G6PI_MYCGA
ID G6PI_MYCGA Reviewed; 426 AA.
AC Q9KX58;
DT 02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 15-AUG-2003, sequence version 2.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Glucose-6-phosphate isomerase {ECO:0000255|HAMAP-Rule:MF_00473};
DE Short=GPI {ECO:0000255|HAMAP-Rule:MF_00473};
DE EC=5.3.1.9 {ECO:0000255|HAMAP-Rule:MF_00473};
DE AltName: Full=Phosphoglucose isomerase {ECO:0000255|HAMAP-Rule:MF_00473};
DE Short=PGI {ECO:0000255|HAMAP-Rule:MF_00473};
DE AltName: Full=Phosphohexose isomerase {ECO:0000255|HAMAP-Rule:MF_00473};
DE Short=PHI {ECO:0000255|HAMAP-Rule:MF_00473};
GN Name=pgi {ECO:0000255|HAMAP-Rule:MF_00473}; OrderedLocusNames=MYCGA6360;
GN ORFNames=MGA_0457;
OS Mycoplasma gallisepticum (strain R(low / passage 15 / clone 2))
OS (Mycoplasmoides gallisepticum).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=710127;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=A5969Var.B;
RA Skamrov A.V., Feoktistova E.S., Gol'dman M.A., Bibilashvili R.S.;
RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R(low / passage 15 / clone 2);
RX PubMed=12949158; DOI=10.1099/mic.0.26427-0;
RA Papazisi L., Gorton T.S., Kutish G., Markham P.F., Browning G.F.,
RA Nguyen D.K., Swartzell S., Madan A., Mahairas G., Geary S.J.;
RT "The complete genome sequence of the avian pathogen Mycoplasma
RT gallisepticum strain R(low).";
RL Microbiology 149:2307-2316(2003).
CC -!- FUNCTION: Catalyzes the reversible isomerization of glucose-6-phosphate
CC to fructose-6-phosphate. {ECO:0000255|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:0000255|HAMAP-Rule:MF_00473};
CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC {ECO:0000255|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:0000255|HAMAP-Rule:MF_00473}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00473}.
CC -!- SIMILARITY: Belongs to the GPI family. {ECO:0000255|HAMAP-
CC Rule:MF_00473, ECO:0000305}.
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DR EMBL; L35043; AAF36765.1; -; Genomic_DNA.
DR EMBL; AE015450; AAP56986.2; -; Genomic_DNA.
DR RefSeq; WP_011113896.1; NC_004829.2.
DR AlphaFoldDB; Q9KX58; -.
DR SMR; Q9KX58; -.
DR PRIDE; Q9KX58; -.
DR KEGG; mga:MGA_0457; -.
DR PATRIC; fig|233150.7.peg.713; -.
DR HOGENOM; CLU_037303_0_1_14; -.
DR OMA; NNIGEDY; -.
DR OrthoDB; 417261at2; -.
DR UniPathway; UPA00109; UER00181.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000001418; Chromosome.
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; PTHR11469; 1.
DR Pfam; PF00342; PGI; 1.
DR PRINTS; PR00662; G6PISOMERASE.
DR SUPFAM; SSF53697; SSF53697; 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; Gluconeogenesis; Glycolysis; Isomerase; Reference proteome.
FT CHAIN 1..426
FT /note="Glucose-6-phosphate isomerase"
FT /id="PRO_0000180678"
FT ACT_SITE 282
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT ACT_SITE 303
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT ACT_SITE 419
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT CONFLICT 65
FT /note="T -> A (in Ref. 1; AAF36765)"
FT /evidence="ECO:0000305"
FT CONFLICT 119
FT /note="I -> V (in Ref. 1; AAF36765)"
FT /evidence="ECO:0000305"
FT CONFLICT 123
FT /note="V -> I (in Ref. 1; AAF36765)"
FT /evidence="ECO:0000305"
FT CONFLICT 417
FT /note="N -> D (in Ref. 1; AAF36765)"
FT /evidence="ECO:0000305"
FT CONFLICT 426
FT /note="L -> LKE (in Ref. 1; AAF36765)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 426 AA; 48484 MW; 8C40A7D813D78357 CRC64;
MIKLTFNLIK GLDYKKLDKN YQAKLDEIFS QLKNKKTPSA NMLGWIDYVD QDHTKIYKSI
DNKITEWDKL KVTDVVVIGI GGSFTGIKAI LDVVAYLPSE QKRQIHFIRS LSENSFLKIL
EEVKDKNWGI 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 NQPGVENYKQ
RMFKLL
