G6PI2_NEIMB
ID G6PI2_NEIMB Reviewed; 547 AA.
AC Q9K153;
DT 02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 112.
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}; OrderedLocusNames=NMB0334;
OS Neisseria meningitidis serogroup B (strain MC58).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=122586;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MC58;
RX PubMed=10710307; DOI=10.1126/science.287.5459.1809;
RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E.,
RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C.,
RA Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H.,
RA Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., Mason T.M.,
RA Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D.,
RA Utterback T.R., Khouri H.M., Qin H., Vamathevan J.J., Gill J., Scarlato V.,
RA Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M.,
RA Moxon E.R., Rappuoli R., Venter J.C.;
RT "Complete genome sequence of Neisseria meningitidis serogroup B strain
RT MC58.";
RL Science 287:1809-1815(2000).
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; AE002098; AAF40777.1; -; Genomic_DNA.
DR PIR; A81211; A81211.
DR RefSeq; NP_273383.1; NC_003112.2.
DR RefSeq; WP_002224874.1; NC_003112.2.
DR AlphaFoldDB; Q9K153; -.
DR SMR; Q9K153; -.
DR STRING; 122586.NMB0334; -.
DR PaxDb; Q9K153; -.
DR EnsemblBacteria; AAF40777; AAF40777; NMB0334.
DR KEGG; nme:NMB0334; -.
DR PATRIC; fig|122586.8.peg.422; -.
DR HOGENOM; CLU_017947_3_1_4; -.
DR OMA; CPAYAYG; -.
DR UniPathway; UPA00109; UER00181.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000000425; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR GO; GO:0004347; F:glucose-6-phosphate isomerase activity; IBA:GO_Central.
DR GO; GO:0048029; F:monosaccharide binding; IBA:GO_Central.
DR GO; GO:0006094; P:gluconeogenesis; IBA:GO_Central.
DR GO; GO:0051156; P:glucose 6-phosphate metabolic process; IBA:GO_Central.
DR GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
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..547
FT /note="Glucose-6-phosphate isomerase 2"
FT /id="PRO_0000180694"
FT ACT_SITE 351
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT ACT_SITE 382
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT ACT_SITE 508
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
SQ SEQUENCE 547 AA; 60199 MW; 54B0CC7FB74BA028 CRC64;
MNAFTRAWYA LERHYQDTRH VLLRDRFACE PDRFERMHER LDGMLFDYSK NRLGEDTLQL
LCNLADAADL EGKMRALRTG AKVNGSEGRA ALHTALRLPD GADAVYVDGR DVLPEIRREL
NRALKFAHSL DDGSYQGITG KRITDFVHIG IGGSDLGPAM CVQALEPFRR HITVHFAANA
DPACLDAVLC RLNPETTVFC VASKSFKTPE TLLNAQAVKA WYRGAGFSES ETACHFCAVS
ADTAAAAAFG IAAERVFAMY DWVGGRYSVW SPVGLPVMVA VGGARFRELL AGAHAMDRHF
FSTPTRHNIP VLMALIAVWY NNFQHADGQT AVPYSHNLRL LPAWLNQLDM ESLGKSRASD
GSPAVCKTGG IVFGGEGVNC QHAYFQLLHQ GTRLIPCDFI VPMTAQGRED GRSRFTVANA
FAQAEALMKG KTLDEARAEL ADLPEAERER LAPHKEFPGN RPSNSILIDR LTPYNLGMLM
AAYEHKTFVQ GAIWNVNPFD QWGVEYGKQL AKTIIGELEG GTSVHDASTE GLMAFYRECR
LKGGGAA
