ID   G6PI1_RHOSR             Reviewed;         550 AA.
AC   Q0S539;
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 1;
DE            Short=GPI 1;
DE            EC=5.3.1.9;
DE   AltName: Full=Phosphoglucose isomerase 1;
DE            Short=PGI 1;
DE   AltName: Full=Phosphohexose isomerase 1;
DE            Short=PHI 1;
GN   Name=pgi1; OrderedLocusNames=RHA1_ro05567;
OS   Rhodococcus sp. (strain RHA1).
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; CP000431; ABG97347.1; -; Genomic_DNA.
DR   RefSeq; YP_705505.1; -.
DR   GeneID; 4223118; -.
DR   GenomeReviews; CP000431_GR; RHA1_ro05567.
DR   KEGG; rha:RHA1_ro05567; -.
DR   HOGENOM; Q0S539; -.
DR   OMA; Q0S539; PYSNDLA.
DR   BioCyc; RSP101510:RHA1_RO05567-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.
FT   CHAIN         1    550       Glucose-6-phosphate isomerase 1.
FT                                /FTId=PRO_0000252637.
FT   ACT_SITE    355    355       Proton donor (By similarity).
FT   ACT_SITE    386    386       By similarity.
FT   ACT_SITE    512    512       By similarity.
SQ   SEQUENCE   550 AA;  60028 MW;  20C5F1651E86995C CRC64;
     MSSDITGTAA WQKLRDHHAQ IQSVHLRELF EKDPARGQEL TVTAGDLYID YSKHRIDRDT
     LGLLLELARS ADLEARRDAM FAGEHINTSE DRAVLHTALR LPADASLVVD GQDVVADVHE
     VLDRMGDFTD RVRSGEWRGA TGERIKTVVN IGIGGSDLGP VMVYRALRHY ADAGISVRFI
     SNVDPADLVR SLQGLDPATT LFIVASKTFS TLETLTNATA ARRWLLGGLG LGNEAVAKHF
     VAVSTHADRV AEFGIDTANM FGFWDWVGGR YSVDSAIGLS VMAAIGKERF AEFLAGFHAV
     DEHFRTAPLE ENAPVLLGLI GLWYSNFFGA ESRAVLPYSN DLVRFAAYLQ QLTMESNGKS
     VRADGTPVPT STGEIFWGEP GTNGQHAFYQ LLHQGTRLVP SDFIGFGEPT DDLPTADGTG
     SMHDLLMSNF FAQTKVLAFG KTAEEIAAEG TPEHLVPHKV MPGNRPSTTI LAPKLTPSVI
     GQLIALYEHQ VFVEGVVWGI DSFDQWGVEL GKTQAVELQP VLTAAEEPAA QSDSSTDSLV
     RWYRRQRGRA
//