PGMI_PYRAE
ID PGMI_PYRAE Reviewed; 302 AA.
AC Q8ZWV0;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Bifunctional phosphoglucose/phosphomannose isomerase;
DE AltName: Full=Glucose-6-phosphate isomerase;
DE Short=GPI;
DE EC=5.3.1.9;
DE AltName: Full=Mannose-6-phosphate isomerase;
DE EC=5.3.1.8;
DE AltName: Full=Phosphoglucose isomerase;
DE Short=PGI;
DE AltName: Full=Phosphomannose isomerase;
DE Short=PMI;
GN OrderedLocusNames=PAE1610;
OS Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP
OS 104966 / NBRC 100827 / IM2).
OC Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Pyrobaculum.
OX NCBI_TaxID=178306;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2;
RX PubMed=11792869; DOI=10.1073/pnas.241636498;
RA Fitz-Gibbon S.T., Ladner H., Kim U.-J., Stetter K.O., Simon M.I.,
RA Miller J.H.;
RT "Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum
RT aerophilum.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:984-989(2002).
RN [2]
RP CHARACTERIZATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=15290326; DOI=10.1007/s00792-004-0411-6;
RA Hansen T., Urbanke C., Schoenheit P.;
RT "Bifunctional phosphoglucose/phosphomannose isomerase from the
RT hyperthermophilic archaeon Pyrobaculum aerophilum.";
RL Extremophiles 8:507-512(2004).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.16 ANGSTROMS) OF NATIVE PROTEIN AND IN COMPLEX
RP WITH 5-PHOSPHOARABINONATE, AND ISOMERIZATION MECHANISM.
RX PubMed=15252053; DOI=10.1074/jbc.m406855200;
RA Swan M.K., Hansen T., Schoenheit P., Davies C.;
RT "A novel phosphoglucose isomerase (PGI)/phosphomannose isomerase from the
RT crenarchaeon Pyrobaculum aerophilum is a member of the PGI superfamily:
RT structural evidence at 1.16-A resolution.";
RL J. Biol. Chem. 279:39838-39845(2004).
CC -!- FUNCTION: Catalyzes the isomerization of both glucose 6-phosphate and
CC epimeric mannose 6-phosphate at a similar catalytic efficiency.
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 -!- CATALYTIC ACTIVITY:
CC Reaction=D-mannose 6-phosphate = D-fructose 6-phosphate;
CC Xref=Rhea:RHEA:12356, ChEBI:CHEBI:58735, ChEBI:CHEBI:61527;
CC EC=5.3.1.8;
CC -!- ACTIVITY REGULATION: Inhibited by 5-phosphoarabinonate (PAB) and 6-
CC phosphogluconate.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.7 mM for glucose 6-phosphate (at 50 degrees Celsius)
CC {ECO:0000269|PubMed:15290326};
CC KM=0.3 mM for fructose 6-phosphate (at 50 degrees Celsius)
CC {ECO:0000269|PubMed:15290326};
CC KM=1.9 mM for glucose 6-phosphate (at 80 degrees Celsius)
CC {ECO:0000269|PubMed:15290326};
CC KM=0.06 mM for fructose 6-phosphate (at 80 degrees Celsius)
CC {ECO:0000269|PubMed:15290326};
CC KM=0.49 mM for mannose 6-phosphate (at 80 degrees Celsius)
CC {ECO:0000269|PubMed:15290326};
CC Vmax=50 mmol/min/mg enzyme with glucose 6-phosphate as substrate (at
CC 50 degrees Celsius) {ECO:0000269|PubMed:15290326};
CC Vmax=31.3 mmol/min/mg enzyme with fructose 6-phosphate as substrate
CC (at 50 degrees Celsius) {ECO:0000269|PubMed:15290326};
CC Vmax=150 mmol/min/mg enzyme with glucose 6-phosphate as substrate (at
CC 80 degrees Celsius) {ECO:0000269|PubMed:15290326};
CC Vmax=109 mmol/min/mg enzyme with fructose 6-phosphate as substrate
CC (at 80 degrees Celsius) {ECO:0000269|PubMed:15290326};
CC Vmax=117 mmol/min/mg enzyme with mannose 6-phosphate as substrate (at
CC 80 degrees Celsius) {ECO:0000269|PubMed:15290326};
CC pH dependence:
CC Optimum pH is 7.4. {ECO:0000269|PubMed:15290326};
CC Temperature dependence:
CC Optimum temperature is 100 degrees Celsius.
CC {ECO:0000269|PubMed:15290326};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15252053}.
CC -!- MISCELLANEOUS: The lack of any movement in response to the binding of
CC ligand may be due to its inherent thermostability, which would tend to
CC restrict any flexibility in the protein.
CC -!- SIMILARITY: Belongs to the PGI/PMI family. {ECO:0000305}.
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DR EMBL; AE009441; AAL63599.1; -; Genomic_DNA.
DR PDB; 1TZB; X-ray; 1.16 A; A/B=1-302.
DR PDB; 1TZC; X-ray; 1.45 A; A/B=1-302.
DR PDB; 1X9H; X-ray; 1.50 A; A/B=1-302.
DR PDB; 1X9I; X-ray; 1.16 A; A/B=1-302.
DR PDBsum; 1TZB; -.
DR PDBsum; 1TZC; -.
DR PDBsum; 1X9H; -.
DR PDBsum; 1X9I; -.
DR AlphaFoldDB; Q8ZWV0; -.
DR SMR; Q8ZWV0; -.
DR STRING; 178306.PAE1610; -.
DR EnsemblBacteria; AAL63599; AAL63599; PAE1610.
DR KEGG; pai:PAE1610; -.
DR PATRIC; fig|178306.9.peg.1186; -.
DR eggNOG; arCOG00052; Archaea.
DR HOGENOM; CLU_059687_0_1_2; -.
DR InParanoid; Q8ZWV0; -.
DR OMA; FPELNHN; -.
DR BRENDA; 5.3.1.8; 5239.
DR BRENDA; 5.3.1.9; 5239.
DR SABIO-RK; Q8ZWV0; -.
DR EvolutionaryTrace; Q8ZWV0; -.
DR Proteomes; UP000002439; Chromosome.
DR GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR GO; GO:0004347; F:glucose-6-phosphate isomerase activity; IEA:UniProtKB-EC.
DR GO; GO:0004476; F:mannose-6-phosphate isomerase activity; IEA:UniProtKB-EC.
DR GO; GO:1901135; P:carbohydrate derivative metabolic process; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd05017; SIS_PGI_PMI_1; 1.
DR CDD; cd05637; SIS_PGI_PMI_2; 1.
DR InterPro; IPR019490; Glu6P/Mann6P_isomerase_C.
DR InterPro; IPR001347; SIS_dom.
DR InterPro; IPR046348; SIS_dom_sf.
DR InterPro; IPR035484; SIS_PGI/PMI_1.
DR Pfam; PF10432; bact-PGI_C; 1.
DR SUPFAM; SSF53697; SSF53697; 1.
DR PROSITE; PS51464; SIS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Isomerase; Multifunctional enzyme; Reference proteome.
FT CHAIN 1..302
FT /note="Bifunctional phosphoglucose/phosphomannose
FT isomerase"
FT /id="PRO_0000227794"
FT DOMAIN 27..160
FT /note="SIS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00797"
FT ACT_SITE 203
FT /note="Proton acceptor"
FT /evidence="ECO:0000305"
FT ACT_SITE 219
FT /note="Proton donor"
FT /evidence="ECO:0000305"
FT ACT_SITE 298
FT /note="Proton acceptor"
FT /evidence="ECO:0000305"
FT BINDING 48
FT /ligand="substrate"
FT BINDING 87
FT /ligand="substrate"
FT BINDING 92
FT /ligand="substrate"
FT HELIX 3..9
FT /evidence="ECO:0007829|PDB:1TZB"
FT HELIX 10..14
FT /evidence="ECO:0007829|PDB:1TZB"
FT STRAND 23..27
FT /evidence="ECO:0007829|PDB:1TZB"
FT STRAND 30..33
FT /evidence="ECO:0007829|PDB:1TZB"
FT STRAND 38..43
FT /evidence="ECO:0007829|PDB:1TZB"
FT HELIX 46..61
FT /evidence="ECO:0007829|PDB:1TZB"
FT STRAND 65..71
FT /evidence="ECO:0007829|PDB:1TZB"
FT STRAND 79..86
FT /evidence="ECO:0007829|PDB:1TZB"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:1TZB"
FT HELIX 93..104
FT /evidence="ECO:0007829|PDB:1TZB"
FT STRAND 109..115
FT /evidence="ECO:0007829|PDB:1TZB"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:1TZB"
FT STRAND 121..123
FT /evidence="ECO:0007829|PDB:1TZB"
FT STRAND 125..127
FT /evidence="ECO:0007829|PDB:1TZB"
FT HELIX 134..137
FT /evidence="ECO:0007829|PDB:1TZB"
FT HELIX 138..153
FT /evidence="ECO:0007829|PDB:1TZB"
FT HELIX 168..178
FT /evidence="ECO:0007829|PDB:1TZB"
FT STRAND 183..187
FT /evidence="ECO:0007829|PDB:1TZB"
FT HELIX 188..190
FT /evidence="ECO:0007829|PDB:1TZB"
FT HELIX 191..203
FT /evidence="ECO:0007829|PDB:1TZB"
FT STRAND 210..214
FT /evidence="ECO:0007829|PDB:1TZB"
FT HELIX 216..219
FT /evidence="ECO:0007829|PDB:1TZB"
FT HELIX 221..224
FT /evidence="ECO:0007829|PDB:1TZB"
FT STRAND 229..233
FT /evidence="ECO:0007829|PDB:1TZB"
FT STRAND 235..237
FT /evidence="ECO:0007829|PDB:1TZB"
FT HELIX 239..252
FT /evidence="ECO:0007829|PDB:1TZB"
FT STRAND 255..258
FT /evidence="ECO:0007829|PDB:1TZB"
FT HELIX 263..284
FT /evidence="ECO:0007829|PDB:1TZB"
FT HELIX 292..300
FT /evidence="ECO:0007829|PDB:1TZB"
SQ SEQUENCE 302 AA; 33548 MW; 853E7B8E4BA9AA21 CRC64;
MSQLLQDYLN WENYILRRVD FPTSYVVEGE VVRIEAMPRL YISGMGGSGV VADLIRDFSL
TWNWEVEVIA VKDYFLKARD GLLIAVSYSG NTIETLYTVE YAKRRRIPAV AITTGGRLAQ
MGVPTVIVPK ASAPRAALPQ LLTAALHVVA KVYGIDVKIP EGLEPPNEAL IHKLVEEFQK
RPTIIAAESM RGVAYRVKNE FNENAKIEPS VEILPEAHHN WIEGSERAVV ALTSPHIPKE
HQERVKATVE IVGGSIYAVE MHPKGVLSFL RDVGIASVKL AEIRGVNPLA TPRIDALKRR
LQ
