ID   G6PI_CHLPN              Reviewed;         526 AA.
AC   Q9Z6N4; Q9JS76; Q9K1X5;
DT   02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   02-NOV-2001, sequence version 2.
DT   03-AUG-2022, entry version 135.
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=CPn_1025, CP_0827, CpB1064;
OS   Chlamydia pneumoniae (Chlamydophila pneumoniae).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=83558;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CWL029;
RX   PubMed=10192388; DOI=10.1038/7716;
RA   Kalman S., Mitchell W.P., Marathe R., Lammel C.J., Fan J., Hyman R.W.,
RA   Olinger L., Grimwood J., Davis R.W., Stephens R.S.;
RT   "Comparative genomes of Chlamydia pneumoniae and C. trachomatis.";
RL   Nat. Genet. 21:385-389(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AR39;
RX   PubMed=10684935; DOI=10.1093/nar/28.6.1397;
RA   Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O.,
RA   Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S.,
RA   Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J.,
RA   Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G.,
RA   Salzberg S.L., Eisen J.A., Fraser C.M.;
RT   "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae
RT   AR39.";
RL   Nucleic Acids Res. 28:1397-1406(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J138;
RX   PubMed=10871362; DOI=10.1093/nar/28.12.2311;
RA   Shirai M., Hirakawa H., Kimoto M., Tabuchi M., Kishi F., Ouchi K.,
RA   Shiba T., Ishii K., Hattori M., Kuhara S., Nakazawa T.;
RT   "Comparison of whole genome sequences of Chlamydia pneumoniae J138 from
RT   Japan and CWL029 from USA.";
RL   Nucleic Acids Res. 28:2311-2314(2000).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TW-183;
RA   Geng M.M., Schuhmacher A., Muehldorfer I., Bensch K.W., Schaefer K.P.,
RA   Schneider S., Pohl T., Essig A., Marre R., Melchers K.;
RT   "The genome sequence of Chlamydia pneumoniae TW183 and comparison with
RT   other Chlamydia strains based on whole genome sequence analysis.";
RL   Submitted (MAY-2002) 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, ECO:0000305}.
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DR   EMBL; AE001363; AAD19162.1; -; Genomic_DNA.
DR   EMBL; AE002161; AAF38620.1; -; Genomic_DNA.
DR   EMBL; BA000008; BAA99232.1; -; Genomic_DNA.
DR   EMBL; AE009440; AAP98993.1; -; Genomic_DNA.
DR   PIR; B81533; B81533.
DR   PIR; C72005; C72005.
DR   PIR; F86618; F86618.
DR   RefSeq; NP_225219.1; NC_000922.1.
DR   RefSeq; WP_010895403.1; NZ_LN846995.1.
DR   AlphaFoldDB; Q9Z6N4; -.
DR   SMR; Q9Z6N4; -.
DR   STRING; 115711.CP_0827; -.
DR   EnsemblBacteria; AAD19162; AAD19162; CPn_1025.
DR   EnsemblBacteria; AAF38620; AAF38620; CP_0827.
DR   KEGG; cpa:CP_0827; -.
DR   KEGG; cpj:pgi; -.
DR   KEGG; cpn:CPn_1025; -.
DR   KEGG; cpt:CpB1064; -.
DR   PATRIC; fig|115713.3.peg.1123; -.
DR   eggNOG; COG0166; Bacteria.
DR   HOGENOM; CLU_017947_3_1_0; -.
DR   UniPathway; UPA00109; UER00181.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000000583; Chromosome.
DR   Proteomes; UP000000801; 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.
FT   CHAIN           1..526
FT                   /note="Glucose-6-phosphate isomerase"
FT                   /id="PRO_0000180619"
FT   ACT_SITE        347
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT   ACT_SITE        378
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT   ACT_SITE        493
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT   VARIANT         354
FT                   /note="V -> A (in strain: CWL029 and TW-183)"
FT   CONFLICT        41
FT                   /note="L -> W (in Ref. 2; AAF38620)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        477
FT                   /note="F -> L (in Ref. 1; AAD19162)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   526 AA;  57596 MW;  B89E515860235912 CRC64;
     MERKRFIDCD STKILQELAL NPLDLTAPGV LSAERIKKFS LLGGGFTFSF ATERLDDAIL
     AALISLAEER GLHESMLAMQ QGQVVNYIEG FPSEMRPALH TATRAWVTDS SFTGEAEDIA
     VRSRVEAQRL KDFLTKVRSQ FTTIVQIGIG GSELGPKALY RALRAYCPTD KHVHFISNID
     PDNGAEVLDT IDCAKALVVV VSKSGTTIET AVNEAFFADY FAKKGLSFKD HFIAVTCEGS
     PMDDTGKYLE VFHLWESIGG RFSSTSMVGG VVLGFAYGFE VFLQLLQGAS AMDQIALQPN
     ARENLPMLSA LISIWNRNFL GYPTEAVIPY SSGLEFFPAH LQQCCMESNG KSIVQDGRRV
     GFSTSPVIWG EPGTNGQHSF FQCLHQGTDI IPVEFIGFEK SQKGEDISFQ GTTSSQKLFA
     NMIAQAIALA CGSENTNPNK NFDGNRPSSV LVSSQLNPYS LGELLSYYEN KIVFQGFCWG
     INSFDQEGVS LGKALANRVL ELLEGADASN FPEAASLLTL FNIKFR