ID   G6PI1_CHRSD             Reviewed;         548 AA.
AC   Q1QZ19;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   16-JUN-2009, entry version 23.
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=Csal_0932;
OS   Chromohalobacter salexigens (strain DSM 3043 / ATCC BAA-138 / NCIMB
OS   13768).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Chromohalobacter.
OX   NCBI_TaxID=290398;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Brettin T.,
RA   Bruce D., Han C., Tapia R., Gilna P., Saunders E., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Csonka L.N.,
RA   O'Conner K., Vreeland R.H., Oren A., Vargas C., Nieto J., Arahal D.R.,
RA   Goodner B., Wheeler C., Hall P., Ewing A., Benson L., McBeath D.,
RA   Canovas D., Richardson P.;
RT   "Complete sequence of Chromohalobacter salexigens DSM 3043.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000285; ABE58289.1; -; Genomic_DNA.
DR   RefSeq; YP_572988.1; -.
DR   GeneID; 4026786; -.
DR   GenomeReviews; CP000285_GR; Csal_0932.
DR   KEGG; csa:Csal_0932; -.
DR   NMPDR; fig|290398.4.peg.922; -.
DR   HOGENOM; Q1QZ19; -.
DR   OMA; Q1QZ19; GPKIVSQ.
DR   BioCyc; CSAL290398:CSAL_0932-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    548       Glucose-6-phosphate isomerase 1.
FT                                /FTId=PRO_0000252615.
FT   ACT_SITE    353    353       Proton donor (By similarity).
FT   ACT_SITE    384    384       By similarity.
FT   ACT_SITE    495    495       By similarity.
SQ   SEQUENCE   548 AA;  61466 MW;  6B3402F328E242F9 CRC64;
     MFQLTRSVTW RALERLKQET FDDRISDYFA ADPQRFEKMS LRVGGLFLDY SKHHVSDAVL
     AKLIELADHS ALVQRRAQMF SGDIINVTED RPVLHTALRH LGDEPVYADG KDVMPEIQST
     REQIKRFSEA VRSGEWKGYS GERIKDVVNI GIGGSDLGPN MACRALLKYR HPELNFHFVS
     NVDGTHIQKV LQRLDPATTL FIVSTKTFST QETLLNAKTA RRWFLDNAGE DADVGAHFIA
     ASTNRKAAME FGIREENVFE FWAWVGGRYS MWSSIGLPIA LSIGFDGFME LLEGAHEMDR
     HFIEAPFAEN MPVLMALIGI WYINFIGAET HAIVPYDQAL HQLPSFLQQL DMESNGKSVD
     IFDQPVNYKT GPIVWGQTGS NGQHAFFQLL HQGTRYVPID FIASLKPEPG FEDHHFALLT
     NMLAQANAFM EGSQDGSQLD PYSCPGNRPS STLLLDELTP RNLGALIALY EHKVFVQGVI
     WNINSFDQWG VQLGKRIAGE ISERIDTNVG DFDASTQGLL SLVREYFPAS TPDAKASDNN
     KKSRGKTS
//