G6PI2_PSEPK
ID G6PI2_PSEPK Reviewed; 554 AA.
AC Q88DW7;
DT 23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-MAY-2003, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Glucose-6-phosphate isomerase 2 {ECO:0000255|HAMAP-Rule:MF_00473};
DE Short=GPI 2 {ECO:0000255|HAMAP-Rule:MF_00473};
DE EC=5.3.1.9 {ECO:0000255|HAMAP-Rule:MF_00473};
DE AltName: Full=Phosphoglucose isomerase 2 {ECO:0000255|HAMAP-Rule:MF_00473};
DE Short=PGI 2 {ECO:0000255|HAMAP-Rule:MF_00473};
DE AltName: Full=Phosphohexose isomerase 2 {ECO:0000255|HAMAP-Rule:MF_00473};
DE Short=PHI 2 {ECO:0000255|HAMAP-Rule:MF_00473};
GN Name=pgi2 {ECO:0000255|HAMAP-Rule:MF_00473}; Synonyms=pgi-2;
GN OrderedLocusNames=PP_4701;
OS Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950
OS / KT2440).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=160488;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX PubMed=12534463; DOI=10.1046/j.1462-2920.2002.00366.x;
RA Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H.,
RA Martins dos Santos V.A.P., Fouts D.E., Gill S.R., Pop M., Holmes M.,
RA Brinkac L.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Kolonay J.F.,
RA Madupu R., Nelson W.C., White O., Peterson J.D., Khouri H.M., Hance I.,
RA Chris Lee P., Holtzapple E.K., Scanlan D., Tran K., Moazzez A.,
RA Utterback T.R., Rizzo M., Lee K., Kosack D., Moestl D., Wedler H.,
RA Lauber J., Stjepandic D., Hoheisel J., Straetz M., Heim S., Kiewitz C.,
RA Eisen J.A., Timmis K.N., Duesterhoeft A., Tuemmler B., Fraser C.M.;
RT "Complete genome sequence and comparative analysis of the metabolically
RT versatile Pseudomonas putida KT2440.";
RL Environ. Microbiol. 4:799-808(2002).
CC -!- FUNCTION: Catalyzes the reversible isomerization of glucose-6-phosphate
CC to fructose-6-phosphate. {ECO:0000255|HAMAP-Rule:MF_00473}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-glucose 6-phosphate = beta-D-fructose 6-phosphate;
CC Xref=Rhea:RHEA:11816, ChEBI:CHEBI:57634, ChEBI:CHEBI:58225;
CC EC=5.3.1.9; Evidence={ECO:0000255|HAMAP-Rule:MF_00473};
CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC {ECO:0000255|HAMAP-Rule:MF_00473}.
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 2/4.
CC {ECO:0000255|HAMAP-Rule:MF_00473}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00473}.
CC -!- SIMILARITY: Belongs to the GPI family. {ECO:0000255|HAMAP-
CC Rule:MF_00473, ECO:0000305}.
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DR EMBL; AE015451; AAN70274.1; -; Genomic_DNA.
DR RefSeq; NP_746810.1; NC_002947.4.
DR RefSeq; WP_010955350.1; NC_002947.4.
DR AlphaFoldDB; Q88DW7; -.
DR SMR; Q88DW7; -.
DR STRING; 160488.PP_4701; -.
DR EnsemblBacteria; AAN70274; AAN70274; PP_4701.
DR KEGG; ppu:PP_4701; -.
DR PATRIC; fig|160488.4.peg.5011; -.
DR eggNOG; COG0166; Bacteria.
DR HOGENOM; CLU_017947_3_1_6; -.
DR OMA; IGVWYIN; -.
DR PhylomeDB; Q88DW7; -.
DR BioCyc; PPUT160488:G1G01-5022-MON; -.
DR UniPathway; UPA00109; UER00181.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000000556; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR GO; GO:0004347; F:glucose-6-phosphate isomerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniRule.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule.
DR CDD; cd05015; SIS_PGI_1; 1.
DR CDD; cd05016; SIS_PGI_2; 1.
DR Gene3D; 1.10.1390.10; -; 1.
DR HAMAP; MF_00473; G6P_isomerase; 1.
DR InterPro; IPR001672; G6P_Isomerase.
DR InterPro; IPR023096; G6P_Isomerase_C.
DR InterPro; IPR018189; Phosphoglucose_isomerase_CS.
DR InterPro; IPR046348; SIS_dom_sf.
DR InterPro; IPR035476; SIS_PGI_1.
DR InterPro; IPR035482; SIS_PGI_2.
DR PANTHER; PTHR11469; PTHR11469; 1.
DR Pfam; PF00342; PGI; 1.
DR PRINTS; PR00662; G6PISOMERASE.
DR SUPFAM; SSF53697; SSF53697; 1.
DR PROSITE; PS00765; P_GLUCOSE_ISOMERASE_1; 1.
DR PROSITE; PS00174; P_GLUCOSE_ISOMERASE_2; 1.
DR PROSITE; PS51463; P_GLUCOSE_ISOMERASE_3; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Gluconeogenesis; Glycolysis; Isomerase; Reference proteome.
FT CHAIN 1..554
FT /note="Glucose-6-phosphate isomerase 2"
FT /id="PRO_0000180712"
FT ACT_SITE 359
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT ACT_SITE 390
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT ACT_SITE 518
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
SQ SEQUENCE 554 AA; 61455 MW; 06BDB4FD62122707 CRC64;
MAYYRTPHDV TALPAWQALQ KHRDAMQSFS MREAFAADAK RFDQFSLSAC GLFLDYSKNL
ITEQSRDLLV NLANEVGLQD AIKSMFSGEI INASEGRPVL HTALRRPVGD KLSVNGVNVM
PEVHKVLNQI TELVGRIHDG LWRGYSEKPI TDVVNIGIGG SFLGPELVSE ALLPYAQRGV
RCHYLANIDG SEFHELSANL RAETTLFIVS SKSFNTLETL KNAMAARTWY LAQGGSEAEL
YRHFIAVSSN KAAAVAFGIR EENIFPMWDW VGGRYSLWSA IGLPIALAIG TANFKELLSG
AYTMDQHFQT APFDKNMPVL LALLGVWYGN FWDANSHAIL PYDHYLRNIT KHLQQLDMES
NGKSVLQDGT PVKTDTGPVI WGGVGCNGQH AYHQLLHQGT QLIPADFIVP VVSFNPVADH
HQWLYANCLS QSQALMLGKT REEAEAELRA KGLNEADIEK LAPHKVIPGN RPSNTLVVER
ISPRRLGALV AMYEHKVFVQ SVIWGINAFD QWGVELGKEL GKGVYQRLVG SLEDSAEDGS
TQGLINYFRG RHRG
