ID Q79E36_MYCGL Unreviewed; 428 AA.
AC Q79E36;
DT 10-MAY-2005, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2005, sequence version 1.
DT 27-MAR-2024, entry version 82.
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_R {ECO:0000313|EMBL:AAO37621.1};
GN Synonyms=pgi {ECO:0000256|HAMAP-Rule:MF_00473};
OS Mycoplasmoides gallisepticum (Mycoplasma gallisepticum).
OC Bacteria; Mycoplasmatota; Mycoplasmoidales; Mycoplasmoidaceae;
OC Mycoplasmoides.
OX NCBI_TaxID=2096 {ECO:0000313|EMBL:AAO37621.1};
RN [1] {ECO:0000313|EMBL:AAO37621.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=A5969 {ECO:0000313|EMBL:AAO37621.1};
RX PubMed=8754006;
RA Skamrov A.V., Bibilashvili R.Sh.;
RT "A physical map of Mycoplasma gallisepticum strain A5969 genome and
RT determination of its positions on certain genes.";
RL Mol. Biol. (Mosk.) 30:585-594(1996).
RN [2] {ECO:0000313|EMBL:AAO37621.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=A5969 {ECO:0000313|EMBL:AAO37621.1};
RA Skamrov A., Feoktistova E., Goldman M., Beabealashvilli R.;
RL Submitted (FEB-2003) 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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00473}.
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DR EMBL; L35043; AAO37621.1; -; Genomic_DNA.
DR RefSeq; WP_065164838.1; NZ_MATN01000050.1.
DR AlphaFoldDB; Q79E36; -.
DR UniPathway; UPA00109; UER00181.
DR UniPathway; UPA00138; -.
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 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 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 282
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
FT ACT_SITE 419
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
SQ SEQUENCE 428 AA; 48712 MW; 4122318DDA0024E9 CRC64;
MIKLTFNLIK GLDYKKLDKN YQAKLDEIFS QLKNKKTPSA NMLGWIDYVD QDHTKIYKSI
DNKIAEWDKL KVTDVVVIGI GGSFTGIKAI LDVVAYLPSE QKRQIHFIRS LSENSFLKVL
EEIKDKNWGI VVISKSGTTL EPSVGFKLFR EALYKQYGEQ AQKRIVAITD PKKGVLHDIA
VKNKYEMLPI YSDIGGRFST ITPSGLLVAG LVGADYKQLI EGAKKAKADL FASSELKKNS
AYTYAALRHY LYTEMKKDVE IAITYEEQHE YLMLQHRQLF GESEGKSLNS LFPTYSVFTT
DLHSMGQLYQ DGKKIFFETV FSFEKANKNK LKLKNSEFNN DDQLDYLTKK SVNQLNYVAC
EATKQAHASA GVPIIEIDVK ENSAYGFGYL YFWLCVATSV SALLLGHDPY NQPGVEDYKQ
RMFKLLKE
//
