G6PI_RHIE6
ID G6PI_RHIE6 Reviewed; 541 AA.
AC B3Q0A9;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Glucose-6-phosphate isomerase {ECO:0000255|HAMAP-Rule:MF_00473};
DE Short=GPI {ECO:0000255|HAMAP-Rule:MF_00473};
DE EC=5.3.1.9 {ECO:0000255|HAMAP-Rule:MF_00473};
DE AltName: Full=Phosphoglucose isomerase {ECO:0000255|HAMAP-Rule:MF_00473};
DE Short=PGI {ECO:0000255|HAMAP-Rule:MF_00473};
DE AltName: Full=Phosphohexose isomerase {ECO:0000255|HAMAP-Rule:MF_00473};
DE Short=PHI {ECO:0000255|HAMAP-Rule:MF_00473};
GN Name=pgi {ECO:0000255|HAMAP-Rule:MF_00473};
GN OrderedLocusNames=RHECIAT_CH0000548;
OS Rhizobium etli (strain CIAT 652).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX NCBI_TaxID=491916;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIAT 652;
RA Gonzalez V., Acosta J.L., Santamaria R.I., Bustos P.,
RA Hernandez-Gonzalez I.L., Fernandez J.L., Diaz R., Flores M., Mora J.,
RA Palacios R., Davila G.;
RT "Genome diversity and DNA divergence of Rhizobium etli.";
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001074; ACE89541.1; -; Genomic_DNA.
DR RefSeq; WP_012482526.1; NC_010994.1.
DR AlphaFoldDB; B3Q0A9; -.
DR SMR; B3Q0A9; -.
DR EnsemblBacteria; ACE89541; ACE89541; RHECIAT_CH0000548.
DR GeneID; 45955890; -.
DR KEGG; rec:RHECIAT_CH0000548; -.
DR eggNOG; COG0166; Bacteria.
DR HOGENOM; CLU_017947_3_1_5; -.
DR OMA; IGVWYIN; -.
DR UniPathway; UPA00109; UER00181.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000008817; Chromosome.
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..541
FT /note="Glucose-6-phosphate isomerase"
FT /id="PRO_1000125748"
FT ACT_SITE 346
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT ACT_SITE 377
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT ACT_SITE 506
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
SQ SEQUENCE 541 AA; 58611 MW; E748254923CFB303 CRC64;
MNAIVEQLKS TAAATKATDL RAAFAADAQR FSRFSVALDD LLMDFSKTAV NDDILKLLVK
LAEDGGVEKK REEMFSGKAI NFTEDRAVLH TALRNRSNTP VLVDGKDVMP DVNAVLAAMG
KFADEIRSGA LKGATGKAIT DVINIGIGGS DLGPVMATLA LAPFHDGPRA HFVSNIDGAH
IADILKLVQP ETTLFIVASK TFTTVETMTN AQTARNFIAK ALGEAAVQHH FAAVSTALDK
VAAFGIDSAR VFGFWDWVGG RYSIWSAIGL PLMIAIGPEN FGKFLDGAHA VDNHFRKAPI
TENLPMLLGL IGFYHRNVLG YPTRAILPYD QRLSRFPAYL QQLDMESNGK GVTIDGTPVE
GNSGPVVWGE PGTNGQHAFY QLIHQGTSII PAEFMIAANA FEPELRHQHQ LLISNVLAQS
EALMKGRTFA EAKKQLTDKG MDDKKADFIA PHRVFTGNRP SITFVYDKLT PYALGRLIAL
YEHRVFVEGV LFRINSFDQW GVELGKELAT GLLPVVEGKE SAEGHDSSTQ GLVAALAKLA
K