|PDB:1SPI"
FT   HELIX           140..142
FT                   /evidence="ECO:0007829|PDB:1SPI"
FT   HELIX           145..152
FT                   /evidence="ECO:0007829|PDB:1SPI"
FT   STRAND          158..162
FT                   /evidence="ECO:0007829|PDB:1SPI"
FT   STRAND          181..185
FT                   /evidence="ECO:0007829|PDB:1SPI"
FT   HELIX           190..193
FT                   /evidence="ECO:0007829|PDB:1SPI"
FT   STRAND          202..206
FT                   /evidence="ECO:0007829|PDB:1SPI"
FT   STRAND          239..260
FT                   /evidence="ECO:0007829|PDB:1SPI"
FT   STRAND          263..270
FT                   /evidence="ECO:0007829|PDB:1SPI"
FT   TURN            271..274
FT                   /evidence="ECO:0007829|PDB:1SPI"
FT   STRAND          275..282
FT                   /evidence="ECO:0007829|PDB:1SPI"
FT   STRAND          291..293
FT                   /evidence="ECO:0007829|PDB:1SPI"
FT   HELIX           296..298
FT                   /evidence="ECO:0007829|PDB:1SPI"
FT   HELIX           304..313
FT                   /evidence="ECO:0007829|PDB:1SPI"
FT   STRAND          317..320
FT                   /evidence="ECO:0007829|PDB:1SPI"
FT   HELIX           331..341
FT                   /evidence="ECO:0007829|PDB:1SPI"
FT   STRAND          344..347
FT                   /evidence="ECO:0007829|PDB:1SPI"
FT   STRAND          349..353
FT                   /evidence="ECO:0007829|PDB:1SPI"
FT   STRAND          356..359
FT                   /evidence="ECO:0007829|PDB:1SPI"
FT   TURN            360..363
FT                   /evidence="ECO:0007829|PDB:1SPI"
FT   HELIX           364..374
FT                   /evidence="ECO:0007829|PDB:1SPI"
FT   STRAND          377..388
FT                   /evidence="ECO:0007829|PDB:1SPI"
FT   STRAND          391..394
FT                   /evidence="ECO:0007829|PDB:1SPI"
FT   STRAND          399..402
FT                   /evidence="ECO:0007829|PDB:1SPI"
FT   HELIX           405..411
FT                   /evidence="ECO:0007829|PDB:1SPI"
SQ   SEQUENCE   415 AA;  45230 MW;  A23465129F54A5A1 CRC64;
     MASIGPATTT AVKLRSSIFN PQSSTLSPSQ QCITFTKSLH SFPTATRHNV ASGVRCMAAV
     GEAATETKAR TRSKYEIETL TGWLLKQEMA GVIDAELTIV LSSISLACKQ IASLVQRAGI
     SNLTGIQGAV NIQGEDQKKL DVVSNEVFSS CLRSSGRTGI IASEEEDVPV AVEESYSGNY
     IVVFDPLDGS SNIDAAVSTG SIFGIYSPND ECIVDSDHDD ESQLSAEEQR CVVNVCQPGD
     NLLAAGYCMY SSSVIFVLTI GKGVYAFTLD PMYGEFVLTS EKIQIPKAGK IYSFNEGNYK
     MWDDKLKKYM DDLKEPGESQ KPYSSRYIGS LVGDFHRTLL YGGIYGYPRD AKSKNGKLRL
     LYECAPMSFI VEQAGGKGSD GHQRILDIQP TEIHQRVPLY IGSVEEVEKL EKYLA
 
 
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