ID G6PI2_RHIME Reviewed; 200 AA. AC Q92UI1; DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 27-MAR-2024, entry version 110. DE RecName: Full=Putative glucose-6-phosphate isomerase 2; DE Short=GPI 2; DE EC=5.3.1.9; DE AltName: Full=Phosphoglucose isomerase 2; DE Short=PGI 2; DE AltName: Full=Phosphohexose isomerase 2; DE Short=PHI 2; GN Name=pgiA2; OrderedLocusNames=RB1150; ORFNames=SMb20857; OS Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium OS meliloti). OG Plasmid pSymB (megaplasmid 2). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales; OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium. OX NCBI_TaxID=266834; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=1021; RX PubMed=11481431; DOI=10.1073/pnas.161294698; RA Finan T.M., Weidner S., Wong K., Buhrmester J., Chain P., Vorhoelter F.J., RA Hernandez-Lucas I., Becker A., Cowie A., Gouzy J., Golding B., Puehler A.; RT "The complete sequence of the 1,683-kb pSymB megaplasmid from the N2-fixing RT endosymbiont Sinorhizobium meliloti."; RL Proc. Natl. Acad. Sci. U.S.A. 98:9889-9894(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=1021; RX PubMed=11474104; DOI=10.1126/science.1060966; RA Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F., RA Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G., RA Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P., RA Cowie A., Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S., RA Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I., RA Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S., RA Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C., RA Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R., RA Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H., RA Wong K., Yeh K.-C., Batut J.; RT "The composite genome of the legume symbiont Sinorhizobium meliloti."; RL Science 293:668-672(2001). 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; CC -!- COFACTOR: CC Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250}; CC Note=Binds 1 Fe cation per subunit. {ECO:0000250}; CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3- CC phosphate and glycerone phosphate from D-glucose: step 2/4. CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- MISCELLANEOUS: R.meliloti has a classic glucose-6-phosphate isomerase CC (AC Q92SC4) and two archaeal-type glucose-6-phosphate isomerases. CC -!- SIMILARITY: Belongs to the archaeal-type GPI family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AL591985; CAC49550.1; -; Genomic_DNA. DR PIR; F95985; F95985. DR RefSeq; NP_437690.1; NC_003078.1. DR AlphaFoldDB; Q92UI1; -. DR SMR; Q92UI1; -. DR EnsemblBacteria; CAC49550; CAC49550; SM_b20857. DR KEGG; sme:SM_b20857; -. DR PATRIC; fig|266834.11.peg.6079; -. DR eggNOG; COG2140; Bacteria. DR HOGENOM; CLU_105797_0_0_5; -. DR OrthoDB; 5592106at2; -. DR UniPathway; UPA00109; UER00181. DR Proteomes; UP000001976; Plasmid pSymB. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004347; F:glucose-6-phosphate isomerase activity; IEA:UniProtKB-UniRule. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniRule. DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule. DR CDD; cd02218; cupin_PGI; 1. DR Gene3D; 2.60.120.10; Jelly Rolls; 1. DR HAMAP; MF_01410; G6P_isomerase_arch; 1. DR InterPro; IPR016758; G6P_isomerase_archaea/bacteria. DR InterPro; IPR010551; G6P_isomerase_prok. DR InterPro; IPR014710; RmlC-like_jellyroll. DR InterPro; IPR011051; RmlC_Cupin_sf. DR Pfam; PF06560; GPI; 1. DR PIRSF; PIRSF019325; Glucose-6-phosphate_isomerase; 1. DR SUPFAM; SSF51182; RmlC-like cupins; 1. PE 3: Inferred from homology; KW Cytoplasm; Gluconeogenesis; Glycolysis; Iron; Isomerase; Metal-binding; KW Plasmid; Reference proteome. FT CHAIN 1..200 FT /note="Putative glucose-6-phosphate isomerase 2" FT /id="PRO_0000185362" FT BINDING 92 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /evidence="ECO:0000250" FT BINDING 94 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /evidence="ECO:0000250" FT BINDING 101 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /evidence="ECO:0000250" FT BINDING 140 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /evidence="ECO:0000250" SQ SEQUENCE 200 AA; 22063 MW; 7D397D5ADC890AD3 CRC64; MLILFEPGVC QVDVATGRLK GATNRYVKTF RDLAGLYRDE SAYQALIATR GDDVAYEVTD YKPSANGGDI IIGVTRMEPG KIGDEYFMTR GHIHARPNRP EMYYGEAGVG VMLLESPHGE IRTIEMRART MCYVPPFWIH RSVNVGLEPL VMTFSYPADA GQDYDVIAKA GGMRTVLSMT GTVDGPQSIT PVIQGDTHRL //