G6PI_MYCA1
ID G6PI_MYCA1 Reviewed; 554 AA.
AC A0QBN4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 78.
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=MAV_1068;
OS Mycobacterium avium (strain 104).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium avium complex (MAC).
OX NCBI_TaxID=243243;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=104;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CP000479; ABK66481.1; -; Genomic_DNA.
DR RefSeq; WP_011723919.1; NC_008595.1.
DR AlphaFoldDB; A0QBN4; -.
DR SMR; A0QBN4; -.
DR PRIDE; A0QBN4; -.
DR EnsemblBacteria; ABK66481; ABK66481; MAV_1068.
DR GeneID; 66692798; -.
DR KEGG; mav:MAV_1068; -.
DR HOGENOM; CLU_017947_3_1_11; -.
DR OMA; IGVWYIN; -.
DR OrthoDB; 417261at2; -.
DR UniPathway; UPA00109; UER00181.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000001574; 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 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; 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.
FT CHAIN 1..554
FT /note="Glucose-6-phosphate isomerase"
FT /id="PRO_1000013987"
FT REGION 527..554
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 358
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT ACT_SITE 389
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT ACT_SITE 515
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
SQ SEQUENCE 554 AA; 60652 MW; 780F82619506EF92 CRC64;
MTSVHTLPDI TATPAWDALR KHHDRIGDTH LRQFFEEDPD RGRELTVTVG DLYIDYSKHR
VTRETLRLLV DLARTAKLEE RRDQMFAGVH INTSEDRAVL HTALRLPRDA ELIVDGRNVV
ADVHEVLDAM GEFTDRLRSG EWTGATGKRI STVVNIGIGG SDLGPVMVYQ ALRHYADAGI
SARFVSNVDP ADLIATLADL DPATTLFIVA SKTFSTLETL TNATAARRWI TDALGDAAVA
HHFVAVSTNK RLVDDFGINT DNMFGFWDWV GGRYSVDSAI GLSVMAVIGR EAFADFLSGF
HIVDRHFQTA PLESNAPVLL GLIGLWYSNF MGAQSRAVLP YSNDLARFAA YLQQLTMESN
GKSTRADGSP VTTDTGEIFW GEPGTNGQHA FYQLLHQGTR LVPADFIGFS QPIDDLPTAE
GSGSMHDLLM SNFFAQTQVL AFGKTAEEIA AEGTPADIVP HKVMPGNRPS TSILANRLTP
SVLGQLIALY EHQVFTEGVI WGIDSFDQWG VELGKTQAKA LLPVITADNS PAPQSDSSTD
ALVRRYRSER GRTS