G6PI_DESHD
ID G6PI_DESHD Reviewed; 533 AA.
AC B8G1G1;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 68.
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=Dhaf_3194;
OS Desulfitobacterium hafniense (strain DSM 10664 / DCB-2).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Desulfitobacterium.
OX NCBI_TaxID=272564;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10664 / DCB-2;
RX PubMed=22316246; DOI=10.1186/1471-2180-12-21;
RA Kim S.H., Harzman C., Davis J.K., Hutcheson R., Broderick J.B., Marsh T.L.,
RA Tiedje J.M.;
RT "Genome sequence of Desulfitobacterium hafniense DCB-2, a Gram-positive
RT anaerobe capable of dehalogenation and metal reduction.";
RL BMC Microbiol. 12:21-21(2012).
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; CP001336; ACL21214.1; -; Genomic_DNA.
DR RefSeq; WP_015944462.1; NC_011830.1.
DR AlphaFoldDB; B8G1G1; -.
DR SMR; B8G1G1; -.
DR EnsemblBacteria; ACL21214; ACL21214; Dhaf_3194.
DR KEGG; dhd:Dhaf_3194; -.
DR HOGENOM; CLU_033288_0_0_9; -.
DR OMA; CPAYAYG; -.
DR UniPathway; UPA00109; UER00181.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000007726; 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; 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_1000135526"
FT ACT_SITE 322
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT ACT_SITE 351
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT ACT_SITE 455
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
SQ SEQUENCE 533 AA; 59326 MW; 89E9C3CED4D4E83F CRC64;
MVIITSWKRF KEYLYYDQEL ELLLDISRMN FSAEFLTELA EPMRDAYHQL QLLEKGALAN
PDEGRMVGHY WLRNPDLAPT EEIAQDIKET LKEILDFAEQ IHSGRLQGEK GNPFRNILLV
GVGGSILGPR FVADALASSR DKMKAFFIDN GDPDGIDRVL SRIGEELPAT LCLIISKSGG
TIETRNGMLE VRRAYEEAGL SFPDHAVAIT QRGSQLDKLS QKEGWLRAFP MWDWVGGRTS
LLSAVGLLSL ALQGIDVAGL LQGAKDCDGR TRRPDTLANP GALLALMWYY STQGQGGKQM
VVLPYKDRLE LFTKYLQQLI MESLGKEKNL QGETVHQGIT VYGNKGSSDQ HSYLQQLLEG
PDNFFVTFIE VLKDRQGSSA YMEENSTSGE YLQAFLLGTR EALTQKGRES LTITVKEVNA
YTIGVLIALF ERAVSIYALL VGINAYHQPA VEMGKKAAGQ AIQLKNNIVE CLKKHPDKRF
SVHEIALAIG EEAHQEMVFK LLLHLTTNPE HGVNMAAGHP LPESRFFVSG PIL
