ID   G6PI2_COLP3             Reviewed;         551 AA.
AC   Q483D3;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   16-JUN-2009, entry version 25.
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=CPS_2108;
OS   Colwellia psychrerythraea (strain 34H / ATCC BAA-681) (Vibrio
OS   psychroerythus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Colwelliaceae; Colwellia.
OX   NCBI_TaxID=167879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16043709; DOI=10.1073/pnas.0504766102;
RA   Methe B.A., Nelson K.E., Deming J.W., Momen B., Melamud E., Zhang X.,
RA   Moult J., Madupu R., Nelson W.C., Dodson R.J., Brinkac L.M.,
RA   Daugherty S.C., Durkin A.S., DeBoy R.T., Kolonay J.F., Sullivan S.A.,
RA   Zhou L., Davidsen T.M., Wu M., Huston A.L., Lewis M., Weaver B.,
RA   Weidman J.F., Khouri H., Utterback T.R., Feldblyum T.V., Fraser C.M.;
RT   "The psychrophilic lifestyle as revealed by the genome sequence of
RT   Colwellia psychrerythraea 34H through genomic and proteomic
RT   analyses.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:10913-10918(2005).
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; CP000083; AAZ25825.1; -; Genomic_DNA.
DR   RefSeq; YP_268834.1; -.
DR   GeneID; 3520071; -.
DR   GenomeReviews; CP000083_GR; CPS_2108.
DR   KEGG; cps:CPS_2108; -.
DR   NMPDR; fig|167879.3.peg.2020; -.
DR   TIGR; CPS_2108; -.
DR   HOGENOM; Q483D3; -.
DR   OMA; Q483D3; NSPDINF.
DR   BioCyc; CPSY167879:CPS_2108-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    551       Glucose-6-phosphate isomerase 2.
FT                                /FTId=PRO_0000180630.
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   551 AA;  60730 MW;  79AC8B0F995DD572 CRC64;
     MDIKKLSSLA HCAKTRSIVS LFDQKERAND FSLSTSHLYL DYSKQNITDV ELEQLIEIAE
     DVGLSESITG QFNGDKINNT EGRSVLHTIL RAPQVIKQQI LGDTLANEVE AAELQMAKVV
     NDVQKGILTS HTGQRFTDVL AIGIGGSYYG VKVSLSALEH YRDLALSVHV IANVDGGALE
     EKLKTLNFET TLVVVISKTF TTQETMLNAK AVKQWMLSCA SVKDLELNNV PLIIEKQWFA
     VSSNIEAAKE FGINIKHILP MWDWVGGRFS IWSTVGLPLA LAIGNDNFNK LKQGAYEMDV
     HFKSTDFKNN MPVIMALLGI WNRNALEYPT LAILPYAHSL RALPGYLQQT DMESNGKSVS
     KSGDKLSWLT APVVFGQEGT NGQHAFMQLM HQSDDIIPTD FIVALKGRSQ YTENHKVLVA
     NCFAQSEALM QGKTLTQVES ELEMSALSTA EISLIAPHKT MKGNTPSNTL VMDLLTPETI
     GSLLALYEHK IFVQGVLWQV NSFDQWGVEL GKQLGTRILS AIDGAEDDLL SASSQSLIAR
     FRARSNVTPS V
//