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 27-MAR-2024, entry version 105. 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; Thermoproteota; 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 / RC 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 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 NCBIfam; TIGR02128; G6PI_arch; 1. DR Pfam; PF10432; bact-PGI_C; 1. DR SUPFAM; SSF53697; SIS domain; 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 //