G6PI1_NEIMB
ID G6PI1_NEIMB Reviewed; 548 AA.
AC Q9JYX3;
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 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=NMB1388;
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; AAF41752.1; -; Genomic_DNA.
DR PIR; C81089; C81089.
DR RefSeq; NP_274402.1; NC_003112.2.
DR RefSeq; WP_002225136.1; NC_003112.2.
DR AlphaFoldDB; Q9JYX3; -.
DR SMR; Q9JYX3; -.
DR STRING; 122586.NMB1388; -.
DR PaxDb; Q9JYX3; -.
DR EnsemblBacteria; AAF41752; AAF41752; NMB1388.
DR KEGG; nme:NMB1388; -.
DR PATRIC; fig|122586.8.peg.1740; -.
DR HOGENOM; CLU_017947_3_1_4; -.
DR OMA; IGVWYIN; -.
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..548
FT /note="Glucose-6-phosphate isomerase 1"
FT /id="PRO_0000180693"
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; 62084 MW; 28A85A19BFF174E1 CRC64;
MKHLHDLPAW SKLWNHFDDS KTLHMREMFE QDPQRAERYW LQVGGLTLDY SKNRINDETM
SLLFELAREA GVPERMRQMF HGEKINTTEN 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 ELKAQGMDEV RIEELVPHKT FSGNRPTNLI LMDKVNPRNM
GSLIAMYEHK TFVQGIIWGI NSFDQWGVEL GKQLAKTILG ELTGETGPQK HDSSTERLIN
LYLQTNRK
