ID E0WQQ8_9ENTR Unreviewed; 553 AA.
AC E0WQQ8;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 60.
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 ECO:0000313|EMBL:EFL92468.1};
GN ORFNames=REG_0250 {ECO:0000313|EMBL:EFL92468.1};
OS Candidatus Regiella insecticola LSR1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; aphid secondary symbionts; Regiella.
OX NCBI_TaxID=663321 {ECO:0000313|EMBL:EFL92468.1, ECO:0000313|Proteomes:UP000005726};
RN [1] {ECO:0000313|EMBL:EFL92468.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LSR1 {ECO:0000313|EMBL:EFL92468.1};
RX PubMed=19840097;
RA Degnan P.H., Leonardo T.E., Cass B.N., Hurwitz B., Stern D., Gibbs R.A.,
RA Richards S., Moran N.A.;
RT "Dynamics of genome evolution in facultative symbionts of aphids.";
RL Environ. Microbiol. 0:0-0(2009).
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; GL379589; EFL92468.1; -; Genomic_DNA.
DR RefSeq; WP_006704188.1; NZ_GL379589.1.
DR AlphaFoldDB; E0WQQ8; -.
DR STRING; 663321.REG_0250; -.
DR eggNOG; COG0166; Bacteria.
DR HOGENOM; CLU_017947_3_1_6; -.
DR UniPathway; UPA00109; UER00181.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000005726; Miscellaneous, Scaffold Scaffold1.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000005726}.
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 517
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
SQ SEQUENCE 553 AA; 62699 MW; 4CA76EAC00D0839A CRC64;
MKNINPSETK AWKALQQHFA EMKKIHIRDL FKENAERFSQ FSITIEDEML VDYSKNRINA
ETMKKLQALA TETHLKDAID SMFSGEKINR TEDRAVLHTA LRNRDNHPVL LDGKDVMPEV
NKVLARMEEF CKCVIEGEWK GYSGKAITDV VNIGIGGSDL GPYMVTEALA HNKNHLHMHF
VSNIDGTHII ETLKKLNPET TLFLIASKTF TTQETMTNAH SAREWLLKTV KEKSDIAKHF
VALSTNSEAV SKFGIDTRNM FEFWDWVGGR YSLWSAVGLS IALSIGFENF KNLLEGAHAM
DKHFKEAPAE KNAPVLLALI GIWYNNFFGA ETEAILPYDQ YMHRFPAYCQ QGNMESNGKC
VDRDGKRVTY QTGSIIWGEP GTNGQHAFYQ LIHQGTKMIP CDFIAPAISH NPLNNHHDIL
LSNFFAQTEA LAFGKTCPEE IEVEKKTTAT DKKPEQITEV IPCKEFEGNK PTNSILLREI
NPFNLGMLIA LYEHKIFTQG AILNIFSFDQ WGVELGKQLA NNILPVLRNN EKISTNDGST
NALINQFKKW RKN
//
