G6PI_PYRFU
ID G6PI_PYRFU Reviewed; 189 AA.
AC P83194;
DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Glucose-6-phosphate isomerase;
DE Short=GPI;
DE EC=5.3.1.9;
DE AltName: Full=Phosphoglucose isomerase;
DE Short=PGI;
DE AltName: Full=Phosphohexose isomerase;
DE Short=PHI;
GN Name=pgiA; OrderedLocusNames=PF0196;
OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=186497;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-20, AND
RP CHARACTERIZATION.
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=11533028; DOI=10.1074/jbc.m104603200;
RA Verhees C.H., Huynen M.A., Ward D.E., Schiltz E., de Vos W.M.,
RA van der Oost J.;
RT "The phosphoglucose isomerase from the hyperthermophilic archaeon
RT Pyrococcus furiosus is a unique glycolytic enzyme that belongs to the cupin
RT superfamily.";
RL J. Biol. Chem. 276:40926-40932(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA DiRuggiero J., Robb F.T.;
RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT horikoshii inferred from complete genomic sequences.";
RL Genetics 152:1299-1305(1999).
RN [3]
RP PROTEIN SEQUENCE OF 1-28, AND CHARACTERIZATION.
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=11344151; DOI=10.1128/jb.183.11.3428-3435.2001;
RA Hansen T., Oehlmann M., Schoenheit P.;
RT "Novel type of glucose-6-phosphate isomerase in the hyperthermophilic
RT archaeon Pyrococcus furiosus.";
RL J. Bacteriol. 183:3428-3435(2001).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-glucose 6-phosphate = beta-D-fructose 6-phosphate;
CC Xref=Rhea:RHEA:11816, ChEBI:CHEBI:57634, ChEBI:CHEBI:58225;
CC EC=5.3.1.9;
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
CC Note=Binds 1 Fe cation per subunit. {ECO:0000250};
CC -!- ACTIVITY REGULATION: Inhibited by mannose 6-phosphate, fructose 1-
CC phosphate and fructose 1,6-bisphosphate.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.0.;
CC Temperature dependence:
CC Optimum temperature is 90-96 degrees Celsius. Highly thermostable.;
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 2/4.
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the archaeal-type GPI family. {ECO:0000305}.
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DR EMBL; AF381250; AAL27992.1; -; Genomic_DNA.
DR EMBL; AE009950; AAL80320.1; -; Genomic_DNA.
DR RefSeq; WP_011011309.1; NC_018092.1.
DR PDB; 1QXJ; X-ray; 1.80 A; A/B=1-189.
DR PDB; 1QXR; X-ray; 1.70 A; A/B=1-189.
DR PDB; 1QY4; X-ray; 1.80 A; A/B=1-189.
DR PDB; 1X7N; X-ray; 1.89 A; A=1-189.
DR PDB; 1X82; X-ray; 1.50 A; A=1-189.
DR PDB; 1X8E; X-ray; 2.80 A; A/B=1-189.
DR PDB; 2GC0; X-ray; 2.00 A; A/B=1-187.
DR PDB; 2GC1; X-ray; 1.95 A; A/B=1-187.
DR PDB; 2GC2; X-ray; 2.10 A; A/B=1-187.
DR PDB; 2GC3; X-ray; 2.10 A; A/B=1-187.
DR PDB; 3SXW; X-ray; 1.80 A; A=1-189.
DR PDB; 4LTA; X-ray; 2.04 A; A/B=1-189.
DR PDB; 4LUK; X-ray; 1.41 A; A=1-189.
DR PDB; 4LUL; X-ray; 1.89 A; A/B=1-189.
DR PDB; 4LUM; X-ray; 1.79 A; A/B=1-189.
DR PDBsum; 1QXJ; -.
DR PDBsum; 1QXR; -.
DR PDBsum; 1QY4; -.
DR PDBsum; 1X7N; -.
DR PDBsum; 1X82; -.
DR PDBsum; 1X8E; -.
DR PDBsum; 2GC0; -.
DR PDBsum; 2GC1; -.
DR PDBsum; 2GC2; -.
DR PDBsum; 2GC3; -.
DR PDBsum; 3SXW; -.
DR PDBsum; 4LTA; -.
DR PDBsum; 4LUK; -.
DR PDBsum; 4LUL; -.
DR PDBsum; 4LUM; -.
DR AlphaFoldDB; P83194; -.
DR SMR; P83194; -.
DR STRING; 186497.PF0196; -.
DR PRIDE; P83194; -.
DR EnsemblBacteria; AAL80320; AAL80320; PF0196.
DR GeneID; 41711987; -.
DR KEGG; pfu:PF0196; -.
DR PATRIC; fig|186497.12.peg.203; -.
DR eggNOG; arCOG02602; Archaea.
DR HOGENOM; CLU_105797_0_0_2; -.
DR OMA; YPADAGH; -.
DR OrthoDB; 72912at2157; -.
DR PhylomeDB; P83194; -.
DR BioCyc; MetaCyc:MON-11807; -.
DR BRENDA; 5.3.1.9; 5243.
DR SABIO-RK; P83194; -.
DR UniPathway; UPA00109; UER00181.
DR EvolutionaryTrace; P83194; -.
DR Proteomes; UP000001013; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004347; F:glucose-6-phosphate isomerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniRule.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule.
DR Gene3D; 2.60.120.10; -; 1.
DR HAMAP; MF_01410; G6P_isomerase_arch; 1.
DR InterPro; IPR016758; G6P_isomerase_archaea/bacteria.
DR InterPro; IPR010551; G6P_isomerase_prok.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR011051; RmlC_Cupin_sf.
DR Pfam; PF06560; GPI; 1.
DR PIRSF; PIRSF019325; Glucose-6-phosphate_isomerase; 1.
DR SUPFAM; SSF51182; SSF51182; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Gluconeogenesis;
KW Glycolysis; Iron; Isomerase; Metal-binding; Reference proteome.
FT CHAIN 1..189
FT /note="Glucose-6-phosphate isomerase"
FT /id="PRO_0000185357"
FT BINDING 88
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 90
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 97
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 136
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT CONFLICT 11
FT /note="D -> N (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 28
FT /note="S -> P (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 6..10
FT /evidence="ECO:0007829|PDB:1QXR"
FT TURN 12..14
FT /evidence="ECO:0007829|PDB:4LUK"
FT STRAND 22..26
FT /evidence="ECO:0007829|PDB:4LUK"
FT HELIX 27..30
FT /evidence="ECO:0007829|PDB:4LUK"
FT TURN 31..33
FT /evidence="ECO:0007829|PDB:1QXR"
FT HELIX 37..46
FT /evidence="ECO:0007829|PDB:4LUK"
FT STRAND 50..57
FT /evidence="ECO:0007829|PDB:4LUK"
FT STRAND 66..73
FT /evidence="ECO:0007829|PDB:4LUK"
FT STRAND 91..94
FT /evidence="ECO:0007829|PDB:4LUM"
FT STRAND 97..111
FT /evidence="ECO:0007829|PDB:4LUK"
FT STRAND 117..122
FT /evidence="ECO:0007829|PDB:4LUK"
FT STRAND 127..130
FT /evidence="ECO:0007829|PDB:4LUK"
FT STRAND 135..140
FT /evidence="ECO:0007829|PDB:4LUK"
FT STRAND 142..144
FT /evidence="ECO:0007829|PDB:4LUK"
FT STRAND 146..153
FT /evidence="ECO:0007829|PDB:4LUK"
FT HELIX 161..166
FT /evidence="ECO:0007829|PDB:4LUK"
FT STRAND 169..175
FT /evidence="ECO:0007829|PDB:4LUK"
FT STRAND 178..183
FT /evidence="ECO:0007829|PDB:4LUK"
SQ SEQUENCE 189 AA; 21476 MW; C5D8380C59F2A785 CRC64;
MYKEPFGVKV DFETGIIEGA KKSVRRLSDM EGYFVDERAW KELVEKEDPV VYEVYAVEQE
EKEGDLNFAT TVLYPGKVGK EFFFTKGHFH AKLDRAEVYV ALKGKGGMLL QTPEGDAKWI
SMEPGTVVYV PPYWAHRTVN IGDEPFIFLA IYPADAGHDY GTIAEKGFSK IVIEENGEVK
VVDNPRWKK
