ID G6PI2_GEOSE Reviewed; 445 AA. AC P13376; DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1990, sequence version 1. DT 27-MAR-2024, entry version 116. DE RecName: Full=Glucose-6-phosphate isomerase 2 {ECO:0000255|HAMAP-Rule:MF_00473}; DE Short=GPI 2 {ECO:0000255|HAMAP-Rule:MF_00473}; DE EC=5.3.1.9 {ECO:0000255|HAMAP-Rule:MF_00473}; DE AltName: Full=Phosphoglucose isomerase 2 {ECO:0000255|HAMAP-Rule:MF_00473}; DE Short=PGI 2 {ECO:0000255|HAMAP-Rule:MF_00473}; DE AltName: Full=Phosphohexose isomerase 2 {ECO:0000255|HAMAP-Rule:MF_00473}; DE Short=PHI 2 {ECO:0000255|HAMAP-Rule:MF_00473}; GN Name=pgi2 {ECO:0000255|HAMAP-Rule:MF_00473}; Synonyms=pgiB; OS Geobacillus stearothermophilus (Bacillus stearothermophilus). OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Geobacillus. OX NCBI_TaxID=1422; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=T521; RX PubMed=2532320; DOI=10.1093/nar/17.23.10107; RA Tao W., Wang L., Shen R., Sheng Z.; RT "Complete nucleotide sequences of two phosphoglucoisomerase isozymes from RT Bacillus stearothermophilus."; RL Nucleic Acids Res. 17:10107-10108(1989). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS). RX PubMed=10318897; DOI=10.1073/pnas.96.10.5412; RA Sun Y.-J., Chou C.-C., Chen W.-S., Wu R.-T., Meng M., Hsiao C.-D.; RT "The crystal structure of a multifunctional protein: phosphoglucose RT isomerase/autocrine motility factor/neuroleukin."; RL Proc. Natl. Acad. Sci. U.S.A. 96:5412-5417(1999). CC -!- FUNCTION: Catalyzes the reversible isomerization of glucose-6-phosphate CC to fructose-6-phosphate. {ECO:0000255|HAMAP-Rule:MF_00473}. 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; Evidence={ECO:0000255|HAMAP-Rule:MF_00473}; CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis. CC {ECO:0000255|HAMAP-Rule:MF_00473}. CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3- CC phosphate and glycerone phosphate from D-glucose: step 2/4. CC {ECO:0000255|HAMAP-Rule:MF_00473}. CC -!- SUBUNIT: Homodimer. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00473}. CC -!- SIMILARITY: Belongs to the GPI family. {ECO:0000255|HAMAP- CC Rule:MF_00473, 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; X16640; CAA34635.1; -; Genomic_DNA. DR PIR; S06198; NUBSS. DR PDB; 1B0Z; X-ray; 2.30 A; A=1-445. DR PDB; 1C7Q; X-ray; 2.30 A; A=1-445. DR PDB; 1C7R; X-ray; 2.50 A; A=1-445. DR PDB; 2PGI; X-ray; 2.30 A; A=1-445. DR PDBsum; 1B0Z; -. DR PDBsum; 1C7Q; -. DR PDBsum; 1C7R; -. DR PDBsum; 2PGI; -. DR AlphaFoldDB; P13376; -. DR SMR; P13376; -. DR DrugBank; DB03042; 5-Phosphoarabinonic Acid. DR DrugBank; DB02257; N-Bromoacetyl-Aminoethyl Phosphate. DR BRENDA; 5.3.1.9; 623. DR SABIO-RK; P13376; -. DR UniPathway; UPA00109; UER00181. DR UniPathway; UPA00138; -. DR EvolutionaryTrace; P13376; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro. DR GO; GO:0004347; F:glucose-6-phosphate isomerase activity; IEA:UniProtKB-UniRule. DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniRule. DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule. DR CDD; cd05015; SIS_PGI_1; 1. DR CDD; cd05016; SIS_PGI_2; 1. DR HAMAP; MF_00473; G6P_isomerase; 1. DR InterPro; IPR001672; G6P_Isomerase. DR InterPro; IPR018189; Phosphoglucose_isomerase_CS. DR InterPro; IPR046348; SIS_dom_sf. DR InterPro; IPR035476; SIS_PGI_1. DR InterPro; IPR035482; SIS_PGI_2. DR PANTHER; PTHR11469; GLUCOSE-6-PHOSPHATE ISOMERASE; 1. DR PANTHER; PTHR11469:SF1; GLUCOSE-6-PHOSPHATE ISOMERASE; 1. DR Pfam; PF00342; PGI; 1. DR PRINTS; PR00662; G6PISOMERASE. DR SUPFAM; SSF53697; SIS domain; 1. DR PROSITE; PS00765; P_GLUCOSE_ISOMERASE_1; 1. DR PROSITE; PS00174; P_GLUCOSE_ISOMERASE_2; 1. DR PROSITE; PS51463; P_GLUCOSE_ISOMERASE_3; 1. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Gluconeogenesis; Glycolysis; Isomerase. FT CHAIN 1..445 FT /note="Glucose-6-phosphate isomerase 2" FT /id="PRO_0000180592" FT ACT_SITE 285 FT /note="Proton donor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473" FT ACT_SITE 306 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473" FT ACT_SITE 420 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473" FT STRAND 3..6 FT /evidence="ECO:0007829|PDB:1B0Z" FT HELIX 8..10 FT /evidence="ECO:0007829|PDB:1B0Z" FT TURN 11..13 FT /evidence="ECO:0007829|PDB:1C7Q" FT HELIX 16..21 FT /evidence="ECO:0007829|PDB:1B0Z" FT HELIX 23..34 FT /evidence="ECO:0007829|PDB:1B0Z" FT HELIX 41..43 FT /evidence="ECO:0007829|PDB:1B0Z" FT TURN 45..48 FT /evidence="ECO:0007829|PDB:1B0Z" FT HELIX 49..52 FT /evidence="ECO:0007829|PDB:1B0Z" FT HELIX 55..71 FT /evidence="ECO:0007829|PDB:1B0Z" FT STRAND 73..78 FT /evidence="ECO:0007829|PDB:1B0Z" FT HELIX 81..83 FT /evidence="ECO:0007829|PDB:1B0Z" FT HELIX 85..94 FT /evidence="ECO:0007829|PDB:1B0Z" FT HELIX 99..101 FT /evidence="ECO:0007829|PDB:1B0Z" FT STRAND 102..105 FT /evidence="ECO:0007829|PDB:1C7Q" FT STRAND 107..114 FT /evidence="ECO:0007829|PDB:1B0Z" FT HELIX 117..127 FT /evidence="ECO:0007829|PDB:1B0Z" FT STRAND 132..137 FT /evidence="ECO:0007829|PDB:1B0Z" FT STRAND 139..141 FT /evidence="ECO:0007829|PDB:1B0Z" FT HELIX 144..161 FT /evidence="ECO:0007829|PDB:1B0Z" FT HELIX 163..166 FT /evidence="ECO:0007829|PDB:1B0Z" FT HELIX 167..169 FT /evidence="ECO:0007829|PDB:1B0Z" FT STRAND 170..174 FT /evidence="ECO:0007829|PDB:1B0Z" FT HELIX 180..188 FT /evidence="ECO:0007829|PDB:1B0Z" FT STRAND 191..194 FT /evidence="ECO:0007829|PDB:1B0Z" FT TURN 207..210 FT /evidence="ECO:0007829|PDB:1B0Z" FT HELIX 211..217 FT /evidence="ECO:0007829|PDB:1B0Z" FT HELIX 221..235 FT /evidence="ECO:0007829|PDB:1B0Z" FT HELIX 240..242 FT /evidence="ECO:0007829|PDB:1B0Z" FT HELIX 244..257 FT /evidence="ECO:0007829|PDB:1B0Z" FT STRAND 262..269 FT /evidence="ECO:0007829|PDB:1B0Z" FT HELIX 270..272 FT /evidence="ECO:0007829|PDB:1B0Z" FT HELIX 273..287 FT /evidence="ECO:0007829|PDB:1B0Z" FT STRAND 295..300 FT /evidence="ECO:0007829|PDB:1B0Z" FT HELIX 303..306 FT /evidence="ECO:0007829|PDB:1B0Z" FT HELIX 309..314 FT /evidence="ECO:0007829|PDB:1B0Z" FT STRAND 319..328 FT /evidence="ECO:0007829|PDB:1B0Z" FT TURN 346..350 FT /evidence="ECO:0007829|PDB:1B0Z" FT HELIX 353..370 FT /evidence="ECO:0007829|PDB:1B0Z" FT STRAND 375..382 FT /evidence="ECO:0007829|PDB:1B0Z" FT HELIX 385..406 FT /evidence="ECO:0007829|PDB:1B0Z" FT HELIX 416..426 FT /evidence="ECO:0007829|PDB:1B0Z" FT TURN 430..432 FT /evidence="ECO:0007829|PDB:1C7Q" FT HELIX 433..441 FT /evidence="ECO:0007829|PDB:1B0Z" SQ SEQUENCE 445 AA; 50141 MW; 078AD337669D1AE1 CRC64; MAISFDYSNA LPFMQENELD YLSEFVKAAH HMLHERKGPG SDFLGWVDWP IRYDKNEFSR IKQAAERIRN HSDALVVIGI GGSYLGARAA IEALSHTFHN QMNDTTQIYF AGQNISSTYI SHLLDVLEGK DLSINVISKS GTTTEPAIAF RIFRDYMEKK YGKEEARKRI YVTTDRTKGA LKKLADQEGY ETFVIPDNIG GRYSVLTAVG LLPIAVAGLN IDRMMEGAAS AYHKYNNPDL LTNESYQYAA VRNILYRKGK AIELLVNYEP SLHYVSEWWK QLFGESEGKD QKGLFPASVD FTTDLHSMGQ YVQEGRRNLI ETVLHVKKPQ IELTIQEDPE NIDGLNFLAG KTLDEVNKKA FQGTLLAHVD GGVPNLIVEL DEMNEYTFGE MVYFFEKACG ISGHLLGVNP FDQPGVEAYK KNMFALLGKP GFEDEKAALM KRLSK //