ID A0A292RGH7_9BACT Unreviewed; 462 AA.
AC A0A292RGH7;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
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=CPT80_03195 {ECO:0000313|EMBL:DAA97206.1};
OS Candidatus Gastranaerophilales bacterium HUM_9.
OC Bacteria; Candidatus Melainabacteria; Candidatus Gastranaerophilales.
OX NCBI_TaxID=1916320 {ECO:0000313|EMBL:DAA97206.1, ECO:0000313|Proteomes:UP000218540};
RN [1] {ECO:0000313|EMBL:DAA97206.1, ECO:0000313|Proteomes:UP000218540}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HUM_9 {ECO:0000313|EMBL:DAA97206.1};
RX PubMed=28360330; DOI=.1126/science.aal3794;
RA Soo R.M., Hemp J., Parks D.H., Fischer W.W., Hugenholtz P.;
RT "On the origins of oxygenic photosynthesis and aerobic respiration in
RT Cyanobacteria.";
RL Science 355:1436-1440(2017).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:DAA97206.1}.
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DR EMBL; DABG01000009; DAA97206.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A292RGH7; -.
DR STRING; 1916320.GCA_002103075_00550; -.
DR UniPathway; UPA00109; UER00181.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000218540; 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 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 {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 294
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
FT ACT_SITE 323
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
FT ACT_SITE 436
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
SQ SEQUENCE 462 AA; 51789 MW; AFFA13387C7F97A1 CRC64;
MIELNYKYAD ALVIGEENGL NLEQEFANYK ETIANIITDL NQRKDKPGQW LQWMNLGYNE
ETVWYVKEFA SMVKGKFDNI LVLGIGGSAL GGIAVTEALL KPYWNMLTPE QRDGMPRIFF
LDNIDPDSIT GLLEMLDLKK TLVNVITKSG STAETMSQYM IVKNLLEQEL GDEYRKNIVA
TTDKMTGVLR QLADQEGYKT FVVPDDVGGR FSVFSAVGLV PFALVGLNID EIIQGVKDMD
LALKNTDINN NIAAQNALIH YLMDTKKGKN LSVMMPYSSR LKYVSDWYVQ LWAESLGKED
NKNGEKVHVG PTPIKAVGAT DQHSQIQLYN EGPNDKVINF IRVGKFEHTL EIPKIFEYTG
IGYLGGKTVN DLINAEADST RVALSDYQRP TITITLPEID EYNVAQLLYM LEVQTAIAGE
LYNINTFNQP GVEQAKNYTY ALMGRSGYED SAKRIQSKMA TV
//
