ID   G6PI1_NEIMA             Reviewed;         548 AA.
AC   Q9JTW1; A1ISI7;
DT   02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Glucose-6-phosphate isomerase 1 {ECO:0000255|HAMAP-Rule:MF_00473};
DE            Short=GPI 1 {ECO:0000255|HAMAP-Rule:MF_00473};
DE            EC=5.3.1.9 {ECO:0000255|HAMAP-Rule:MF_00473};
DE   AltName: Full=Phosphoglucose isomerase 1 {ECO:0000255|HAMAP-Rule:MF_00473};
DE            Short=PGI 1 {ECO:0000255|HAMAP-Rule:MF_00473};
DE   AltName: Full=Phosphohexose isomerase 1 {ECO:0000255|HAMAP-Rule:MF_00473};
DE            Short=PHI 1 {ECO:0000255|HAMAP-Rule:MF_00473};
GN   Name=pgi1 {ECO:0000255|HAMAP-Rule:MF_00473}; OrderedLocusNames=NMA1604;
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; CAM08745.1; -; Genomic_DNA.
DR   PIR; A81854; A81854.
DR   RefSeq; WP_002245967.1; NC_003116.1.
DR   AlphaFoldDB; Q9JTW1; -.
DR   SMR; Q9JTW1; -.
DR   EnsemblBacteria; CAM08745; CAM08745; NMA1604.
DR   KEGG; nma:NMA1604; -.
DR   HOGENOM; CLU_017947_3_1_4; -.
DR   OMA; IGVWYIN; -.
DR   BioCyc; NMEN122587:NMA_RS08030-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..548
FT                   /note="Glucose-6-phosphate isomerase 1"
FT                   /id="PRO_0000180691"
FT   ACT_SITE        353
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT   ACT_SITE        384
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT   ACT_SITE        512
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
SQ   SEQUENCE   548 AA;  62026 MW;  4BC7F50C0D674BFB CRC64;
     MKHLHDLPAW SKLWNHFDDS KTLHMREMFE QDPQRAERYW LQVGGLTLDY SKNRINDETM
     SLLFELAHEA GVPERMRQMF HGKKINTTEN RAVLHVALRN RTNSPIVVDG EDVMPKVNRV
     LQRMGEFAHE VRSGSWLGYT NQVITDVVNI GIGGSDLGPL MMCTALKPFG HPRLNMHFVS
     NVDGSQLRDV LSKVHPETTL FIIASKTFTT QETLTNALTA REWFLNHAGD EEAVAKHFAA
     VSTNQKAVAE FGIDTANMFE FWDWVGGRYS LWSAIGLPIM LYLGEENFIE MLNGAHLMDQ
     HFINTPLERN LPVILALIGI WYINYYGGGS HVIAPYDQHL HRLPKFIQQL DMESNGKQVT
     LDGKAVGHET SPIIWGETGI NGQHAFFQLL HQGTHITPID LIASLEKRSN LPGHHEILLA
     NVFAQAEAFM RGKTPDEVRA ELKAQGMDEA RIEELVPHKT FSGNRPTNLI LMDKVNPRNM
     GSLIAMYEHK TFVQGIIWGI NSFDQWGVEL GKQLAKTILG ELTGETGSQK HDSSTERLIN
     LYLQTNRK