ID   G6PI_BRUME              Reviewed;         549 AA.
AC   Q8YF86;
DT   27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   27-MAR-2002, sequence version 1.
DT   27-MAR-2024, entry version 113.
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};
GN   OrderedLocusNames=BMEI1636;
OS   Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=224914;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=16M / ATCC 23456 / NCTC 10094;
RX   PubMed=11756688; DOI=10.1073/pnas.221575398;
RA   DelVecchio V.G., Kapatral V., Redkar R.J., Patra G., Mujer C., Los T.,
RA   Ivanova N., Anderson I., Bhattacharyya A., Lykidis A., Reznik G.,
RA   Jablonski L., Larsen N., D'Souza M., Bernal A., Mazur M., Goltsman E.,
RA   Selkov E., Elzer P.H., Hagius S., O'Callaghan D., Letesson J.-J.,
RA   Haselkorn R., Kyrpides N.C., Overbeek R.;
RT   "The genome sequence of the facultative intracellular pathogen Brucella
RT   melitensis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:443-448(2002).
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; AE008917; AAL52817.1; -; Genomic_DNA.
DR   PIR; AF3456; AF3456.
DR   RefSeq; WP_004682840.1; NZ_GG703778.1.
DR   PDB; 4EM6; X-ray; 1.90 A; A/B/C/D=1-549.
DR   PDBsum; 4EM6; -.
DR   AlphaFoldDB; Q8YF86; -.
DR   SMR; Q8YF86; -.
DR   GeneID; 29594490; -.
DR   KEGG; bme:BMEI1636; -.
DR   KEGG; bmel:DK63_1855; -.
DR   PATRIC; fig|224914.52.peg.1954; -.
DR   eggNOG; COG0166; Bacteria.
DR   PhylomeDB; Q8YF86; -.
DR   UniPathway; UPA00109; UER00181.
DR   UniPathway; UPA00138; -.
DR   PRO; PR:Q8YF86; -.
DR   Proteomes; UP000000419; Chromosome I.
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; 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   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Gluconeogenesis; Glycolysis; Isomerase.
FT   CHAIN           1..549
FT                   /note="Glucose-6-phosphate isomerase"
FT                   /id="PRO_0000180609"
FT   ACT_SITE        353
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT   ACT_SITE        384
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT   ACT_SITE        513
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT   HELIX           5..21
FT                   /evidence="ECO:0007829|PDB:4EM6"
FT   HELIX           27..33
FT                   /evidence="ECO:0007829|PDB:4EM6"
FT   HELIX           37..40
FT                   /evidence="ECO:0007829|PDB:4EM6"
FT   STRAND          42..45
FT                   /evidence="ECO:0007829|PDB:4EM6"
FT   STRAND          48..51
FT                   /evidence="ECO:0007829|PDB:4EM6"
FT   HELIX           59..71
FT                   /evidence="ECO:0007829|PDB:4EM6"
FT   HELIX           74..82
FT                   /evidence="ECO:0007829|PDB:4EM6"
FT   TURN            89..92
FT                   /evidence="ECO:0007829|PDB:4EM6"
FT   HELIX           97..101
FT                   /evidence="ECO:0007829|PDB:4EM6"
FT   HELIX           116..135
FT                   /evidence="ECO:0007829|PDB:4EM6"
FT   STRAND          136..139
FT                   /evidence="ECO:0007829|PDB:4EM6"
FT   STRAND          148..152
FT                   /evidence="ECO:0007829|PDB:4EM6"
FT   HELIX           155..157
FT                   /evidence="ECO:0007829|PDB:4EM6"
FT   HELIX           159..167
FT                   /evidence="ECO:0007829|PDB:4EM6"
FT   HELIX           169..171
FT                   /evidence="ECO:0007829|PDB:4EM6"
FT   STRAND          174..180
FT                   /evidence="ECO:0007829|PDB:4EM6"
FT   HELIX           185..192
FT                   /evidence="ECO:0007829|PDB:4EM6"
FT   HELIX           197..199
FT                   /evidence="ECO:0007829|PDB:4EM6"
FT   STRAND          200..205
FT                   /evidence="ECO:0007829|PDB:4EM6"
FT   STRAND          207..209
FT                   /evidence="ECO:0007829|PDB:4EM6"
FT   HELIX           212..229
FT                   /evidence="ECO:0007829|PDB:4EM6"
FT   HELIX           231..236
FT                   /evidence="ECO:0007829|PDB:4EM6"
FT   STRAND          238..241
FT                   /evidence="ECO:0007829|PDB:4EM6"
FT   HELIX           245..251
FT                   /evidence="ECO:0007829|PDB:4EM6"
FT   HELIX           255..257
FT                   /evidence="ECO:0007829|PDB:4EM6"
FT   HELIX           267..269
FT                   /evidence="ECO:0007829|PDB:4EM6"
FT   HELIX           274..276
FT                   /evidence="ECO:0007829|PDB:4EM6"
FT   HELIX           277..283
FT                   /evidence="ECO:0007829|PDB:4EM6"
FT   HELIX           285..304
FT                   /evidence="ECO:0007829|PDB:4EM6"
FT   HELIX           307..309
FT                   /evidence="ECO:0007829|PDB:4EM6"
FT   HELIX           311..324
FT                   /evidence="ECO:0007829|PDB:4EM6"
FT   STRAND          330..336
FT                   /evidence="ECO:0007829|PDB:4EM6"
FT   HELIX           338..340
FT                   /evidence="ECO:0007829|PDB:4EM6"
FT   HELIX           343..355
FT                   /evidence="ECO:0007829|PDB:4EM6"
FT   STRAND          373..375
FT                   /evidence="ECO:0007829|PDB:4EM6"
FT   HELIX           381..384
FT                   /evidence="ECO:0007829|PDB:4EM6"
FT   HELIX           387..392
FT                   /evidence="ECO:0007829|PDB:4EM6"
FT   STRAND          393..395
FT                   /evidence="ECO:0007829|PDB:4EM6"
FT   STRAND          399..406
FT                   /evidence="ECO:0007829|PDB:4EM6"
FT   HELIX           410..412
FT                   /evidence="ECO:0007829|PDB:4EM6"
FT   HELIX           413..432
FT                   /evidence="ECO:0007829|PDB:4EM6"
FT   HELIX           436..445
FT                   /evidence="ECO:0007829|PDB:4EM6"
FT   HELIX           450..456
FT                   /evidence="ECO:0007829|PDB:4EM6"
FT   HELIX           457..460
FT                   /evidence="ECO:0007829|PDB:4EM6"
FT   STRAND          468..474
FT                   /evidence="ECO:0007829|PDB:4EM6"
FT   HELIX           478..499
FT                   /evidence="ECO:0007829|PDB:4EM6"
FT   HELIX           507..509
FT                   /evidence="ECO:0007829|PDB:4EM6"
FT   HELIX           510..523
FT                   /evidence="ECO:0007829|PDB:4EM6"
FT   HELIX           534..547
FT                   /evidence="ECO:0007829|PDB:4EM6"
SQ   SEQUENCE   549 AA;  59642 MW;  B2EFDDCE8392C968 CRC64;
     MARDATKLEA TVAKLKKHWA ESAPRDMRAA FSADPGRFGR YSLCLDDLLF DWSKCRVNDE
     TMALLKELAV AADVEGRRAA MFAGEHINNT EDRAVLHVAL RDTSSKEVLV DGHNVLPDVK
     HVLDRMAAFA DGIRSGALKG ATGRKITDIV NIGIGGSDLG PVMATLALAP YHDEPRAHFV
     SNIDGAHIAD TLSPLDPAST LIIVASKTFT TIETMTNAQT ARKWVADTLG EAAVGAHFAA
     VSTALDKVAA FGIPEDRVFG FWDWVGGRYS VWSAIGLPVM IAVGPDNFRK FLAGAHAMDV
     HFRDAPLEKN LPVMLGLIGY WHRAICGYGS RAIIPYDQRL SRLPAYLQQL DMESNGKSVT
     LDGKPVSGPT GPVVWGEPGT NGQHAFFQLL HQGTDTIPLE FIVAAKGHEP TLDHQHEMLM
     ANCLAQSEAL MKGRTLDEAR AQLQAKNLPA SQVERIAPHR VFSGNRPSLT LIHDMLDPYT
     LGRLIALYEH RVFVEAQIFG INAFDQWGVE LGKELATELL PVVSGKEGAS GRDASTQGLV
     AHLHARRKA
//