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FBPAP_IGNH4
ID   FBPAP_IGNH4             Reviewed;         387 AA.
AC   A8A9E4;
DT   07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 61.
DE   RecName: Full=Fructose-1,6-bisphosphate aldolase/phosphatase {ECO:0000303|PubMed:20348906};
DE            Short=FBP A/P {ECO:0000255|HAMAP-Rule:MF_02067};
DE            Short=FBP aldolase/phosphatase {ECO:0000303|PubMed:20348906};
DE            EC=3.1.3.11 {ECO:0000269|PubMed:20348906};
DE            EC=4.1.2.13 {ECO:0000269|PubMed:20348906};
GN   Name=fbp {ECO:0000255|HAMAP-Rule:MF_02067};
GN   OrderedLocusNames=Igni_0363 {ECO:0000312|EMBL:ABU81546.1};
OS   Ignicoccus hospitalis (strain KIN4/I / DSM 18386 / JCM 14125).
OC   Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC   Desulfurococcaceae; Ignicoccus.
OX   NCBI_TaxID=453591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KIN4/I / DSM 18386 / JCM 14125;
RX   PubMed=19000309; DOI=10.1186/gb-2008-9-11-r158;
RA   Podar M., Anderson I., Makarova K.S., Elkins J.G., Ivanova N., Wall M.A.,
RA   Lykidis A., Mavromatis K., Sun H., Hudson M.E., Chen W., Deciu C.,
RA   Hutchison D., Eads J.R., Anderson A., Fernandes F., Szeto E., Lapidus A.,
RA   Kyrpides N.C., Saier M.H. Jr., Richardson P.M., Rachel R., Huber H.,
RA   Eisen J.A., Koonin E.V., Keller M., Stetter K.O.;
RT   "A genomic analysis of the archaeal system Ignicoccus hospitalis-
RT   Nanoarchaeum equitans.";
RL   Genome Biol. 9:R158.1-R158.18(2008).
RN   [2]
RP   FUNCTION AS BOTH FBPASE AND FBP ALDOLASE, CATALYTIC ACTIVITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY.
RC   STRAIN=KIN4/I / DSM 18386 / JCM 14125;
RX   PubMed=20348906; DOI=10.1038/nature08884;
RA   Say R.F., Fuchs G.;
RT   "Fructose 1,6-bisphosphate aldolase/phosphatase may be an ancestral
RT   gluconeogenic enzyme.";
RL   Nature 464:1077-1081(2010).
CC   -!- FUNCTION: Catalyzes two subsequent steps in gluconeogenesis: the aldol
CC       condensation of dihydroxyacetone phosphate (DHAP) and glyceraldehyde-3-
CC       phosphate (GA3P) to fructose-1,6-bisphosphate (FBP), and the
CC       dephosphorylation of FBP to fructose-6-phosphate (F6P).
CC       {ECO:0000269|PubMed:20348906}.
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         Evidence={ECO:0000269|PubMed:20348906};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-
CC         phosphate + dihydroxyacetone phosphate; Xref=Rhea:RHEA:14729,
CC         ChEBI:CHEBI:32966, ChEBI:CHEBI:57642, ChEBI:CHEBI:59776; EC=4.1.2.13;
CC         Evidence={ECO:0000269|PubMed:20348906};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:F9VMT6};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.02 mM for D-fructose 1,6-bisphosphate (when assaying the FBP
CC         phosphatase activity, at 48 degrees Celsius)
CC         {ECO:0000269|PubMed:20348906};
CC         KM=0.23 mM for triosephosphates (when assaying the FBP aldolase
CC         activity in the anabolic direction, at 48 degrees Celsius)
CC         {ECO:0000269|PubMed:20348906};
CC         Vmax=0.88 umol/min/mg enzyme for the FBP phosphatase activity (at 48
CC         degrees Celsius) {ECO:0000269|PubMed:20348906};
CC         Vmax=0.54 umol/min/mg enzyme for the FBP aldolase activity (at 48
CC         degrees Celsius) {ECO:0000269|PubMed:20348906};
CC       pH dependence:
CC         Optimum pH is 8.0 for FBP phosphatase activity and 7-8.5 for the FBP
CC         aldolase activity. {ECO:0000269|PubMed:20348906};
CC       Temperature dependence:
CC         Highly thermostable. Survives boiling for 1 hour.
CC         {ECO:0000269|PubMed:20348906};
CC   -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC       {ECO:0000305|PubMed:20348906}.
CC   -!- SUBUNIT: Homooctamer; dimer of tetramers.
CC       {ECO:0000250|UniProtKB:F9VMT6}.
CC   -!- DOMAIN: Consists of a single catalytic domain, but remodels its active-
CC       site architecture via a large structural change to exhibit dual
CC       activities. {ECO:0000250|UniProtKB:F9VMT6}.
CC   -!- SIMILARITY: Belongs to the FBP aldolase/phosphatase family.
CC       {ECO:0000255|HAMAP-Rule:MF_02067, ECO:0000305}.
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DR   EMBL; CP000816; ABU81546.1; -; Genomic_DNA.
DR   RefSeq; WP_011998398.1; NC_009776.1.
DR   AlphaFoldDB; A8A9E4; -.
DR   SMR; A8A9E4; -.
DR   STRING; 453591.Igni_0363; -.
DR   EnsemblBacteria; ABU81546; ABU81546; Igni_0363.
DR   GeneID; 5563123; -.
DR   KEGG; iho:Igni_0363; -.
DR   eggNOG; arCOG04180; Archaea.
DR   HOGENOM; CLU_041630_0_0_2; -.
DR   OMA; YMRRHGP; -.
DR   OrthoDB; 21175at2157; -.
DR   PhylomeDB; A8A9E4; -.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000000262; Chromosome.
DR   GO; GO:0042132; F:fructose 1,6-bisphosphate 1-phosphatase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_02067; FBP_aldolase_phosphatase; 1.
DR   InterPro; IPR002803; FBPase_V.
DR   InterPro; IPR036076; FBPase_V_sf.
DR   PANTHER; PTHR38341; PTHR38341; 1.
DR   Pfam; PF01950; FBPase_3; 1.
DR   PIRSF; PIRSF015647; FBPtase_archl; 1.
DR   SUPFAM; SSF111249; SSF111249; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Gluconeogenesis; Hydrolase; Lyase; Magnesium;
KW   Metal-binding; Reference proteome; Schiff base.
FT   CHAIN           1..387
FT                   /note="Fructose-1,6-bisphosphate aldolase/phosphatase"
FT                   /id="PRO_0000437180"
FT   ACT_SITE        13
FT                   /note="Proton acceptor; for FBP phosphatase activity"
FT                   /evidence="ECO:0000250|UniProtKB:F9VMT6"
FT   ACT_SITE        229
FT                   /note="Proton donor/acceptor; for FBP aldolase activity"
FT                   /evidence="ECO:0000250|UniProtKB:F9VMT6"
FT   ACT_SITE        232
FT                   /note="Schiff-base intermediate with DHAP; for FBP aldolase
FT                   activity"
FT                   /evidence="ECO:0000250|UniProtKB:F9VMT6"
FT   BINDING         13
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:F9VMT6"
FT   BINDING         20
FT                   /ligand="beta-D-fructose 1,6-bisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:32966"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250|UniProtKB:F9VMT6"
FT   BINDING         20
FT                   /ligand="dihydroxyacetone phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57642"
FT                   /evidence="ECO:0000250|UniProtKB:F9VMT6"
FT   BINDING         20
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:F9VMT6"
FT   BINDING         54
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:F9VMT6"
FT   BINDING         54
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:F9VMT6"
FT   BINDING         55
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:F9VMT6"
FT   BINDING         92
FT                   /ligand="beta-D-fructose 1,6-bisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:32966"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250|UniProtKB:F9VMT6"
FT   BINDING         96
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:F9VMT6"
FT   BINDING         105..106
FT                   /ligand="beta-D-fructose 1,6-bisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:32966"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250|UniProtKB:F9VMT6"
FT   BINDING         133
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:F9VMT6"
FT   BINDING         134
FT                   /ligand="beta-D-fructose 1,6-bisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:32966"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250|UniProtKB:F9VMT6"
FT   BINDING         134
FT                   /ligand="dihydroxyacetone phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57642"
FT                   /evidence="ECO:0000250|UniProtKB:F9VMT6"
FT   BINDING         232
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:F9VMT6"
FT   BINDING         233
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:F9VMT6"
FT   BINDING         233
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000250|UniProtKB:F9VMT6"
FT   BINDING         234
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:F9VMT6"
FT   BINDING         234
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:F9VMT6"
FT   BINDING         242..243
FT                   /ligand="beta-D-fructose 1,6-bisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:32966"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000250|UniProtKB:F9VMT6"
FT   BINDING         266
FT                   /ligand="beta-D-fructose 1,6-bisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:32966"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250|UniProtKB:F9VMT6"
FT   BINDING         266
FT                   /ligand="dihydroxyacetone phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57642"
FT                   /evidence="ECO:0000250|UniProtKB:F9VMT6"
FT   BINDING         287
FT                   /ligand="beta-D-fructose 1,6-bisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:32966"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250|UniProtKB:F9VMT6"
FT   BINDING         287
FT                   /ligand="dihydroxyacetone phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57642"
FT                   /evidence="ECO:0000250|UniProtKB:F9VMT6"
FT   BINDING         348
FT                   /ligand="beta-D-fructose 1,6-bisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:32966"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250|UniProtKB:F9VMT6"
SQ   SEQUENCE   387 AA;  42514 MW;  278DF5048404E211 CRC64;
     MAQKTTISVI KADIGSLAGH HTVHPDCMAA ASRVLAEAKK NGVINDFYVT HVGDDLILIM
     THTKGVDHPD VHGLAWEAFK KAAEVAKELG LYAAGQDLLS DAFSGNVRGL GPAAAEMEIE
     ERPSEPIVIF AADKTEPGAF NLPLYKIFAD PFNTAGLVID PRLHDGFVFE VVDVFEDKGV
     HLNTPEELYD LLALIGTPSR YVIRRVFRKD GKIAAVVSVE RLNLIAGKYV GKDDPVMIVR
     AQSGFPAVGE VLEPFTFPHL VAGWMRGSHN GPLMPVPVRD ARPTRFDGPP RVIALGFQVK
     NAKLVGPSDL FDDPAFDEAR RTANKVADYI RRHGPFMPHR LDPSEMEYTT LPQVLERLKD
     RFKPVKDLPV PKVKHSEMLS GAEEAHD
 
 
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