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Database: UniProt
Entry: G3ADS8_9GAMM
LinkDB: G3ADS8_9GAMM
Original site: G3ADS8_9GAMM 
ID   G3ADS8_9GAMM            Unreviewed;       549 AA.
AC   G3ADS8;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   RecName: Full=Glucose-6-phosphate isomerase {ECO:0000256|HAMAP-Rule:MF_00473};
DE            Short=GPI {ECO:0000256|HAMAP-Rule:MF_00473};
DE            EC=5.3.1.9 {ECO:0000256|HAMAP-Rule:MF_00473};
DE   AltName: Full=Phosphoglucose isomerase {ECO:0000256|HAMAP-Rule:MF_00473};
DE            Short=PGI {ECO:0000256|HAMAP-Rule:MF_00473};
DE   AltName: Full=Phosphohexose isomerase {ECO:0000256|HAMAP-Rule:MF_00473};
DE            Short=PHI {ECO:0000256|HAMAP-Rule:MF_00473};
GN   Name=pgi {ECO:0000256|HAMAP-Rule:MF_00473};
GN   ORFNames=STA_A00390 {ECO:0000313|EMBL:CCB84940.1};
OS   Candidatus Steffania adelgidicola str. Klausen-Leopoldsdorf.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Steffania.
OX   NCBI_TaxID=994478 {ECO:0000313|EMBL:CCB84940.1};
RN   [1] {ECO:0000313|EMBL:CCB84940.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Klausen-Leopoldsdorf {ECO:0000313|EMBL:CCB84940.1};
RX   PubMed=21833037; DOI=10.1038/ismej.2011.102;
RA   Toenshoff E.R., Penz T., Narzt T., Collingro A., Schmitz-Esser S.,
RA   Pfeiffer S., Klepal W., Wagner M., Weinmaier T., Rattei T., Horn M.;
RT   "Bacteriocyte-associated gammaproteobacterial symbionts of the Adelges
RT   nordmannianae/piceae complex (Hemiptera: Adelgidae).";
RL   ISME J. 6:384-396(2012).
CC   -!- FUNCTION: Catalyzes the reversible isomerization of glucose-6-phosphate
CC       to fructose-6-phosphate. {ECO:0000256|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:0000256|ARBA:ARBA00029321,
CC         ECO:0000256|HAMAP-Rule:MF_00473, ECO:0000256|RuleBase:RU000612};
CC   -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC       {ECO:0000256|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:0000256|ARBA:ARBA00004926, ECO:0000256|HAMAP-Rule:MF_00473,
CC       ECO:0000256|RuleBase:RU000612}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00473}.
CC   -!- SIMILARITY: Belongs to the GPI family. {ECO:0000256|ARBA:ARBA00006604,
CC       ECO:0000256|HAMAP-Rule:MF_00473, ECO:0000256|RuleBase:RU000612}.
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DR   EMBL; FR872579; CCB84940.1; -; Genomic_DNA.
DR   AlphaFoldDB; G3ADS8; -.
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   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; 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 {ECO:0000256|HAMAP-Rule:MF_00473};
KW   Gluconeogenesis {ECO:0000256|ARBA:ARBA00022432, ECO:0000256|HAMAP-
KW   Rule:MF_00473};
KW   Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|HAMAP-
KW   Rule:MF_00473};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_00473}.
FT   ACT_SITE        355
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
FT   ACT_SITE        386
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
FT   ACT_SITE        514
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
SQ   SEQUENCE   549 AA;  62105 MW;  3564B934C39B76A7 CRC64;
     MKNINPTHTL AWKVLQQHFD VMKDVKISDL FRQDSERFLS FSATFHDYML VDYSKNRITA
     ETMMRLLALA KECGLKDAIA SMFQGEKINF TEDRAVLHIA LRNRSNTPIN VDGKNVMLDV
     NTVLGKMKIF CKRVINGEWK GYTGRTITDI VNIGIGGSDL GPYMVTEALR PYKNHLNVHY
     VSNIDGTHLA ETIKDLDPAT TLFLVASKTF TTQETMTNAQ SARDWFLKSA FDKKRIACHF
     IALSSNAKAV TEFGIDTQNM FEVWDWVGGR YSLWSAIGLS IALSLGFENF EKLLSGAHTM
     DQHFSSTPLD KNLPVLLALI SIWYNNFFNM ETEAILPYDQ YMHRLAAYFQ QGNMESNGKC
     VDRKGYVVNY QTGPIIWGEP GTNGQHAFYQ LIHQGTKIVP CDFIAAAISH NPLADHQDKL
     LSNFFAQTEA LAFGKSRAVV EKECSAVGKL TEEVQAILPF KVFEGNRPSN SILLREMTPH
     SLGALIALYE HKIFTQGVIF NIYSFDQWGV ELGKQLANRI LSELVSHELI DTHDSSTNAL
     INRYKSWRY
//
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