G6PI_STRMU
ID G6PI_STRMU Reviewed; 449 AA.
AC Q9X670;
DT 02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 119.
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}; Synonyms=gpi;
GN OrderedLocusNames=SMU_307;
OS Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=210007;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=LT11;
RX PubMed=10639465; DOI=10.1128/iai.68.2.925-930.2000;
RA Boyd D.A., Thevenot T., Gumbmann M., Honeyman A.L., Hamilton I.R.;
RT "Identification of the operon for the sorbitol (glucitol)
RT phosphoenolpyruvate:sugar phosphotransferase system in Streptococcus
RT mutans.";
RL Infect. Immun. 68:925-930(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700610 / UA159;
RX PubMed=12397186; DOI=10.1073/pnas.172501299;
RA Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT pathogen.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
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; AF132127; AAD33517.1; -; Genomic_DNA.
DR EMBL; AE014133; AAN58070.1; -; Genomic_DNA.
DR PIR; T51720; T51720.
DR RefSeq; NP_720764.1; NC_004350.2.
DR RefSeq; WP_002262911.1; NC_004350.2.
DR AlphaFoldDB; Q9X670; -.
DR SMR; Q9X670; -.
DR STRING; 210007.SMU_307; -.
DR PRIDE; Q9X670; -.
DR EnsemblBacteria; AAN58070; AAN58070; SMU_307.
DR KEGG; smu:SMU_307; -.
DR PATRIC; fig|210007.7.peg.266; -.
DR eggNOG; COG0166; Bacteria.
DR HOGENOM; CLU_037303_0_1_9; -.
DR OMA; NNIGEDY; -.
DR PhylomeDB; Q9X670; -.
DR UniPathway; UPA00109; UER00181.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000002512; 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 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; 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..449
FT /note="Glucose-6-phosphate isomerase"
FT /id="PRO_0000180737"
FT ACT_SITE 291
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT ACT_SITE 312
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT ACT_SITE 426
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
SQ SEQUENCE 449 AA; 49422 MW; 6ADB7E073F86A202 CRC64;
MTHIKFDYSK VLGKFLASHE LDYIQMQVTA ADEALRKGTG PGAEMTGWLN LPQNYDKEEF
ARIKKAAEKI KSDSEVLVVI GIGGSYLGAR AAIDFLNSSF VNLENKEERK APQILYAGNS
ISSNYLADLV DYVADKDFSV NVISKSGTTT EPAIAFRVFK DLLVKKYGQE EANQRIYATT
DRVKGAVKVE ADANGWETFV VPDSVGGRFT VLTAVGLLPI AASGADLDQL MAGAEAARQD
YSSAELSENE AYQYAAIRNI LYRKGYVTEV LANYEPSLQY FSEWWKQLAG ESEGKDQKGI
YPTSANFSTD LHSLGQFIQE GNRNLFETVI RVEKARKNIL VPEAAEDLDG LAYLQGKDVD
FVNKKATDGV LLAHTDGGVP NTFLTIPEQD EFTLGYVIYF FELAIGLSGY LNGVNPFDQP
GVEAYKKNMF ALLGKPGFEE LGAELNARL
