G6PI_SYNE7
ID G6PI_SYNE7 Reviewed; 528 AA.
AC Q31LL0;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 86.
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=Synpcc7942_2029;
OS Synechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans
OS R2).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX NCBI_TaxID=1140;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7942 / FACHB-805;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Kyrpides N., Lykidis A., Richardson P.;
RT "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL Submitted (AUG-2005) 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; CP000100; ABB58059.1; -; Genomic_DNA.
DR RefSeq; WP_011244376.1; NC_007604.1.
DR AlphaFoldDB; Q31LL0; -.
DR SMR; Q31LL0; -.
DR STRING; 1140.Synpcc7942_2029; -.
DR PRIDE; Q31LL0; -.
DR EnsemblBacteria; ABB58059; ABB58059; Synpcc7942_2029.
DR KEGG; syf:Synpcc7942_2029; -.
DR eggNOG; COG0166; Bacteria.
DR HOGENOM; CLU_033288_0_0_3; -.
DR OMA; CPAYAYG; -.
DR OrthoDB; 417261at2; -.
DR BioCyc; SYNEL:SYNPCC7942_2029-MON; -.
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 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; PTHR11469; 1.
DR Pfam; PF00342; PGI; 2.
DR PRINTS; PR00662; G6PISOMERASE.
DR SUPFAM; SSF53697; SSF53697; 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..528
FT /note="Glucose-6-phosphate isomerase"
FT /id="PRO_0000252658"
FT ACT_SITE 322
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT ACT_SITE 351
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT ACT_SITE 455
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
SQ SEQUENCE 528 AA; 57795 MW; DDBA0B6484B358FA CRC64;
MTAQQLWQRY LDWLYYDPSL EFYLDISRMG FDDAFVTSMQ PKFQHAFAAM AELEAGAIAN
PDEQRMVGHY WLRDPELAPT PELQTQIRDT LAAIQDFALK VHSGVLRPPT GSRFTDILSI
GIGGSALGPQ FVSEALRPQA ALLQIHFFDN TDPAGFDRVL ADLGDRLAST LVIVISKSGG
TPETRNGMLE VQSAFAQRGI AFAPQAVAVT GVGSHLDHVA ITERWLARFP MEDWVGGRTS
ELSAVGLLSA ALLGIDITAM LAGARQMDAL TRHSDLRQNP AALLALSWYW AGNGQGKKDM
VILPYKDSLL LFSRYLQQLI MESLGKERDL LGKVVHQGIA VYGNKGSTDQ HAYVQQLREG
IPNFFATFIE VLEDRQGPSP VVEPGITSGD YLSGLLQGTR AALYENGRES ITITVPRVDA
QQVGALIALY ERAVGLYASL VGINAYHQPG VEAGKKAAAG VLEIQRQIVE LLQQGQPLSI
AAIADDLGQS EQIETIYKIL RHLEANQRGV QLTGDRHNPL SLIASWQR