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   27-MAR-2024, entry version 152.
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; Bacillota; 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; 224308-BSU31350; -.
DR   EnsemblBacteria; CAB15124; CAB15124; BSU_31350.
DR   GeneID; 83887006; -.
DR   GeneID; 937165; -.
DR   KEGG; bsu:BSU31350; -.
DR   PATRIC; fig|224308.179.peg.3399; -.
DR   eggNOG; COG0166; Bacteria.
DR   InParanoid; P80860; -.
DR   OrthoDB; 140919at2; -.
DR   PhylomeDB; P80860; -.
DR   BioCyc; BSUB:BSU31350-MONOMER; -.
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; GLUCOSE-6-PHOSPHATE ISOMERASE; 1.
DR   PANTHER; PTHR11469:SF1; GLUCOSE-6-PHOSPHATE ISOMERASE; 1.
DR   Pfam; PF00342; PGI; 2.
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   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
//