G6PI1_STRAW
ID G6PI1_STRAW Reviewed; 549 AA.
AC Q82M90;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Glucose-6-phosphate isomerase 1 {ECO:0000255|HAMAP-Rule:MF_00473};
DE Short=GPI 1 {ECO:0000255|HAMAP-Rule:MF_00473};
DE EC=5.3.1.9 {ECO:0000255|HAMAP-Rule:MF_00473};
DE AltName: Full=Phosphoglucose isomerase 1 {ECO:0000255|HAMAP-Rule:MF_00473};
DE Short=PGI 1 {ECO:0000255|HAMAP-Rule:MF_00473};
DE AltName: Full=Phosphohexose isomerase 1 {ECO:0000255|HAMAP-Rule:MF_00473};
DE Short=PHI 1 {ECO:0000255|HAMAP-Rule:MF_00473};
GN Name=pgi1 {ECO:0000255|HAMAP-Rule:MF_00473}; OrderedLocusNames=SAV_1770;
OS Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC
OS 14893 / NCIMB 12804 / NRRL 8165 / MA-4680).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=227882;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL
RC 8165 / MA-4680;
RX PubMed=11572948; DOI=10.1073/pnas.211433198;
RA Omura S., Ikeda H., Ishikawa J., Hanamoto A., Takahashi C., Shinose M.,
RA Takahashi Y., Horikawa H., Nakazawa H., Osonoe T., Kikuchi H., Shiba T.,
RA Sakaki Y., Hattori M.;
RT "Genome sequence of an industrial microorganism Streptomyces avermitilis:
RT deducing the ability of producing secondary metabolites.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:12215-12220(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL
RC 8165 / MA-4680;
RX PubMed=12692562; DOI=10.1038/nbt820;
RA Ikeda H., Ishikawa J., Hanamoto A., Shinose M., Kikuchi H., Shiba T.,
RA Sakaki Y., Hattori M., Omura S.;
RT "Complete genome sequence and comparative analysis of the industrial
RT microorganism Streptomyces avermitilis.";
RL Nat. Biotechnol. 21:526-531(2003).
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; BA000030; BAC69481.1; -; Genomic_DNA.
DR RefSeq; WP_010983209.1; NZ_JZJK01000086.1.
DR AlphaFoldDB; Q82M90; -.
DR SMR; Q82M90; -.
DR STRING; 227882.SAV_1770; -.
DR EnsemblBacteria; BAC69481; BAC69481; SAVERM_1770.
DR KEGG; sma:SAVERM_1770; -.
DR eggNOG; COG0166; Bacteria.
DR HOGENOM; CLU_017947_3_1_11; -.
DR OMA; VERCKAM; -.
DR OrthoDB; 417261at2; -.
DR UniPathway; UPA00109; UER00181.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000000428; 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..549
FT /note="Glucose-6-phosphate isomerase 1"
FT /id="PRO_0000180747"
FT ACT_SITE 358
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT ACT_SITE 389
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT ACT_SITE 513
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
SQ SEQUENCE 549 AA; 60210 MW; B856B99B5D47BC19 CRC64;
MSDSPRLTRR PEWTELEDHR AGPLLHPALR ELFAADPERA ERYVVRAGDL RLDYSKHLIT
DETLALLQEL ATATDVFGLR DAMFRGEKIN VTENRAVLHT ALRAPRDAVI EVDGENVVPA
VHAVLDRMAD FADRVRSGEW TGHTGSRIRT VVNIGIGGSD LGPAMAYEAL RAFTDRSLTV
RFVSNVDGAD LHEAVRDLDP AETLFVIASK TFTTIETITN ATSARSWLLA GLDGDEKAVA
KHFVALSTNA GKVSDFGIDT ANMFEFWDWV GGRYSFDSAI GLSLMIAIGP ERFRELLDGF
RIVDEHFRTA PAEANAPLLL GLLGVWYGSF FGAQSHAVLP YSHYLSKFTA YLQQLDMESN
GKSVDRDGHP VEWQTGPVVW GTPGTNGQHA YYQLLHQGTK VIPADLIGFI NPVDGLSDEL
AAQHDLLMAN LFAQGQALAF GKTGDEVRAE GVPEEQVPHR TFRGNHPTTT ILAAELTPSV
LGQLIALYEH KVFVQGAIWN IDSFDQWGVE LGKVLAKRVE PALTEGADVP GLDPSTAALV
AAYRTHRKK
