G6PI_CLOBL
ID G6PI_CLOBL Reviewed; 450 AA.
AC A7GIL4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 78.
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=CLI_3449;
OS Clostridium botulinum (strain Langeland / NCTC 10281 / Type F).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=441772;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Langeland / NCTC 10281 / Type F;
RA Brinkac L.M., Daugherty S., Dodson R.J., Madupu R., Brown J.L., Bruce D.,
RA Detter C., Munk C., Smith L.A., Smith T.J., White O., Brettin T.S.;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000728; ABS41702.1; -; Genomic_DNA.
DR RefSeq; WP_012101005.1; NC_009699.1.
DR AlphaFoldDB; A7GIL4; -.
DR SMR; A7GIL4; -.
DR EnsemblBacteria; ABS41702; ABS41702; CLI_3449.
DR KEGG; cbf:CLI_3449; -.
DR HOGENOM; CLU_037303_0_1_9; -.
DR OMA; CPAYAYG; -.
DR UniPathway; UPA00109; UER00181.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000002410; Chromosome.
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 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; 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; PS51463; P_GLUCOSE_ISOMERASE_3; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Gluconeogenesis; Glycolysis; Isomerase.
FT CHAIN 1..450
FT /note="Glucose-6-phosphate isomerase"
FT /id="PRO_1000013955"
FT ACT_SITE 291
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT ACT_SITE 312
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT ACT_SITE 426
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
SQ SEQUENCE 450 AA; 50637 MW; 78F54CEEFCEC2362 CRC64;
MENSLSLDLT KTKPYVEEHE IQYLESIIRE MDNTLGKKTG PGNKFLGWMD LPINYNKEEF
ARIKKAAEKI KNTCDVFIVI GIGGSYLGSR AAIEMISNTF YNNLEKNQRR VPQIYFAGNN
ISSTYMADLL ELVKDKDICV NVISKSGTTT EPAIAFRIFK ELLEKKYGKE GAKERIFATT
DVAKGALRTL ADLEGYETFV IPDDVGGRFS VLTPVGLLPI AVSGIDVDEM MKGAADARQE
YSSDNIEKNH VYRYVAVRNA LYRKGKTTEM LVNFEPCLHY FGEWWKQLYG ESEGKDGKGI
FPAAADFSTD LHSMGQYIQE GLRNIFETFI NVENPRKSII IKEDKENLDG LNFLAEKDMD
YVNHQALRGT VLAHNDGGVP AIVLNVPELS AYYFGQLVYF FEKACGISGY LQGVNPFDQP
GVEAYKKNMF ALLGKPGYED MKATLEERLK