ID   G6PI3_RHOSR             Reviewed;         550 AA.
AC   Q0RV72;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   16-JUN-2009, entry version 19.
DE   RecName: Full=Glucose-6-phosphate isomerase 3;
DE            Short=GPI 3;
DE            EC=5.3.1.9;
DE   AltName: Full=Phosphoglucose isomerase 3;
DE            Short=PGI 3;
DE   AltName: Full=Phosphohexose isomerase 3;
DE            Short=PHI 3;
GN   Name=pgi3; OrderedLocusNames=RHA1_ro11167;
OS   Rhodococcus sp. (strain RHA1).
OG   Plasmid pRHL3.
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Corynebacterineae; Nocardiaceae; Rhodococcus.
OX   NCBI_TaxID=101510;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17030794; DOI=10.1073/pnas.0607048103;
RA   McLeod M.P., Warren R.L., Hsiao W.W.L., Araki N., Myhre M.,
RA   Fernandes C., Miyazawa D., Wong W., Lillquist A.L., Wang D.,
RA   Dosanjh M., Hara H., Petrescu A., Morin R.D., Yang G., Stott J.M.,
RA   Schein J.E., Shin H., Smailus D., Siddiqui A.S., Marra M.A.,
RA   Jones S.J.M., Holt R., Brinkman F.S.L., Miyauchi K., Fukuda M.,
RA   Davies J.E., Mohn W.W., 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   -!- 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.
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DR   EMBL; CP000434; ABH00814.1; -; Genomic_DNA.
DR   RefSeq; YP_708972.1; -.
DR   GeneID; 4226608; -.
DR   GenomeReviews; CP000434_GR; RHA1_ro11167.
DR   KEGG; rha:RHA1_ro11167; -.
DR   HOGENOM; Q0RV72; -.
DR   OMA; Q0RV72; HDASTEG.
DR   BioCyc; RSP101510:RHA1_RO11167-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;
KW   Plasmid.
FT   CHAIN         1    550       Glucose-6-phosphate isomerase 3.
FT                                /FTId=PRO_0000252639.
FT   ACT_SITE    357    357       Proton donor (By similarity).
FT   ACT_SITE    388    388       By similarity.
FT   ACT_SITE    514    514       By similarity.
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
//