G6PI2_RHOJR
ID G6PI2_RHOJR Reviewed; 551 AA.
AC Q0RVH6;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Glucose-6-phosphate isomerase 2 {ECO:0000255|HAMAP-Rule:MF_00473};
DE Short=GPI 2 {ECO:0000255|HAMAP-Rule:MF_00473};
DE EC=5.3.1.9 {ECO:0000255|HAMAP-Rule:MF_00473};
DE AltName: Full=Phosphoglucose isomerase 2 {ECO:0000255|HAMAP-Rule:MF_00473};
DE Short=PGI 2 {ECO:0000255|HAMAP-Rule:MF_00473};
DE AltName: Full=Phosphohexose isomerase 2 {ECO:0000255|HAMAP-Rule:MF_00473};
DE Short=PHI 2 {ECO:0000255|HAMAP-Rule:MF_00473};
GN Name=pgi2 {ECO:0000255|HAMAP-Rule:MF_00473};
GN OrderedLocusNames=RHA1_ro11063;
OS Rhodococcus jostii (strain RHA1).
OG Plasmid pRHL3.
OC Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus.
OX NCBI_TaxID=101510;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RHA1;
RX PubMed=17030794; DOI=10.1073/pnas.0607048103;
RA McLeod M.P., Warren R.L., Hsiao W.W.L., Araki N., Myhre M., Fernandes C.,
RA Miyazawa D., Wong W., Lillquist A.L., Wang D., Dosanjh M., Hara H.,
RA Petrescu A., Morin R.D., Yang G., Stott J.M., Schein J.E., Shin H.,
RA Smailus D., Siddiqui A.S., Marra M.A., Jones S.J.M., Holt R.,
RA Brinkman F.S.L., Miyauchi K., Fukuda M., Davies J.E., Mohn W.W.,
RA Eltis L.D.;
RT "The complete genome of Rhodococcus sp. RHA1 provides insights into a
RT catabolic powerhouse.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15582-15587(2006).
CC -!- FUNCTION: Catalyzes the reversible isomerization of glucose-6-phosphate
CC to fructose-6-phosphate. {ECO:0000255|HAMAP-Rule:MF_00473}.
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; Evidence={ECO:0000255|HAMAP-Rule:MF_00473};
CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC {ECO:0000255|HAMAP-Rule:MF_00473}.
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 2/4.
CC {ECO:0000255|HAMAP-Rule:MF_00473}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00473}.
CC -!- SIMILARITY: Belongs to the GPI family. {ECO:0000255|HAMAP-
CC Rule:MF_00473}.
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DR EMBL; CP000434; ABH00710.1; -; Genomic_DNA.
DR RefSeq; WP_011600338.1; NC_008271.1.
DR AlphaFoldDB; Q0RVH6; -.
DR SMR; Q0RVH6; -.
DR STRING; 101510.RHA1_ro11063; -.
DR EnsemblBacteria; ABH00710; ABH00710; RHA1_ro11063.
DR KEGG; rha:RHA1_ro11063; -.
DR PATRIC; fig|101510.16.peg.8894; -.
DR eggNOG; COG0166; Bacteria.
DR HOGENOM; CLU_017947_3_1_11; -.
DR OMA; CPAYAYG; -.
DR UniPathway; UPA00109; UER00181.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000008710; Plasmid pRHL3.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR GO; GO:0004347; F:glucose-6-phosphate isomerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniRule.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule.
DR CDD; cd05015; SIS_PGI_1; 1.
DR CDD; cd05016; SIS_PGI_2; 1.
DR Gene3D; 1.10.1390.10; -; 1.
DR HAMAP; MF_00473; G6P_isomerase; 1.
DR InterPro; IPR001672; G6P_Isomerase.
DR InterPro; IPR023096; G6P_Isomerase_C.
DR InterPro; IPR018189; Phosphoglucose_isomerase_CS.
DR InterPro; IPR046348; SIS_dom_sf.
DR InterPro; IPR035476; SIS_PGI_1.
DR InterPro; IPR035482; SIS_PGI_2.
DR PANTHER; PTHR11469; PTHR11469; 1.
DR Pfam; PF00342; PGI; 1.
DR PRINTS; PR00662; G6PISOMERASE.
DR SUPFAM; SSF53697; SSF53697; 1.
DR PROSITE; PS00765; P_GLUCOSE_ISOMERASE_1; 1.
DR PROSITE; PS00174; P_GLUCOSE_ISOMERASE_2; 1.
DR PROSITE; PS51463; P_GLUCOSE_ISOMERASE_3; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Gluconeogenesis; Glycolysis; Isomerase; Plasmid;
KW Reference proteome.
FT CHAIN 1..551
FT /note="Glucose-6-phosphate isomerase 2"
FT /id="PRO_0000252638"
FT ACT_SITE 352
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT ACT_SITE 383
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT ACT_SITE 509
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
SQ SEQUENCE 551 AA; 60350 MW; ADE6DD98F743050C CRC64;
MTHIVTDTPL WKKLSDHHWE VVGTHLRELF DTDPDRGVDL IVTAADLYID YSKHRVTRET
MGLLVDLARA AGVERHREAM FTGAHINTSE DRAVLHTALR ANPERELIVD GQDVVGDVHT
VLRRMGEFTD RVRSGAWRGA TGERIRTVVN IGIGGSDLGP AMAYRALRHY VDGPEVRFVS
NIDPADLLSN LTDLDPRTTL FVVVSKTFST LETMTNASAA RRWITEALGE HAVPRHFVAV
STDEERVTAF GITARNIFGF WEWVGGRYSV GSAAGLSVMI AIGRERFTEF LGGMRAIDEH
FRTTPLESNA PVILGMLGVW YSSFFGADAR AVLPYAHDLA RFPAYLQQLT MESNGKSVRT
DGTPVGTFTG EIFWGEPGTN GQHAFHQLLH QGTHLIPVDF LGFAEPIEDL PTLDGIGSVH
DVLTANLFAQ SKVLAFGKNA DEVAADGTPS ALVPHKVMSG NRPSTTILGA KLTPSTLGQL
IALYEHQVFV QGIVWGIDSF DQWGVELGKT SALELGPALW DLDGAAYVGD SSTTGLIRTY
RLARGERRCL P