ID   G6PI_PORGI              Reviewed;         445 AA.
AC   Q7MUV9;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   03-AUG-2022, entry version 106.
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=PG_1368;
OS   Porphyromonas gingivalis (strain ATCC BAA-308 / W83).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC   Porphyromonas.
OX   NCBI_TaxID=242619;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-308 / W83;
RX   PubMed=12949112; DOI=10.1128/jb.185.18.5591-5601.2003;
RA   Nelson K.E., Fleischmann R.D., DeBoy R.T., Paulsen I.T., Fouts D.E.,
RA   Eisen J.A., Daugherty S.C., Dodson R.J., Durkin A.S., Gwinn M.L.,
RA   Haft D.H., Kolonay J.F., Nelson W.C., Mason T.M., Tallon L., Gray J.,
RA   Granger D., Tettelin H., Dong H., Galvin J.L., Duncan M.J., Dewhirst F.E.,
RA   Fraser C.M.;
RT   "Complete genome sequence of the oral pathogenic bacterium Porphyromonas
RT   gingivalis strain W83.";
RL   J. Bacteriol. 185:5591-5601(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; AE015924; AAQ66432.1; -; Genomic_DNA.
DR   RefSeq; WP_005874325.1; NC_002950.2.
DR   AlphaFoldDB; Q7MUV9; -.
DR   SMR; Q7MUV9; -.
DR   STRING; 242619.PG_1368; -.
DR   EnsemblBacteria; AAQ66432; AAQ66432; PG_1368.
DR   KEGG; pgi:PG_1368; -.
DR   eggNOG; COG0166; Bacteria.
DR   HOGENOM; CLU_037303_0_1_10; -.
DR   OMA; NNIGEDY; -.
DR   OrthoDB; 417261at2; -.
DR   BioCyc; PGIN242619:G1G02-1274-MON; -.
DR   UniPathway; UPA00109; UER00181.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000000588; 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..445
FT                   /note="Glucose-6-phosphate isomerase"
FT                   /id="PRO_0000180703"
FT   ACT_SITE        284
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT   ACT_SITE        305
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT   ACT_SITE        419
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
SQ   SEQUENCE   445 AA;  48967 MW;  17052160EECFAFAF CRC64;
     MERIRLDLSK TGSSVASYGE TAEKFNALLD NGTGRGSDFL GWVHLPSSIT EEELNAVEAA
     ATILRERCDY VINVGIGGSY LGARAVIEAL QNSFEAYRSD RENPVILYAG NNIGEDYLSE
     LLQFLRDKRF GIIYISKSGT TTEPAIAFRL LKGLLESQVG REDARERIVA VTDSAKGALR
     RMADEEGYRS FVIPDNVGGR FSVLTPVGLL PVAVAGFDIR QLVRGAADMQ AMTASDIPFS
     DNPALRYAAA RNALYAEGKK IEILANFHPK MHYIGEWWKQ LFGESEGKEE KGIFTATVDL
     TTDLHSMGQW MQEGERTIFE TVISVENQDT CLTIPSDSAD LDGLNFLAGK RVDEVNKMAE
     LGTRLAHVDG GVPNIRIILP QLDAYYIGQL FYFFEKAVGV SGYMLGVNPF DQPGVEGYKN
     NMFALLNKPG YETESAAMAG RLKEC