ID A0A1I1RI19_9BURK Unreviewed; 532 AA.
AC A0A1I1RI19;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=SAMN04489710_1013 {ECO:0000313|EMBL:SFD31888.1};
OS Paracidovorax konjaci.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Paracidovorax.
OX NCBI_TaxID=32040 {ECO:0000313|EMBL:SFD31888.1, ECO:0000313|Proteomes:UP000199517};
RN [1] {ECO:0000313|EMBL:SFD31888.1, ECO:0000313|Proteomes:UP000199517}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 7481 {ECO:0000313|EMBL:SFD31888.1,
RC ECO:0000313|Proteomes:UP000199517};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FOMQ01000001; SFD31888.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I1RI19; -.
DR STRING; 32040.SAMN04489710_1013; -.
DR OrthoDB; 140919at2; -.
DR UniPathway; UPA00109; UER00181.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000199517; 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}.
FT ACT_SITE 358
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
FT ACT_SITE 389
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
FT ACT_SITE 498
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
SQ SEQUENCE 532 AA; 57765 MW; 6DFCD2020384F342 CRC64;
MTTPPAVRTR CDRTAAWAAL QAHYAAGGRA FDIREAFAAD PQRFERFSQE APHVFADLSK
NRIDAAIEGL LLQLARECGV EAWRDAMFAG EAINHTEQRA VMHWLLREPP HAADSIEKFA
TNLVADGRRE VQATLQAMLD FAERVRADDG ITDIVNIGIG GSDLGPSMVA KALEDLRHPG
KRLHFVSNVD GAELGSVLRT LRAENTLFLI ASKTFTTAET MTNAHAARAW FVQQGGAEDA
VTRHFAALTT NIPAAAAFGI DTTFGFWDWV GGRYSLWSAI GLPVAIAVGA DAFRSLLAGA
HAMDTHFRTA PLERNLPVRL GLLDVWYRNF HGFATRSVAP YSHGLRRLPA YLQQLEMESN
GKGVDAAGEA LPFATSPVVW GEPGTNGQHA FFQMIHQGPD IVPVEFIALR EPGRDLADQH
PRLVANALAQ AKALMLGKAS DDGHRRFTGN RPSTFLVLER LDPAGLGALI ALYEHRVFVS
GALWGINSFD QWGVELGKVL AKELEPRLAS GDASGLDGST GGLLARLAHA RR
//
