G6PI_ZYMMO
ID G6PI_ZYMMO Reviewed; 507 AA.
AC P28718; Q5NN74;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 115.
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}; OrderedLocusNames=ZMO1212;
OS Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC Zymomonadaceae; Zymomonas.
OX NCBI_TaxID=264203;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1708765; DOI=10.1128/jb.173.10.3215-3223.1991;
RA Hesman T.L., Barnell W.O., Conway T.;
RT "Cloning, characterization, and nucleotide sequence analysis of a Zymomonas
RT mobilis phosphoglucose isomerase gene that is subject to carbon source-
RT dependent regulation.";
RL J. Bacteriol. 173:3215-3223(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31821 / ZM4 / CP4;
RX PubMed=15592456; DOI=10.1038/nbt1045;
RA Seo J.-S., Chong H., Park H.S., Yoon K.-O., Jung C., Kim J.J., Hong J.H.,
RA Kim H., Kim J.-H., Kil J.-I., Park C.J., Oh H.-M., Lee J.-S., Jin S.-J.,
RA Um H.-W., Lee H.-J., Oh S.-J., Kim J.Y., Kang H.L., Lee S.Y., Lee K.J.,
RA Kang H.S.;
RT "The genome sequence of the ethanologenic bacterium Zymomonas mobilis
RT ZM4.";
RL Nat. Biotechnol. 23:63-68(2005).
CC -!- FUNCTION: Provides a gateway for fructose into the Entner-Doudouroff
CC pathway.
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, ECO:0000305}.
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DR EMBL; M62957; AAA27698.1; -; Genomic_DNA.
DR EMBL; AE008692; AAV89836.1; -; Genomic_DNA.
DR PIR; A39411; A39411.
DR RefSeq; WP_011241031.1; NZ_CP035711.1.
DR AlphaFoldDB; P28718; -.
DR SMR; P28718; -.
DR STRING; 264203.ZMO1212; -.
DR PRIDE; P28718; -.
DR EnsemblBacteria; AAV89836; AAV89836; ZMO1212.
DR GeneID; 58026983; -.
DR KEGG; zmo:ZMO1212; -.
DR eggNOG; COG0166; Bacteria.
DR HOGENOM; CLU_017947_3_1_5; -.
DR OMA; IGVWYIN; -.
DR OrthoDB; 417261at2; -.
DR UniPathway; UPA00109; UER00181.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000001173; 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; Reference proteome.
FT CHAIN 1..507
FT /note="Glucose-6-phosphate isomerase"
FT /id="PRO_0000180777"
FT ACT_SITE 338
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT ACT_SITE 369
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT ACT_SITE 479
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
SQ SEQUENCE 507 AA; 55399 MW; 5B4E3B1C3CC09399 CRC64;
MARIANKAAI DAAWKQVSAC SEKTLKQLFE EDSNRLSGLV VETAKLRFDF SKNHLDSQKL
TAFKKLLEAC DFDARRKALF AGEKINITED RAVEHMAERG QGAPASVARA KEYHARMRTL
IEAIDAGAFG EVKHLLHIGI GGSALGPKLL IDALTRESGR YDVAVVSNVD GQALEEVFKK
FNPHKTLIAV ASKTFTTAET MLNAESAMEW MKKHGVEDPQ GRMIALTANP AKASEMGIDD
TRILPFAESI GGRYSLWSSI GFPAALALGW EGFQQLLEGG AAMDRHFLEA APEKNAPILA
AFADQYYSAV RGAQTHGIFA YDERLQLLPF YLQQLEMESN GKRVDLDGNL IDHPSAFITW
GGVGTDAQHA VFQLLHQGTR LVPIEFIAAI KADDTLNPVH HKTLLTNAFA QGAALMSGRD
NKDPARSYPG DRPSTTILME ELRPAQLGAL IAFYEHRTFT NGVLLGINSF DQFGVELGKE
MAHAIADHPE NSDFDPSTKA LIAAALK
