ID   G6PI_MYCPN              Reviewed;         430 AA.
AC   P78033;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   27-MAR-2024, entry version 122.
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=MPN_250;
GN   ORFNames=MP582;
OS   Mycoplasma pneumoniae (strain ATCC 29342 / M129 / Subtype 1)
OS   (Mycoplasmoides pneumoniae).
OC   Bacteria; Mycoplasmatota; Mycoplasmoidales; Mycoplasmoidaceae;
OC   Mycoplasmoides.
OX   NCBI_TaxID=272634;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29342 / M129 / Subtype 1;
RX   PubMed=8948633; DOI=10.1093/nar/24.22.4420;
RA   Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.;
RT   "Complete sequence analysis of the genome of the bacterium Mycoplasma
RT   pneumoniae.";
RL   Nucleic Acids Res. 24:4420-4449(1996).
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; U00089; AAB96230.1; -; Genomic_DNA.
DR   PIR; S73908; S73908.
DR   RefSeq; NP_109938.1; NC_000912.1.
DR   RefSeq; WP_010874607.1; NZ_OU342337.1.
DR   AlphaFoldDB; P78033; -.
DR   SMR; P78033; -.
DR   STRING; 272634.MPN_250; -.
DR   EnsemblBacteria; AAB96230; AAB96230; MPN_250.
DR   KEGG; mpn:MPN_250; -.
DR   PATRIC; fig|272634.6.peg.269; -.
DR   HOGENOM; CLU_037303_0_1_14; -.
DR   OrthoDB; 140919at2; -.
DR   BioCyc; MetaCyc:MONOMER-544; -.
DR   BioCyc; MPNE272634:G1GJ3-395-MONOMER; -.
DR   UniPathway; UPA00109; UER00181.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000000808; 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; GLUCOSE-6-PHOSPHATE ISOMERASE; 1.
DR   PANTHER; PTHR11469:SF1; GLUCOSE-6-PHOSPHATE ISOMERASE; 1.
DR   Pfam; PF00342; PGI; 1.
DR   PRINTS; PR00662; G6PISOMERASE.
DR   SUPFAM; SSF53697; SIS domain; 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..430
FT                   /note="Glucose-6-phosphate isomerase"
FT                   /id="PRO_0000180686"
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        420
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
SQ   SEQUENCE   430 AA;  48834 MW;  BBF48166F3DCBA70 CRC64;
     MESKWLTVDT KHLYGFDEAI FIQKYQKKVN QIHQQFLNQQ LPDGHMNGWY SQPDQDHKGL
     LKQINTIAKQ FNALKVTDIV YLGIGGSYTG IRAILDFLKP EQKANIKVHF VPDISAFNIA
     AVARAIKGKS WALVVTSKSG RTLEPAVTFR YFRNLLHKQY KQKHALRTVV ITDAVKGLLV
     GMSNQYGYAH LTIPSNIGGR FSTLSPAGLL LAKLCGHDPK QLLLGTLTAK QELANSDLNT
     NSAYYYAALR HWLYTTKKLK IEVTVAYHSA YEYLLLQHRQ LFGESEGKGG KSLFPTFSLF
     TTDLHSMGQL YQEGEKNFFE TVIQVQTQFH DLELPPSDFN NDDQLDYLLA KSMNEISNTA
     LEAVVEAHFQ SNVNIIKLTL KERTTFMFGY FYFWLSMATM MSGSLLGHNV FDQPGVEVYK
     QLMFAKLGRE
//