ID A0A238TDD3_9NEIS Unreviewed; 556 AA.
AC A0A238TDD3;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
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:SNB79697.1};
GN ORFNames=KEBURONENSIS_01797 {ECO:0000313|EMBL:SMQ13055.1},
GN KEBURONENSIS_01799 {ECO:0000313|EMBL:SNB79697.1};
OS Kingella negevensis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Kingella.
OX NCBI_TaxID=1522312 {ECO:0000313|EMBL:SNB79697.1, ECO:0000313|Proteomes:UP000215450};
RN [1] {ECO:0000313|EMBL:SMQ13055.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Kingella_eburonensis {ECO:0000313|EMBL:SMQ13055.1};
RA Song R., Chenine A.L., Ruprecht R.M.;
RL Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:SNB79697.1, ECO:0000313|Proteomes:UP000215450}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Kingella_eburonensis {ECO:0000313|EMBL:SNB79697.1};
RA Kim H.J., Triplett B.A.;
RL Submitted (JUN-2017) 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; FXUV01000042; SMQ13055.1; -; Genomic_DNA.
DR EMBL; FXUV02000046; SNB79697.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A238TDD3; -.
DR STRING; 1522312.GCA_900177895_02218; -.
DR OrthoDB; 140919at2; -.
DR UniPathway; UPA00109; UER00181.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000215450; 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:UP000215450}.
FT ACT_SITE 352
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
FT ACT_SITE 383
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
FT ACT_SITE 511
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
SQ SEQUENCE 556 AA; 62854 MW; 325A2F792706EAAF CRC64;
MSHPTNLPAW QALQKNFEQT RNEHMREMFE KDPARAERYW LEVGGVHVDF SKNRINDTIL
ANLVDLAKQS GLQERMQQMF NGEKINQTEN RAVLHVALRN RSNRPIKVDG QDVMPEVNSV
LKRMGEFAHA VRSGEWLGYT NQVITDVVNI GIGGSDLGPY MMCTALEDFG HPRLNMHFVS
NVDGAQLRDT LEKVHPETTL FIIASKTFTT QETLTNAQTA RKWFLKEGSE KDIAKHFVAV
STNKKAVAEF GIDTDHMFEF WDWVGGRYSL WSAIGLPIML YLSEENFIEM LEGAHEMDNH
FINTPLEKNL PALLGLVGIW YINFYGGGSQ VIAPYDQHLH RLPRFIQQLD MESNGKQVQM
DGTPVQTETG PIIWGETGIN GQHAFFQLLH QGTHVTPIDL IASLEKRSNL PGHHEILLSN
VFAQAEAFMR GKTPEEARAE LQAQGVSADR IDALVSHKTF SGNRPTNMIL LDRLNPRNLG
SLIAMYEHKV FTQGVVWGIN SFDQWGVELG KQLAKTILAE LTNTIDPQKH DTSTSRLIRL
YRQVNCAEDG TCDLLK
//
