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FBPAP_METS5
ID   FBPAP_METS5             Reviewed;         383 AA.
AC   A4YIZ5;
DT   07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 71.
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=Msed_2259 {ECO:0000312|EMBL:ABP96397.1};
OS   Metallosphaera sedula (strain ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509
OS   / TH2).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Metallosphaera.
OX   NCBI_TaxID=399549;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2;
RX   PubMed=18083856; DOI=10.1128/aem.02019-07;
RA   Auernik K.S., Maezato Y., Blum P.H., Kelly R.M.;
RT   "The genome sequence of the metal-mobilizing, extremely thermoacidophilic
RT   archaeon Metallosphaera sedula provides insights into bioleaching-
RT   associated metabolism.";
RL   Appl. Environ. Microbiol. 74:682-692(2008).
RN   [2]
RP   FUNCTION AS BOTH FBPASE AND FBP ALDOLASE, CATALYTIC ACTIVITY, AND PATHWAY.
RC   STRAIN=ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2;
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   -!- 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; CP000682; ABP96397.1; -; Genomic_DNA.
DR   RefSeq; WP_012022184.1; NC_009440.1.
DR   AlphaFoldDB; A4YIZ5; -.
DR   SMR; A4YIZ5; -.
DR   STRING; 399549.Msed_2259; -.
DR   EnsemblBacteria; ABP96397; ABP96397; Msed_2259.
DR   GeneID; 5104211; -.
DR   GeneID; 59456610; -.
DR   KEGG; mse:Msed_2259; -.
DR   eggNOG; arCOG04180; Archaea.
DR   HOGENOM; CLU_041630_0_0_2; -.
DR   OMA; YMRRHGP; -.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000000242; 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..383
FT                   /note="Fructose-1,6-bisphosphate aldolase/phosphatase"
FT                   /id="PRO_0000437181"
FT   REGION          361..383
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        11
FT                   /note="Proton acceptor; for FBP phosphatase activity"
FT                   /evidence="ECO:0000250|UniProtKB:F9VMT6"
FT   ACT_SITE        228
FT                   /note="Proton donor/acceptor; for FBP aldolase activity"
FT                   /evidence="ECO:0000250|UniProtKB:F9VMT6"
FT   ACT_SITE        231
FT                   /note="Schiff-base intermediate with DHAP; for FBP aldolase
FT                   activity"
FT                   /evidence="ECO:0000250|UniProtKB:F9VMT6"
FT   BINDING         11
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:F9VMT6"
FT   BINDING         18
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         18
FT                   /ligand="dihydroxyacetone phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57642"
FT                   /evidence="ECO:0000250|UniProtKB:F9VMT6"
FT   BINDING         18
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:F9VMT6"
FT   BINDING         52
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:F9VMT6"
FT   BINDING         52
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:F9VMT6"
FT   BINDING         53
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:F9VMT6"
FT   BINDING         90
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         94
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:F9VMT6"
FT   BINDING         103..104
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         131
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:F9VMT6"
FT   BINDING         132
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         132
FT                   /ligand="dihydroxyacetone phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57642"
FT                   /evidence="ECO:0000250|UniProtKB:F9VMT6"
FT   BINDING         231
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
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         232
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000250|UniProtKB:F9VMT6"
FT   BINDING         233
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
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         241..242
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         265
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         265
FT                   /ligand="dihydroxyacetone phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57642"
FT                   /evidence="ECO:0000250|UniProtKB:F9VMT6"
FT   BINDING         286
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         286
FT                   /ligand="dihydroxyacetone phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57642"
FT                   /evidence="ECO:0000250|UniProtKB:F9VMT6"
FT   BINDING         347
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   383 AA;  42534 MW;  87D5E21A3CA547C3 CRC64;
     MRSTVSVIKA DIGSLAGHHV VHPDTMAAAN RVLAEAKRQG IILDYYITNV GDDLELIMSH
     TRGELDTKVH ETAWDAFKEA TKVSKELGLY AAGQDLLSDS FSGNLKGMGP GIAELDIEER
     PSEPIAIFMA DKTEPGAFNL PLYKMFADPF NTAGLVIDPT MNEGFKFEVL DVYEGQSVVL
     NSPEEMYSLL GLIGTPARYV IRRVYRKADN MIGSVTSIER LNLIAGKYVG KDDPVLIVRL
     QHGFPALGEA LEAFSFPYLV PGWMRGSHYG PIMPVSQRDA KATRFDGPPR LIGLGFNVKN
     GKLTGPSDLF DDPAFDETRR MASVITDYMR RHGPFMPHRL EPTEMEYTTL PTLIEKLKPR
     FKKEEDVKKA KPSVYTSKDQ GMD
 
 
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