G6PI_METMP
ID G6PI_METMP Reviewed; 438 AA.
AC Q6LXQ4;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Probable glucose-6-phosphate isomerase {ECO:0000255|HAMAP-Rule:MF_00473};
DE Short=GPI {ECO:0000255|HAMAP-Rule:MF_00473};
DE EC=5.3.1.9 {ECO:0000255|HAMAP-Rule:MF_00473};
DE AltName: Full=Phosphoglucose isomerase {ECO:0000255|HAMAP-Rule:MF_00473};
DE Short=PGI {ECO:0000255|HAMAP-Rule:MF_00473};
DE AltName: Full=Phosphohexose isomerase {ECO:0000255|HAMAP-Rule:MF_00473};
DE Short=PHI {ECO:0000255|HAMAP-Rule:MF_00473};
GN Name=pgi {ECO:0000255|HAMAP-Rule:MF_00473}; OrderedLocusNames=MMP1295;
OS Methanococcus maripaludis (strain S2 / LL).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanococcaceae; Methanococcus.
OX NCBI_TaxID=267377;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S2 / LL;
RX PubMed=15466049; DOI=10.1128/jb.186.20.6956-6969.2004;
RA Hendrickson E.L., Kaul R., Zhou Y., Bovee D., Chapman P., Chung J.,
RA Conway de Macario E., Dodsworth J.A., Gillett W., Graham D.E., Hackett M.,
RA Haydock A.K., Kang A., Land M.L., Levy R., Lie T.J., Major T.A.,
RA Moore B.C., Porat I., Palmeiri A., Rouse G., Saenphimmachak C., Soell D.,
RA Van Dien S., Wang T., Whitman W.B., Xia Q., Zhang Y., Larimer F.W.,
RA Olson M.V., Leigh J.A.;
RT "Complete genome sequence of the genetically tractable hydrogenotrophic
RT methanogen Methanococcus maripaludis.";
RL J. Bacteriol. 186:6956-6969(2004).
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}.
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DR EMBL; BX950229; CAF30851.1; -; Genomic_DNA.
DR RefSeq; WP_011171239.1; NC_005791.1.
DR AlphaFoldDB; Q6LXQ4; -.
DR SMR; Q6LXQ4; -.
DR STRING; 267377.MMP1295; -.
DR EnsemblBacteria; CAF30851; CAF30851; MMP1295.
DR GeneID; 2761531; -.
DR KEGG; mmp:MMP1295; -.
DR PATRIC; fig|267377.15.peg.1328; -.
DR eggNOG; arCOG00052; Archaea.
DR HOGENOM; CLU_037303_1_0_2; -.
DR OMA; CPAYAYG; -.
DR OrthoDB; 24853at2157; -.
DR BioCyc; MMAR267377:MMP_RS06670-MON; -.
DR UniPathway; UPA00109; UER00181.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000000590; 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 HAMAP; MF_00473; G6P_isomerase; 1.
DR InterPro; IPR001672; G6P_Isomerase.
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..438
FT /note="Probable glucose-6-phosphate isomerase"
FT /id="PRO_0000180781"
FT ACT_SITE 280
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT ACT_SITE 301
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT ACT_SITE 410
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
SQ SEQUENCE 438 AA; 49256 MW; 673BF4111B45FE49 CRC64;
MNGELSFKYD NVMEENLGNL GISNGKLESF NNESSKIIEI LKEKELNGEF GFLDVLNDNL
DKYYELNEYS KNFENILIIG IGGSNLGLRA AETGILGSFT SRYEIPRIYY MDNSDPEKTH
DILSNIDLEK TLVFVISKSG NTVETLANFF IVRNLMKKKN IDLEKHVVSI TSGGELEKIT
KKENYIHFEV PENVGGRFSV LSSVGIAPLS CTSVDIKKLI DGAKSIEKSC KCEDIFKNPA
LMNAVIHKLM YNRGKTVSVM MPYIERLRSF GMWYGQLWAE SLGKNGFGQT PVIAVGATSQ
HSQLQLYMDG PNDKIATFLK VNKYRNDLKI EYEYDHHLSG HNLSEVITSE LVGTENSMKH
NNIPNVKITL SKLNEITMGK LFLMYEMQTA ISGELYGINA FDQPAVEYGK KIAHECLTGS
KVDSENKYIN GKYIITSK