ID D7DRF1_METV3 Unreviewed; 431 AA.
AC D7DRF1;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=Probable glucose-6-phosphate isomerase {ECO:0000256|HAMAP-Rule:MF_00473};
DE Short=GPI {ECO:0000256|HAMAP-Rule:MF_00473};
DE EC=5.3.1.9 {ECO:0000256|HAMAP-Rule:MF_00473};
DE AltName: Full=Phosphoglucose isomerase {ECO:0000256|HAMAP-Rule:MF_00473};
DE Short=PGI {ECO:0000256|HAMAP-Rule:MF_00473};
DE AltName: Full=Phosphohexose isomerase {ECO:0000256|HAMAP-Rule:MF_00473};
DE Short=PHI {ECO:0000256|HAMAP-Rule:MF_00473};
GN Name=pgi {ECO:0000256|HAMAP-Rule:MF_00473};
GN OrderedLocusNames=Mvol_0051 {ECO:0000313|EMBL:ADI35711.1}, Mvol_0111
GN {ECO:0000313|EMBL:ADI35771.1};
OS Methanococcus voltae (strain ATCC BAA-1334 / A3).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanococcaceae; Methanococcus.
OX NCBI_TaxID=456320 {ECO:0000313|EMBL:ADI35711.1, ECO:0000313|Proteomes:UP000007722};
RN [1] {ECO:0000313|EMBL:ADI35711.1, ECO:0000313|Proteomes:UP000007722}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A3 {ECO:0000313|EMBL:ADI35711.1}, and ATCC BAA-1334 / A3
RC {ECO:0000313|Proteomes:UP000007722};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Lowry S., Clum A., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Whitman W.B., Woyke T.;
RT "Complete sequence of Methanococcus voltae A3.";
RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the reversible isomerization of glucose-6-phosphate
CC to fructose-6-phosphate. {ECO:0000256|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:0000256|ARBA:ARBA00029321,
CC ECO:0000256|HAMAP-Rule:MF_00473};
CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC {ECO:0000256|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:0000256|ARBA:ARBA00004926, ECO:0000256|HAMAP-Rule:MF_00473}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00473}.
CC -!- SIMILARITY: Belongs to the GPI family. {ECO:0000256|ARBA:ARBA00006604,
CC ECO:0000256|HAMAP-Rule:MF_00473}.
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DR EMBL; CP002057; ADI35711.1; -; Genomic_DNA.
DR EMBL; CP002057; ADI35771.1; -; Genomic_DNA.
DR AlphaFoldDB; D7DRF1; -.
DR STRING; 456320.Mvol_0051; -.
DR KEGG; mvo:Mvol_0051; -.
DR KEGG; mvo:Mvol_0111; -.
DR eggNOG; arCOG00052; Archaea.
DR HOGENOM; CLU_037303_1_0_2; -.
DR InParanoid; D7DRF1; -.
DR OrthoDB; 168618at2157; -.
DR UniPathway; UPA00109; UER00181.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000007722; 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 NCBIfam; NF040629; PGI_Meth; 1.
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 {ECO:0000256|HAMAP-Rule:MF_00473};
KW Gluconeogenesis {ECO:0000256|ARBA:ARBA00022432, ECO:0000256|HAMAP-
KW Rule:MF_00473};
KW Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|HAMAP-
KW Rule:MF_00473};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_00473};
KW Reference proteome {ECO:0000313|Proteomes:UP000007722}.
FT ACT_SITE 279
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
FT ACT_SITE 300
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
FT ACT_SITE 409
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
SQ SEQUENCE 431 AA; 48426 MW; 0238EDCE9FE2DB14 CRC64;
MKGTYKFNFD NVLKDKIGEN GISIDGIDEL RDFTNIAKAN VSKKYENGEL GFIEALDKDL
DEYEKVKELS KEFEYVIIIG IGGSILGSKA VHQGIYGSSN TYHPKVFYLD NSDPEKIYET
LKAVKLEKTL IFVISKSGNT VETLANYFVI KKHMDKNNII PAKPNFVAIT GGGLLQKIAE
KEGYMCYKVP ENVGGRFSVL SAVGLAPLAC LNVDIHNLVK GARKMNDICH TDNIFRNPAL
LNALIHYKMD NRGKKISLMM PYIGRLHQFG MWYRQLWAES LGKDGNGQTP VIALGATDQH
SQLQLYMDGP EDKIMTFLKV NKFKQDYSIE TDYDSDLIEH KLSELIISEQ LGTEQSITEK
GIPNVKITLS ELNEYTLGML MYGYELQTAY CGELLCINAF NQPAVEHAKK LSHAVLKGSI
VEKSYNEIKI E
//
