ID   G6PI1_COLP3             Reviewed;         546 AA.
AC   Q487J6;
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 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=CPS_1020;
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; AAZ27551.1; -; Genomic_DNA.
DR   RefSeq; YP_267769.1; -.
DR   GeneID; 3521810; -.
DR   GenomeReviews; CP000083_GR; CPS_1020.
DR   KEGG; cps:CPS_1020; -.
DR   NMPDR; fig|167879.3.peg.987; -.
DR   TIGR; CPS_1020; -.
DR   HOGENOM; Q487J6; -.
DR   OMA; Q487J6; GPKIVSQ.
DR   BioCyc; CPSY167879:CPS_1020-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    546       Glucose-6-phosphate isomerase 1.
FT                                /FTId=PRO_0000180629.
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   546 AA;  60935 MW;  F34654E22FAE76C7 CRC64;
     MSSRQTLASW KKLQLLAQDK KSQHMNTLFA QDSERFNKFS IELPNMLLDY SKNLIDTETL
     DALLALAEET QVCDWRAKMF AGEKINKTED RAVLHTALRR QSDEAFIIEG ENVTEHVKNQ
     LAEMEVFVNK VRQGHWLGYS GKRITDIVNI GVGGSNLGPQ MVTEALKHYS DGSVNVHYVS
     NVDGAQIAEV LRPLEPEKVL FIVSSKTFTT TETMTNARTA INWLTSASFD ENSVAKHFVA
     VTANKENAMS FGIEEQNIFD MWDWVGGRFS LWSAIGLAIA LDLGFDKFEE LLAGAHDMDQ
     HFINAPLKDN FPAILALISV WNTTFLGSQS QAILPYDQTL HMLTAYLQQA EMESNGKSVS
     WDGDEIDYAT VPSIWGELGI NGQHAFYQYL HQSNNVVPAD FIGSVKSVTP VKGHHETLMA
     NFFAQTQALM VGVNEEQVRA DLKAKGRNAE YIDNVAPHKV HKGNRPTNTI LLKCINPRNL
     GSLIAAYEHK IFVQGIILQI CSFDQWGVEL GKGLAAEIQT ELQTDNISAQ HDCSTSSLLK
     FYQSAK
//