ID   G6PI2_THIDA             Reviewed;         554 AA.
AC   Q3SH73;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 2.
DT   16-JUN-2009, entry version 27.
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=Tbd_2063;
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; AAZ98016.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; YP_315821.1; -.
DR   GeneID; 3672234; -.
DR   GenomeReviews; CP000116_GR; Tbd_2063.
DR   KEGG; tbd:Tbd_2063; -.
DR   NMPDR; fig|292415.3.peg.2219; -.
DR   HOGENOM; Q3SH73; -.
DR   BioCyc; TDEN292415:TBD_2063-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    554       Glucose-6-phosphate isomerase 2.
FT                                /FTId=PRO_0000230940.
FT   ACT_SITE    360    360       Proton donor (By similarity).
FT   ACT_SITE    391    391       By similarity.
FT   ACT_SITE    514    514       By similarity.
SQ   SEQUENCE   554 AA;  62388 MW;  7A4EAAA90F8EE01B CRC64;
     MRTGDTRTSG LSTRPVHRLL QAHHSRMADV HMRELFDTDP QRFERFSLQV GDLLLDYSKN
     RITDETMDLL VRMAEESDVA GWRERMFRGD KINTTENRAV LHVALRNRSN RPVNVDGEDV
     MPKVNAVIER MGAFAEQVRG GVWRGYSGAL ITDVVNIGIG GSDLGPQMVV QALKPYRHPR
     LKLHFISNVD GAHVKETLEA LDPETTLFIV SSKTFTTQET MTNAHYARDW FLARAGDVAH
     VARHFVAVST NRDAVTAFGI DAANMFEFWD WVGGRYSLWS AIGLSIVLAV GAERFLELLE
     GAHEMDEHFR HAPLRQNMPV ILALLGIWYN NFFGAESHAI LPYDHYLRSL PAYLEQADME
     SNGKSVDRDG RVVDYPTGQI IWGATGINGQ HAFYQLLHQG TKMIPADFIV SITPHTELQE
     HHDILIANFL AQTEALMRGR TREETLEEMG RSPGDPSVQH RVFEGNHPSN AILLKKLTPH
     TLGMLIALYE HKIFVEGVIW NLNSYDQWGV ELGKQLAGRI LPELHADAPV AGHDASTNAL
     INHYRRMTQP HPGL
//