G6PI_BRUA2
ID G6PI_BRUA2 Reviewed; 549 AA.
AC Q2YPF3;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 85.
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=BAB1_0316;
OS Brucella abortus (strain 2308).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=359391;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2308;
RX PubMed=16299333; DOI=10.1128/iai.73.12.8353-8361.2005;
RA Chain P.S., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.A.,
RA Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.;
RT "Whole-genome analyses of speciation events in pathogenic Brucellae.";
RL Infect. Immun. 73:8353-8361(2005).
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; AM040264; CAJ10272.1; -; Genomic_DNA.
DR RefSeq; WP_002963449.1; NZ_KN046823.1.
DR AlphaFoldDB; Q2YPF3; -.
DR SMR; Q2YPF3; -.
DR STRING; 359391.BAB1_0316; -.
DR EnsemblBacteria; CAJ10272; CAJ10272; BAB1_0316.
DR GeneID; 3787092; -.
DR KEGG; bmf:BAB1_0316; -.
DR PATRIC; fig|359391.11.peg.2362; -.
DR HOGENOM; CLU_017947_3_1_5; -.
DR OMA; IGVWYIN; -.
DR PhylomeDB; Q2YPF3; -.
DR UniPathway; UPA00109; UER00181.
DR UniPathway; UPA00138; -.
DR PRO; PR:Q2YPF3; -.
DR Proteomes; UP000002719; 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 3: Inferred from homology;
KW Cytoplasm; Gluconeogenesis; Glycolysis; Isomerase; Reference proteome.
FT CHAIN 1..549
FT /note="Glucose-6-phosphate isomerase"
FT /id="PRO_0000230912"
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"
SQ SEQUENCE 549 AA; 59642 MW; A2FEDCCE86183B68 CRC64;
MARDATKLEA TVAKLKKHWA ESAPRDMRAA FSTDPGRFGR 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 LIHDMLDPYA
LGRLIALYEH RVFVEAQIFG INAFDQWGVE LGKELATELL PVVSGKEGAS GRDASTQGLV
AHLHARRKA
