ID   G6PI2_CHRSD             Reviewed;         559 AA.
AC   Q1QUG5;
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 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=Csal_2546;
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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP000285; ABE59893.1; -; Genomic_DNA.
DR   RefSeq; YP_574592.1; -.
DR   GeneID; 4026127; -.
DR   GenomeReviews; CP000285_GR; Csal_2546.
DR   KEGG; csa:Csal_2546; -.
DR   NMPDR; fig|290398.4.peg.1795; -.
DR   HOGENOM; Q1QUG5; -.
DR   OMA; Q1QUG5; FDGRAIT.
DR   BioCyc; CSAL290398:CSAL_2546-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    559       Glucose-6-phosphate isomerase 2.
FT                                /FTId=PRO_0000252616.
FT   ACT_SITE    367    367       Proton donor (By similarity).
FT   ACT_SITE    398    398       By similarity.
FT   ACT_SITE    522    522       By similarity.
SQ   SEQUENCE   559 AA;  62548 MW;  258533FEEE6CAD12 CRC64;
     MSQSTMIHHS EAWQALTQHA DGMRNVHLKS LFAEAPGHHA RFTRRGAGLT LDLSKHRWRD
     ETLTKLLALA REANLERAIE RLQNGERVNL SEDRPALHTA LRLPPEASLV VEGEDVVPDV
     HETLARMQAM VEKCHAGQWR GATGKAITDV VNLGVGGSDL GPLMVTHALA DYRPRDVHQV
     DIHFASTMDG SQLADYLTRF NPATTLFVLS SKSFTTIDTL SNASTARDWL MTRLADGGRD
     AGMREVVMRQ HFIGVSAKPE RMSEWGIDPR HQLRFWEWVG GRYSLWGAIG LPIALAVGME
     NFRELLAGAH EMDRHFRDTP LEDNLPVLLA LAGIWNVNFL DVRAHSILPY DGRLEYFASY
     LEQLEMESNG KSVTNDGEIT PYSTCPVLWG QLGPNAQHAF YQLLHQGTQA VECDFIAPVR
     RYDRVEDPAT RAHLKAQHRL TLANCIAQSR VLMLGDEALP SDAPRPSHKR YRGNQPSTTL
     LLDRLTPRTL GALIALYEHK VFVQATIWDI NPFDQWGVEL GKQIASETEQ ILASRRGAET
     LDDSSRGLLD VVWQAQDAT
//