ID G6PI_ANADE Reviewed; 550 AA. AC Q2IE39; DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot. DT 07-MAR-2006, sequence version 1. DT 16-JUN-2009, entry version 23. 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=Adeh_3080; OS Anaeromyxobacter dehalogenans (strain 2CP-C). OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales; OC Cystobacterineae; Myxococcaceae; Anaeromyxobacter. OX NCBI_TaxID=290397; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C., RA Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M., RA Kyrpides N., Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S., RA Kirby J.R., Zhulin I.B., Loeffler F.E., Richardson P.; RT "Complete sequence of Anaeromyxobacter dehalogenans 2CP-C."; RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: D-glucose 6-phosphate = D-fructose 6- CC phosphate. 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; CP000251; ABC82849.1; -; Genomic_DNA. DR RefSeq; YP_466286.1; -. DR GeneID; 3889158; -. DR GenomeReviews; CP000251_GR; Adeh_3080. DR KEGG; ade:Adeh_3080; -. DR HOGENOM; Q2IE39; -. DR OMA; Q2IE39; PYSNDLA. DR BioCyc; ADEH290397:ADEH_3080-MON; -. 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; 1. DR PROSITE; PS00174; P_GLUCOSE_ISOMERASE_2; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Gluconeogenesis; Glycolysis; Isomerase. FT CHAIN 1 550 Glucose-6-phosphate isomerase. FT /FTId=PRO_0000252607. FT ACT_SITE 357 357 Proton donor (By similarity). FT ACT_SITE 389 389 By similarity. FT ACT_SITE 509 509 By similarity. SQ SEQUENCE 550 AA; 59816 MW; 03D0A07868C37B35 CRC64; MADRNDPLLR TPAWRALETH LAEVRPLHLR ELFARDPGRG DRLAAEGAGL YLDYSKQRVT EETVRLLVAL AEARGLPGRR AAMFRGEKVN ATEGRAALHV ALRAPRGERI EVDGKDVVPE VHAVLDRMAA FAEQVRSGAW TGFTGRRIRT VVNVGIGGSD LGPAMAYRAL RAYTTREIAF RFVSNVDGTD LAEAVRDLDP AETLFLVASK TFTTLETMTN AASARAWLLA ALGDERAVAR HFVAISTNEA EVRRFGIDPA NMFGFWDWVG GRYSMDSAIG LSTMIAVGPG GFRELLAGFR AMDEHFRDAP LERNLPALVG LIGVWNASLL GAETVAVLPY DQYLDRFPAY LQQLTMESNG KRVTASGAPV EGHGTGAIYW GEPGTNGQHS FYQLLHQGTH LVACDFIGFC RTLNPLGRHH DLLMANLFAQ GEALAFGKTA EEARAEGTPE ALVPHRTFPG NRPSSTILAD RLGPGTLGAL VALYEHAVFT QGVIWDVDSF DQWGVELGKV LANRIVKELE APADPALAHD GSTNALIRRY RARRGGSASS //