G6PI2_RHIME
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 03-AUG-2022, entry version 104.
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; Proteobacteria; 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}.
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DR EMBL; AL591985; CAC49550.1; -; Genomic_DNA.
DR PIR; F95985; F95985.
DR RefSeq; NP_437690.1; NC_003078.1.
DR RefSeq; WP_010975982.1; NC_003078.1.
DR AlphaFoldDB; Q92UI1; -.
DR SMR; Q92UI1; -.
DR STRING; 266834.SM_b20857; -.
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 OMA; TRGHIHA; -.
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 Gene3D; 2.60.120.10; -; 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; SSF51182; 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