G6PI_BACSU
ID G6PI_BACSU Reviewed; 450 AA.
AC P80860; O08330;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 4.
DT 03-AUG-2022, entry version 144.
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};
DE AltName: Full=Vegetative protein 54;
DE Short=VEG54;
GN Name=pgi {ECO:0000255|HAMAP-Rule:MF_00473}; Synonyms=yugL;
GN OrderedLocusNames=BSU31350;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9274030; DOI=10.1099/00221287-143-8-2769;
RA Oudega B., Koningstein G., Rodrigues L., de Sales Ramon M., Hilbert H.,
RA Duesterhoeft A., Pohl T.M., Weitzenegger T.;
RT "Analysis of the Bacillus subtilis genome: cloning and nucleotide sequence
RT of a 62 kb region between 275 degrees (rrnB) and 284 degrees (pai).";
RL Microbiology 143:2769-2774(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP SEQUENCE REVISION TO 6-9; 16; 63 AND 70.
RX PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT 168 reference genome a decade later.";
RL Microbiology 155:1758-1775(2009).
RN [4]
RP PROTEIN SEQUENCE OF 2-11.
RC STRAIN=168 / IS58;
RX PubMed=9298659; DOI=10.1002/elps.1150180820;
RA Antelmann H., Bernhardt J., Schmid R., Mach H., Voelker U., Hecker M.;
RT "First steps from a two-dimensional protein index towards a response-
RT regulation map for Bacillus subtilis.";
RL Electrophoresis 18:1451-1463(1997).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-38, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC STRAIN=168;
RX PubMed=17218307; DOI=10.1074/mcp.m600464-mcp200;
RA Macek B., Mijakovic I., Olsen J.V., Gnad F., Kumar C., Jensen P.R.,
RA Mann M.;
RT "The serine/threonine/tyrosine phosphoproteome of the model bacterium
RT Bacillus subtilis.";
RL Mol. Cell. Proteomics 6:697-707(2007).
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; Z93936; CAB07930.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15124.2; -; Genomic_DNA.
DR PIR; B69675; B69675.
DR RefSeq; NP_391013.2; NC_000964.3.
DR RefSeq; WP_003243401.1; NZ_JNCM01000033.1.
DR AlphaFoldDB; P80860; -.
DR SMR; P80860; -.
DR IntAct; P80860; 1.
DR MINT; P80860; -.
DR STRING; 224308.BSU31350; -.
DR iPTMnet; P80860; -.
DR jPOST; P80860; -.
DR PaxDb; P80860; -.
DR PRIDE; P80860; -.
DR EnsemblBacteria; CAB15124; CAB15124; BSU_31350.
DR GeneID; 937165; -.
DR KEGG; bsu:BSU31350; -.
DR PATRIC; fig|224308.179.peg.3399; -.
DR eggNOG; COG0166; Bacteria.
DR InParanoid; P80860; -.
DR OMA; CPAYAYG; -.
DR PhylomeDB; P80860; -.
DR BioCyc; BSUB:BSU31350-MON; -.
DR UniPathway; UPA00109; UER00181.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR GO; GO:0004347; F:glucose-6-phosphate isomerase activity; IBA:GO_Central.
DR GO; GO:0048029; F:monosaccharide binding; IBA:GO_Central.
DR GO; GO:0006094; P:gluconeogenesis; IBA:GO_Central.
DR GO; GO:0051156; P:glucose 6-phosphate metabolic process; IBA:GO_Central.
DR GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
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; 2.
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 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Gluconeogenesis; Glycolysis;
KW Isomerase; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9298659"
FT CHAIN 2..450
FT /note="Glucose-6-phosphate isomerase"
FT /id="PRO_0000180593"
FT ACT_SITE 290
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT ACT_SITE 311
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT ACT_SITE 425
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT MOD_RES 38
FT /note="Phosphothreonine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473,
FT ECO:0000269|PubMed:17218307"
FT CONFLICT 6..9
FT /note="FDYS -> LTTP (in Ref. 1; CAB07930)"
FT /evidence="ECO:0000305"
FT CONFLICT 16
FT /note="N -> PT (in Ref. 1; CAB07930)"
FT /evidence="ECO:0000305"
FT CONFLICT 63
FT /note="K -> Q (in Ref. 1; CAB07930)"
FT /evidence="ECO:0000305"
FT CONFLICT 70
FT /note="K -> Q (in Ref. 1; CAB07930)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 450 AA; 50543 MW; DAAA87AFB81E1DA0 CRC64;
MTHVRFDYSK ALTFFNEHEL TYLRDFVKTA HHNIHEKTGA GSDFLGWVDL PEHYDKEEFA
RIKKSAEKIK SDSDVLLVVG IGGSYLGARA AIEALNHAFY NTLPKAKRGN PQVIFIGNNI
SSSYMRDVMD LLEDVDFSIN VISKSGTTTE PAIAFRIFRK LLEEKYGKEE AKARIYATTD
KERGALKTLS NEEGFESFVI PDDVGGRYSV LTAVGLLPIA VSGVNIDDMM KGALDASKDF
ATSELEDNPA YQYAVVRNVL YNKGKTIEML INYEPALQYF AEWWKQLFGE SEGKDEKGIY
PSSANYSTDL HSLGQYVQEG RRDLFETVLN VEKPKHELTI EEADNDLDGL NYLAGKTVDF
VNKKAFQGTM LAHTDGNVPN LIVNIPELNA YTFGYLVYFF EKACAMSGYL LGVNPFDQPG
VEAYKVNMFA LLGKPGFEEK KAELEKRLED
