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   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=NMA2154;
OS   Neisseria meningitidis serogroup A / serotype 4A (strain DSM 15465 /
OS   Z2491).
OC   Bacteria; Proteobacteria; 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   OMA; CPAYAYG; -.
DR   BioCyc; NMEN122587:NMA_RS10960-MON; -.
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; 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.
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