ID   G6PI2_RHOSR             Reviewed;         551 AA.
AC   Q0RVH6;
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 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=pgi2; OrderedLocusNames=RHA1_ro11063;
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; ABH00710.1; -; Genomic_DNA.
DR   RefSeq; YP_708868.1; -.
DR   GeneID; 4226496; -.
DR   GenomeReviews; CP000434_GR; RHA1_ro11063.
DR   KEGG; rha:RHA1_ro11063; -.
DR   HOGENOM; Q0RVH6; -.
DR   OMA; Q0RVH6; ESICEER.
DR   BioCyc; RSP101510:RHA1_RO11063-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    551       Glucose-6-phosphate isomerase 2.
FT                                /FTId=PRO_0000252638.
FT   ACT_SITE    352    352       Proton donor (By similarity).
FT   ACT_SITE    383    383       By similarity.
FT   ACT_SITE    509    509       By similarity.
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
//