ID   G6PI1_THIDA             Reviewed;         550 AA.
AC   Q3SK65;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   16-JUN-2009, entry version 27.
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=Tbd_0974;
OS   Thiobacillus denitrificans (strain ATCC 25259).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Hydrogenophilales;
OC   Hydrogenophilaceae; Thiobacillus.
OX   NCBI_TaxID=292415;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16452431; DOI=10.1128/JB.188.4.1473-1488.2006;
RA   Beller H.R., Chain P.S., Letain T.E., Chakicherla A., Larimer F.W.,
RA   Richardson P.M., Coleman M.A., Wood A.P., Kelly D.P.;
RT   "The genome sequence of the obligately chemolithoautotrophic,
RT   facultatively anaerobic bacterium Thiobacillus denitrificans.";
RL   J. Bacteriol. 188:1473-1488(2006).
CC   -!- CATALYTIC ACTIVITY: D-glucose 6-phosphate = D-fructose 6-
CC       phosphate.
CC   -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
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; CP000116; AAZ96927.1; -; Genomic_DNA.
DR   RefSeq; YP_314732.1; -.
DR   GeneID; 3671197; -.
DR   GenomeReviews; CP000116_GR; Tbd_0974.
DR   KEGG; tbd:Tbd_0974; -.
DR   NMPDR; fig|292415.3.peg.601; -.
DR   HOGENOM; Q3SK65; -.
DR   OMA; Q3SK65; LANSCEL.
DR   BioCyc; TDEN292415:TBD_0974-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_0000230939.
FT   ACT_SITE    353    353       Proton donor (By similarity).
FT   ACT_SITE    384    384       By similarity.
FT   ACT_SITE    512    512       By similarity.
SQ   SEQUENCE   550 AA;  61247 MW;  46D040BDA2F8EEBF CRC64;
     MKPLKTLPAW KALEQHFKSM RNFDMRAAFR EDAARFETLS LRCGNLLLDY SKNRVTQETM
     RHLAQLARES ELEEMRNAMC TGERINFTEK RAVLHVALRA PVRPALMVEG VDVEREIAKV
     LHRMQRFVES VHNGSWRGHT GKPIRNVVNI GIGGSDLGPA MVCHALDHYA VENVRVHFVS
     NLDPSHLAGT LAQLDPETTL FIVASKTFTT LETLANANSA KAWLLAALRA PEAVARHFVA
     LSTNAQAVEA FGIDPENMFI FWDWVGGRYS LWSAIGLSIA LQIGWGNFQA LLAGAHAMDV
     HFKEAPLEAN MPVILGMLGI WYANFWGTDT YGVFPYDQRL RLLVPFLQQL DMESNGKNVN
     RANKLVNYNT GPIVWGAPGT NGQHAFFELV HQGTRLIPTD FLVAAVNLTP LADQHEWLLA
     NCLAQTEALL KGKSRAVIEA ELIAQGMTRD DARALAPHKV FPGNRPSNTL LYQKLDPHTL
     GMLIALYEHK VFVQGVIWQI NSFDQWGVEL GKQLAPPIRA ALSSVRVIGE HDGSTQGLIA
     DIRRRRGLST
//