G6PI_CERSK
ID G6PI_CERSK Reviewed; 533 AA.
AC B9KRX7;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 63.
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=RSKD131_1059;
OS Cereibacter sphaeroides (strain KD131 / KCTC 12085) (Rhodobacter
OS sphaeroides).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Cereibacter.
OX NCBI_TaxID=557760;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KD131 / KCTC 12085;
RX PubMed=19028901; DOI=10.1128/jb.01565-08;
RA Lim S.-K., Kim S.J., Cha S.H., Oh Y.-K., Rhee H.-J., Kim M.-S., Lee J.K.;
RT "Complete genome sequence of Rhodobacter sphaeroides KD131.";
RL J. Bacteriol. 191:1118-1119(2009).
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; CP001150; ACM00919.1; -; Genomic_DNA.
DR RefSeq; WP_015920489.1; NC_011963.1.
DR AlphaFoldDB; B9KRX7; -.
DR SMR; B9KRX7; -.
DR EnsemblBacteria; ACM00919; ACM00919; RSKD131_1059.
DR GeneID; 67446489; -.
DR KEGG; rsk:RSKD131_1059; -.
DR HOGENOM; CLU_017947_3_1_5; -.
DR OMA; IGVWYIN; -.
DR UniPathway; UPA00109; UER00181.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000001597; Chromosome 1.
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.
FT CHAIN 1..533
FT /note="Glucose-6-phosphate isomerase"
FT /id="PRO_1000135537"
FT ACT_SITE 341
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT ACT_SITE 372
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT ACT_SITE 501
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
SQ SEQUENCE 533 AA; 58310 MW; FD6220A770E35435 CRC64;
MKQIWQALKA HQQAVEHRAI LDLFADPRRA ETFSTRLGDM LFDWSKTNID HTARDLLIDL
AGAAGVAEKR EAMFSGAKIN ETEGRAVLHT ALRNMDRPVR VDGVDVTPAL RETHARMQAF
VRDLRSGRFK GQGGPITDVV NIGIGGSDLG PAMACLALAP YADGPRCQFV SNVDGAHIHD
TLKDLDPATT LVIVASKTFT TIETMTNAET AKRWMATRVS DPAAQFAAVS TAADRTAAFG
IDASRVFGFE DWVGGRYSMW GPIGLALMIA IGPEEFDAFL AGGAEMDRHF REAPFAENLP
VLLALVGLWH NQICGHATRA VLPYDQRLAR LPAYLQQLEM ESNGKRVAMD GHELTHHSGP
IVWGEPGTNG QHAFYQLIHQ GSRIVPCEFL VAREGHEPDL AHQHLLLVSN CLAQSEALLR
GRSVEEARAI LARKGLTGSE LERQARHRVF PGNRPSTVLA YEKLTPATLG RIVALYEHRV
FVEGVILGIN SYDQWGVELG KELALALQPM LEGRAGTEGK DGSTAQLVSY LRC