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 16-JUN-2009, entry version 9. DE RecName: Full=Glucose-6-phosphate isomerase; DE Short=GPI; DE EC=5.3.1.9; DE AltName: Full=Phosphoglucose isomerase; DE Short=PGI; DE AltName: Full=Phosphohexose isomerase; DE Short=PHI; GN Name=pgi; OrderedLocusNames=AM1_4272; OS Acaryochloris marina (strain MBIC 11017). OC Bacteria; Cyanobacteria; Acaryochloris. OX NCBI_TaxID=329726; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 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., RA Shimada Y., Taylor H.L., Tomo T., Tsuchiya T., Wang Z.T., Raymond J., RA Mimuro M., 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 -!- CATALYTIC ACTIVITY: D-glucose 6-phosphate = D-fructose 6- CC phosphate. CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis. CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3- CC phosphate and glycerone phosphate from D-glucose: step 2/4. CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the GPI family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000828; ABW29251.1; -; Genomic_DNA. DR RefSeq; YP_001518568.1; -. DR GeneID; 5683075; -. DR GenomeReviews; CP000828_GR; AM1_4272. DR KEGG; amr:AM1_4272; -. DR OMA; B0CCT9; PYSNDLA. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004347; F:glucose-6-phosphate isomerase activity; IEA:HAMAP. DR GO; GO:0006094; P:gluconeogenesis; IEA:HAMAP. DR GO; GO:0006096; P:glycolysis; IEA:HAMAP. DR HAMAP; MF_00473; -; 1. DR InterPro; IPR001672; G6P_Isomerase. DR InterPro; IPR018189; Phosphoglucose_isomerase_CS. DR PANTHER; PTHR11469; G6P_Isomerase; 1. DR Pfam; PF00342; PGI; 1. DR PRINTS; PR00662; G6PISOMERASE. DR PROSITE; PS00765; P_GLUCOSE_ISOMERASE_1; FALSE_NEG. DR PROSITE; PS00174; P_GLUCOSE_ISOMERASE_2; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Gluconeogenesis; Glycolysis; Isomerase. FT CHAIN 1 529 Glucose-6-phosphate isomerase. FT /FTId=PRO_1000081228. FT ACT_SITE 322 322 Proton donor (By similarity). FT ACT_SITE 351 351 By similarity. FT ACT_SITE 455 455 By similarity. 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 //