G6PI_ACAM1
ID G6PI_ACAM1 Reviewed; 529 AA.
AC B0CCT9;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 75.
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=AM1_4272;
OS Acaryochloris marina (strain MBIC 11017).
OC Bacteria; Cyanobacteria; Synechococcales; Acaryochloridaceae;
OC Acaryochloris.
OX NCBI_TaxID=329726;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MBIC 11017;
RX PubMed=18252824; DOI=10.1073/pnas.0709772105;
RA Swingley W.D., Chen M., Cheung P.C., Conrad A.L., Dejesa L.C., Hao J.,
RA Honchak B.M., Karbach L.E., Kurdoglu A., Lahiri S., Mastrian S.D.,
RA Miyashita H., Page L., Ramakrishna P., Satoh S., Sattley W.M., Shimada Y.,
RA Taylor H.L., Tomo T., Tsuchiya T., Wang Z.T., Raymond J., Mimuro M.,
RA Blankenship R.E., Touchman J.W.;
RT "Niche adaptation and genome expansion in the chlorophyll d-producing
RT cyanobacterium Acaryochloris marina.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:2005-2010(2008).
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; CP000828; ABW29251.1; -; Genomic_DNA.
DR RefSeq; WP_012164582.1; NC_009925.1.
DR AlphaFoldDB; B0CCT9; -.
DR SMR; B0CCT9; -.
DR STRING; 329726.AM1_4272; -.
DR EnsemblBacteria; ABW29251; ABW29251; AM1_4272.
DR KEGG; amr:AM1_4272; -.
DR eggNOG; COG0166; Bacteria.
DR HOGENOM; CLU_033288_0_0_3; -.
DR OMA; CPAYAYG; -.
DR OrthoDB; 417261at2; -.
DR UniPathway; UPA00109; UER00181.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000000268; 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; 2.
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; Reference proteome.
FT CHAIN 1..529
FT /note="Glucose-6-phosphate isomerase"
FT /id="PRO_1000081228"
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 529 AA; 58213 MW; 148311009FE8D76C CRC64;
MDAAALWQRY QDWLYYHEQL GIYVDISRMS FDDAFVERLE PKFVKAFKEM DALEAGAIAN
PDENRMVGHY WLRDSNLAPT PELKKEIITT LEKIEAFAAD VHAGRIKPAT APRFTDVISI
GIGGSSLGPQ FVSQALAVLH PALELHFIDN TDPAGIDYIL DRVQDRLDTT LVVTISKSGG
TPETRNGMLE AKNRFKNLGL DFPKHAVAVT GYGSKLAQIA EEEGWLAMLP MHDWVGGRTS
ELSAVGLVPA SLQGIAIREM LAGAKAMDEA TRVHDLKTNP AALLALSWYF AGEGAGKKDM
VILPYKDSLM LFSRYLQQLV MESLGKEKDL DDKIVHQGIA VYGNKGSTDQ HAYVQELREG
IPNFFLTFIE VLKDRDGTRF EVEPGVTSGD YLSGFLLGTR EALYEKRRDS ITVTLPEVTS
KQVGALIALY ERAVGLYASL INVNAYHQPG VEAGKKAATD TIALQNKIVQ ILRNTLTPLP
ITSLADKAEA PDKIETVYKI VRHLAANKRG VELYGNPAEP GSLQVTLKG