ID   G6PI_BORA1              Reviewed;         520 AA.
AC   Q2KYE9;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   16-JUN-2009, entry version 22.
DE   RecName: Full=Glucose-6-phosphate isomerase;
DE            Short=GPI;
DE            EC=5.3.1.9;
DE   AltName: Full=Phosphoglucose isomerase;
DE            Short=PGI;
DE   AltName: Full=Phosphohexose isomerase;
DE            Short=PHI;
GN   Name=pgi; OrderedLocusNames=BAV0519;
OS   Bordetella avium (strain 197N).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=360910;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16885469; DOI=10.1128/JB.01927-05;
RA   Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D.,
RA   King N.D., Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D.,
RA   Goble A., Lord A., Murphy L., Quail M.A., Rutter S., Squares R.,
RA   Squares S., Woodward J., Parkhill J., Temple L.M.;
RT   "Comparison of the genome sequence of the poultry pathogen Bordetella
RT   avium with those of B. bronchiseptica, B. pertussis, and B.
RT   parapertussis reveals extensive diversity in surface structures
RT   associated with host interaction.";
RL   J. Bacteriol. 188:6002-6015(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; AM167904; CAJ48124.1; -; Genomic_DNA.
DR   RefSeq; YP_785052.1; -.
DR   GeneID; 6267932; -.
DR   GenomeReviews; AM167904_GR; BAV0519.
DR   KEGG; bav:BAV0519; -.
DR   NMPDR; fig|521.1.peg.2329; -.
DR   HOGENOM; Q2KYE9; -.
DR   OMA; Q2KYE9; LANSCEL.
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    520       Glucose-6-phosphate isomerase.
FT                                /FTId=PRO_0000252610.
FT   ACT_SITE    327    327       Proton donor (By similarity).
FT   ACT_SITE    358    358       By similarity.
FT   ACT_SITE    486    486       By similarity.
SQ   SEQUENCE   520 AA;  56800 MW;  7695D4A3B9936D9A CRC64;
     MPQSLPFSPA WLAFEEAVRG ASHRGDHLRI IEGGGLSVDL TAQAYSPQLE AAGLALCEQQ
     GFALARRQLF EGGEANWTEH RPAWHTALRA ALPPPSVAKD ILNERERLRR FVDEADARGA
     YKYVLHLGIG GSDWGPRLVA RALRHQGLKR EVRFASNVDS HAVADAMHQL DPHETLVIVA
     SKSFTTTEPL ANAEVAIHWL QNAGVADPIK QVVAITANVD AALDFGISPQ HVFRFWDWVG
     GRYSLWSAIG LPIALAMGNN TFDELLAGAA AMDEHFLRAP LAANAPVQMA LAGLANRSVM
     GFNSLAIAPY DSRLAHLVPW AQQLEMESLG KVATRDGSPA GVPTGPVVWG MTGTDCQHTF
     FQWLHQDTTG APVDFIVCEH ADHTYDHHHR LLIANCLAQR AALLRGKSFE DALAETCARV
     DDPSEARILA EHLVHPGRRP STLIVLPRMT AHNLGALLAL YEHKVFTQGV LWGINPFDQW
     GVEFGKALAR GIIGELDKPS GMASADPSTR YWVDLLSRRS
//