ID G6PI2_NEIMA Reviewed; 547 AA.
AC Q9JSS6; A1ITY1;
DT 02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 27-MAR-2024, entry version 117.
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=NMA2154;
OS Neisseria meningitidis serogroup A / serotype 4A (strain DSM 15465 /
OS Z2491).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=122587;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15465 / Z2491;
RX PubMed=10761919; DOI=10.1038/35006655;
RA Parkhill J., Achtman M., James K.D., Bentley S.D., Churcher C.M.,
RA Klee S.R., Morelli G., Basham D., Brown D., Chillingworth T., Davies R.M.,
RA Davis P., Devlin K., Feltwell T., Hamlin N., Holroyd S., Jagels K.,
RA Leather S., Moule S., Mungall K.L., Quail M.A., Rajandream M.A.,
RA Rutherford K.M., Simmonds M., Skelton J., Whitehead S., Spratt B.G.,
RA Barrell B.G.;
RT "Complete DNA sequence of a serogroup A strain of Neisseria meningitidis
RT Z2491.";
RL Nature 404:502-506(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; AL157959; CAM09250.1; -; Genomic_DNA.
DR PIR; G81787; G81787.
DR RefSeq; WP_002245857.1; NC_003116.1.
DR AlphaFoldDB; Q9JSS6; -.
DR SMR; Q9JSS6; -.
DR EnsemblBacteria; CAM09250; CAM09250; NMA2154.
DR KEGG; nma:NMA2154; -.
DR HOGENOM; CLU_017947_3_1_4; -.
DR UniPathway; UPA00109; UER00181.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000000626; 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; GLUCOSE-6-PHOSPHATE ISOMERASE; 1.
DR PANTHER; PTHR11469:SF1; GLUCOSE-6-PHOSPHATE ISOMERASE; 1.
DR Pfam; PF00342; PGI; 1.
DR PRINTS; PR00662; G6PISOMERASE.
DR SUPFAM; SSF53697; SIS domain; 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.
FT CHAIN 1..547
FT /note="Glucose-6-phosphate isomerase 2"
FT /id="PRO_0000180692"
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; 60359 MW; 31FCF5D51F1A9E39 CRC64;
MNAFTRAWYA LERHYQDTRH VLLRDRFACE PDRFERMHER LDGMLFDYSK NRLGEDTLQL
LCRLAETADL EGKMRALRTG AKVNNSEGRA ALHTALRLPD GAGAVYADGR DVLPEIRREL
NRALKFAHSL DDGSYQGTTG KRITDFVHIG IGGSDLGPAM CVQALEPFRR HIAVHFAANA
DPACLDEVLC RLNPETTVFC VASKSFKTPE TLLNAEAVKA WYRGAGFSES ETGCHFCAVS
ADTEAAQSFG IAAERVFAMY DWVGGRYSVW SPVGLPVMVA VGGARFRELL AGAHAMDSHF
FHTPPRRNIP VLMALIAVWY NNFQHADGQT AVPYSHNLRL LPAWLNQLDM ESLGKSRASD
GSPAACKTGG IVFGGEGVNC QHAYFQLLHQ GTRLIPCDFI VPMTAQGVED GRSRFTVANA
FAQAEALMKG KTLDEARAEL ADLPEAERER LAPHKEFPGN RPSNSILLER LTPYNLGMLM
AAYEHKTFVQ GVIWDINPFD QWGVEYGKQL AKTIIGELEG GTSVHDASTE GLMAFYRECR
LKGGGAA
//
