ID   G6PI2_CUPPJ             Reviewed;         542 AA.
AC   Q471B8;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 100.
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}; OrderedLocusNames=Reut_A1649;
OS   Cupriavidus pinatubonensis (strain JMP 134 / LMG 1197) (Cupriavidus necator
OS   (strain JMP 134)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=264198;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JMP134 / LMG 1197;
RX   PubMed=20339589; DOI=10.1371/journal.pone.0009729;
RA   Lykidis A., Perez-Pantoja D., Ledger T., Mavromatis K., Anderson I.J.,
RA   Ivanova N.N., Hooper S.D., Lapidus A., Lucas S., Gonzalez B.,
RA   Kyrpides N.C.;
RT   "The complete multipartite genome sequence of Cupriavidus necator JMP134, a
RT   versatile pollutant degrader.";
RL   PLoS ONE 5:E9729-E9729(2010).
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00473}.
CC   -!- SIMILARITY: Belongs to the GPI family. {ECO:0000255|HAMAP-
CC       Rule:MF_00473}.
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DR   EMBL; CP000090; AAZ61015.1; -; Genomic_DNA.
DR   RefSeq; WP_011297813.1; NC_007347.1.
DR   AlphaFoldDB; Q471B8; -.
DR   SMR; Q471B8; -.
DR   STRING; 264198.Reut_A1649; -.
DR   EnsemblBacteria; AAZ61015; AAZ61015; Reut_A1649.
DR   KEGG; reu:Reut_A1649; -.
DR   eggNOG; COG0166; Bacteria.
DR   HOGENOM; CLU_017947_3_1_4; -.
DR   OMA; VERCKAM; -.
DR   OrthoDB; 417261at2; -.
DR   UniPathway; UPA00109; UER00181.
DR   UniPathway; UPA00138; -.
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   Gene3D; 1.10.1390.10; -; 1.
DR   HAMAP; MF_00473; G6P_isomerase; 1.
DR   InterPro; IPR001672; G6P_Isomerase.
DR   InterPro; IPR023096; G6P_Isomerase_C.
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; PTHR11469; 1.
DR   Pfam; PF00342; PGI; 1.
DR   PRINTS; PR00662; G6PISOMERASE.
DR   SUPFAM; SSF53697; SSF53697; 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   3: Inferred from homology;
KW   Cytoplasm; Gluconeogenesis; Glycolysis; Isomerase.
FT   CHAIN           1..542
FT                   /note="Glucose-6-phosphate isomerase 2"
FT                   /id="PRO_0000230930"
FT   ACT_SITE        353
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT   ACT_SITE        384
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT   ACT_SITE        505
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
SQ   SEQUENCE   542 AA;  59420 MW;  66588D86F2F0CC0F CRC64;
     MSTSLSAWQS LREHAAKIRH THMRDWFTGP QGQARSVRLT VEACGLTLDY AKNRVTEDTL
     SLLFALARQA RVCERRDAMF AGEPVNTTER RAALHMALRA HPGDGYRALG VPVEADVSAV
     LAQMERFARD VRSGSWTGFD GRAITDVVNI GIGGSDLGPR MVCRALEQDT EPGPRLHFVA
     NVDGYDLART LARLDAATTL VIVCSKTFTT LETMANARTA RDWFLRHGVT HSDLARHFVA
     VSTNRDAVAA FGIDPVNMFP FWDWVGGRFS LWSAVGLSIA VAIGFDRFRQ LLDGARAMDR
     HFAGAPPEQN LPMILGLLDV WYRSFLGTAS RCVAPYCEPL DLLPAFLQQL EMESNGKSVQ
     HDGAALEAGS AAVVWGTTGT NGQHAYFQMV HQGSQLVPVD FIACLQPHSD LPGHHTKLLA
     NCFAQGEALL RGRTADEVRA EGKADEALVP HLVFEGNRPS NTLLLQRLDA FHLGALLAMS
     EHRTFVQGAL WNINPFDQWG VELGKMLARP IERELEGAPP QPHDASTAAL IRRAAQFCAS
     TD