ID G6PI_ALCBS Reviewed; 548 AA. AC Q0VR14; DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot. DT 05-SEP-2006, sequence version 1. DT 16-JUN-2009, entry version 20. 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=ABO_0936; OS Alcanivorax borkumensis (strain SK2 / ATCC 700651 / DSM 11573). OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Alcanivoracaceae; Alcanivorax. OX NCBI_TaxID=393595; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16878126; DOI=10.1038/nbt1232; RA Schneiker S., Martins dos Santos V.A.P., Bartels D., Bekel T., RA Brecht M., Buhrmester J., Chernikova T.N., Denaro R., Ferrer M., RA Gertler C., Goesmann A., Golyshina O.V., Kaminski F., Khachane A.N., RA Lang S., Linke B., McHardy A.C., Meyer F., Nechitaylo T., Puehler A., RA Regenhardt D., Rupp O., Sabirova J.S., Selbitschka W., Yakimov M.M., RA Timmis K.N., Vorhoelter F.-J., Weidner S., Kaiser O., Golyshin P.N.; RT "Genome sequence of the ubiquitous hydrocarbon-degrading marine RT bacterium Alcanivorax borkumensis."; RL Nat. Biotechnol. 24:997-1004(2006). 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; AM286690; CAL16384.1; -; Genomic_DNA. DR RefSeq; YP_692656.1; -. DR GeneID; 4211325; -. DR GenomeReviews; AM286690_GR; ABO_0936. DR KEGG; abo:ABO_0936; -. DR NMPDR; fig|393595.12.peg.937; -. DR HOGENOM; Q0VR14; -. DR OMA; Q0VR14; HDASTEG. DR BioCyc; ABOR393595:ABO_0936-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 1 548 Glucose-6-phosphate isomerase. FT /FTId=PRO_0000252606. FT ACT_SITE 356 356 Proton donor (By similarity). FT ACT_SITE 387 387 By similarity. FT ACT_SITE 511 511 By similarity. SQ SEQUENCE 548 AA; 60524 MW; C0BAD4A364DC5A10 CRC64; MVPEQNDLTE SSVWLQLENL AREEGSLHLS DFFVQELGRC AHFCLESDGL LVDLSKQRVS SHARDLLVSL ADERGLDRWS EALFAGAEVN CTENRSAKHW LLRDPSDQAA EIHGQLEIMD SIVSRVLEGQ WRGVLGDAIT DVVNVGVGGS ELGPLMAAFA LHSTPLAEGE VRPSLHFASS MDGSQISQVL QELNPRTTLV LVSSKSFTTV DTLHNANTAR SWMARALGLE MDNEAMLRCH FIGISAQPDK MTAWGIPSTN QLQFWDWVGG RYSLWSAIGL PIALTVGMHG FRELLAGAHD MDLHFRQRPW HENIPVMLAL VDVWNINFLD IRARAVLPYD GRLKYLPAYL EQLEMESNGK SVSRNGDPVD YHTCPVIWGE VGPNAQHAFF QLLHQGTQPV ACEFLMTARR YTESAHSGAA VELEGQHALS NANCLAQSRL LAFGEQALDS TLALPAYKRY RGNQPSTTLV LDELSPRTLG SLLAMYEHKV FAQAVIWGIN PFDQWGVEMG KVIATDMLAV LADPDGAHEV DDSSLSLARH IACKQATQ //