G6PI_BRUME
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 03-AUG-2022, entry version 107.
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=BMEI1636;
OS Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094).
OC Bacteria; Proteobacteria; 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 STRING; 224914.BMEI1636; -.
DR EnsemblBacteria; AAL52817; AAL52817; BMEI1636.
DR GeneID; 29594490; -.
DR KEGG; bme:BMEI1636; -.
DR PATRIC; fig|224914.52.peg.1954; -.
DR eggNOG; COG0166; Bacteria.
DR OMA; IGVWYIN; -.
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; 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 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
