ID C7DF78_9RHOB Unreviewed; 533 AA.
AC C7DF78;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 63.
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:EET49689.1};
GN ORFNames=TR2A62_0525 {ECO:0000313|EMBL:EET49689.1};
OS Thalassobium sp. R2A62.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Thalassobium.
OX NCBI_TaxID=633131 {ECO:0000313|EMBL:EET49689.1, ECO:0000313|Proteomes:UP000004701};
RN [1] {ECO:0000313|EMBL:EET49689.1, ECO:0000313|Proteomes:UP000004701}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R2A62 {ECO:0000313|EMBL:EET49689.1,
RC ECO:0000313|Proteomes:UP000004701};
RA Suzuki M., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases.
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; GG697169; EET49689.1; -; Genomic_DNA.
DR RefSeq; WP_009160739.1; NZ_GG697169.2.
DR AlphaFoldDB; C7DF78; -.
DR STRING; 633131.TR2A62_0525; -.
DR eggNOG; COG0166; Bacteria.
DR HOGENOM; CLU_017947_3_1_5; -.
DR OrthoDB; 140919at2; -.
DR UniPathway; UPA00109; UER00181.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000004701; Unassembled WGS sequence.
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:UP000004701}.
FT ACT_SITE 338
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
FT ACT_SITE 369
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
FT ACT_SITE 498
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
SQ SEQUENCE 533 AA; 57642 MW; AAAF7C6B68CF9215 CRC64;
MWNDLKARHA LVADRTILDL FEPERAGDYA VEASDMRLDY SKTNIDAETR DLLFKLLEDA
GVADKRAAMF GGATINDTEG RAVLHTALRN LDGGPIEVDG ADVMPEVLAT LDRMSAFAGA
VRSGEFAGQG GKITDVINIG IGGSDLGPAM ATIAMSPYHD GPRTHFVSNV DGADIAEVLA
ACDPTTTLVI VASKTFTTTE TMTNARTAKA WMSDAVDNPA SQFAALSTSE EKTADFGIPA
DRVFGFEDWV GGRYSMWGPI GLSLMIAIGD DAFRAMLRGA QSMDVHFLNA EWRENMPAIL
AVVGIWHNQV CGYATRAVLP YDNRLARLPA YLQQLEMESN GKRVAMDGTE LDVPSGPVVW
GEPGTNGQHA FYQLIHQGTR VIPCEFLVAA EGFEPELRHQ HVLLMANCLA QSEALMKGRS
MDEARAITEK KGLEGKELER QAAHRVFPGN RPSVTIAYPK LTPCVLGQII ALYEHRVFVE
GVVLGINSYD QWGVELGKEL ATALQPVVEG TESADGKDGS TAALVAFLHK HHS
//
