ID   G6PI3_RHOJR             Reviewed;         550 AA.
AC   Q0RV72;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Glucose-6-phosphate isomerase 3 {ECO:0000255|HAMAP-Rule:MF_00473};
DE            Short=GPI 3 {ECO:0000255|HAMAP-Rule:MF_00473};
DE            EC=5.3.1.9 {ECO:0000255|HAMAP-Rule:MF_00473};
DE   AltName: Full=Phosphoglucose isomerase 3 {ECO:0000255|HAMAP-Rule:MF_00473};
DE            Short=PGI 3 {ECO:0000255|HAMAP-Rule:MF_00473};
DE   AltName: Full=Phosphohexose isomerase 3 {ECO:0000255|HAMAP-Rule:MF_00473};
DE            Short=PHI 3 {ECO:0000255|HAMAP-Rule:MF_00473};
GN   Name=pgi3 {ECO:0000255|HAMAP-Rule:MF_00473};
GN   OrderedLocusNames=RHA1_ro11167;
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; ABH00814.1; -; Genomic_DNA.
DR   RefSeq; WP_011600441.1; NC_008271.1.
DR   AlphaFoldDB; Q0RV72; -.
DR   SMR; Q0RV72; -.
DR   STRING; 101510.RHA1_ro11167; -.
DR   EnsemblBacteria; ABH00814; ABH00814; RHA1_ro11167.
DR   KEGG; rha:RHA1_ro11167; -.
DR   PATRIC; fig|101510.16.peg.8987; -.
DR   eggNOG; COG0166; Bacteria.
DR   HOGENOM; CLU_017947_3_1_11; -.
DR   OMA; FFHAENH; -.
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..550
FT                   /note="Glucose-6-phosphate isomerase 3"
FT                   /id="PRO_0000252639"
FT   ACT_SITE        357
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT   ACT_SITE        388
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT   ACT_SITE        514
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
SQ   SEQUENCE   550 AA;  60172 MW;  0F54949B46249F83 CRC64;
     MTATTAQLLT ETTPWLRLSE HSEEIDRSHL RALFASDPDR VDEFTVTAGD LHIDYSKHLI
     TRRTRELLLD LARSVDVEGN RDAMLHGEHI NTTENRAVLH TALRLPRDAS LSVDGQDIVT
     DVHETLEKMG VFTERLRDGR WRGATGKKIT TVVNIGIGGS DLGPVMVYRA LRHYADAGIS
     LRFVSNLDPA DLTDNLRGLD PAATLFIVTS KTFSTLETLT NATAARRWLV SALGEDAVTK
     HFVAVSTNAQ PVAEFGIAPE NIFGFWDWVG GRYSVGSAIG LSVMAAIGRE RFTELLDGFH
     TIDEHFRTAP PESNAPLLLG MLGVWYSSFR GAQSRAVLPY SNDLVRFPAY LQQLTMESNG
     KSVHTDGSPV RCDTGEIFWG EPGTNGQHAF FQLLHQGTRL VPADFIGFAQ STDDLPTMSG
     TGSMHDLLMA NFFAQSKVLA FGKTRKEIAA ESASADLIPH KVMPGNRPST TILAPRLTPS
     TLGQLIALYE HQVFVQGVVW GIDSFDQWGV ELGKVQALAL APAVAGEAAP CTGDTSTDAL
     IRTYRRLRHP