ID   PGMI_AQUAE              Reviewed;         320 AA.
AC   O66954;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   27-MAR-2024, entry version 102.
DE   RecName: Full=Bifunctional phosphoglucose/phosphomannose isomerase;
DE   AltName: Full=Glucose-6-phosphate isomerase;
DE            Short=GPI;
DE            EC=5.3.1.9;
DE   AltName: Full=Mannose-6-phosphate isomerase;
DE            EC=5.3.1.8;
DE   AltName: Full=Phosphoglucose isomerase;
DE            Short=PGI;
DE   AltName: Full=Phosphomannose isomerase;
DE            Short=PMI;
GN   OrderedLocusNames=aq_750;
OS   Aquifex aeolicus (strain VF5).
OC   Bacteria; Aquificota; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX   NCBI_TaxID=224324;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VF5;
RX   PubMed=9537320; DOI=10.1038/32831;
RA   Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA   Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA   Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT   "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL   Nature 392:353-358(1998).
CC   -!- FUNCTION: Catalyzes the isomerization of both glucose 6-phosphate and
CC       epimeric mannose 6-phosphate at a similar catalytic efficiency.
CC       {ECO:0000250}.
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;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-mannose 6-phosphate = D-fructose 6-phosphate;
CC         Xref=Rhea:RHEA:12356, ChEBI:CHEBI:58735, ChEBI:CHEBI:61527;
CC         EC=5.3.1.8;
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the PGI/PMI family. {ECO:0000305}.
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DR   EMBL; AE000657; AAC06906.1; -; Genomic_DNA.
DR   PIR; G70365; G70365.
DR   RefSeq; NP_213515.1; NC_000918.1.
DR   RefSeq; WP_010880453.1; NC_000918.1.
DR   AlphaFoldDB; O66954; -.
DR   SMR; O66954; -.
DR   STRING; 224324.aq_750; -.
DR   EnsemblBacteria; AAC06906; AAC06906; aq_750.
DR   KEGG; aae:aq_750; -.
DR   PATRIC; fig|224324.8.peg.598; -.
DR   eggNOG; COG2222; Bacteria.
DR   HOGENOM; CLU_059687_0_0_0; -.
DR   InParanoid; O66954; -.
DR   OrthoDB; 9771734at2; -.
DR   Proteomes; UP000000798; Chromosome.
DR   GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR   GO; GO:0004347; F:glucose-6-phosphate isomerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004476; F:mannose-6-phosphate isomerase activity; IEA:UniProtKB-EC.
DR   GO; GO:1901135; P:carbohydrate derivative metabolic process; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd05017; SIS_PGI_PMI_1; 1.
DR   CDD; cd05637; SIS_PGI_PMI_2; 1.
DR   InterPro; IPR019490; Glu6P/Mann6P_isomerase_C.
DR   InterPro; IPR001347; SIS_dom.
DR   InterPro; IPR046348; SIS_dom_sf.
DR   InterPro; IPR035484; SIS_PGI/PMI_1.
DR   NCBIfam; TIGR02128; G6PI_arch; 1.
DR   Pfam; PF10432; bact-PGI_C; 1.
DR   Pfam; PF01380; SIS; 1.
DR   SUPFAM; SSF53697; SIS domain; 1.
DR   PROSITE; PS51464; SIS; 1.
PE   3: Inferred from homology;
KW   Isomerase; Multifunctional enzyme; Reference proteome.
FT   CHAIN           1..320
FT                   /note="Bifunctional phosphoglucose/phosphomannose
FT                   isomerase"
FT                   /id="PRO_0000227793"
FT   DOMAIN          20..153
FT                   /note="SIS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00797"
FT   ACT_SITE        204
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        220
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        313
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   320 AA;  36847 MW;  732BD143902F5AC7 CRC64;
     MEEVYKVVEG FYNQFEWEDI AKDLTPYKGI VFCGMGGSGI IGSFASKWLE HRSFNKPTFV
     VKDYTLPPFV DRDYLVFCIS YSGNTEETLS NFEEAIGRGI KPLCITSNGK LMERAKEEGC
     EIYEVPKGFQ PRYSLGFMLS KVLNLLGVDK DELEDAKENL KENLESLKQK GKEIANRIYG
     YIPVVYSTPL TAHIAERWKG QINENSKSPA YFTILPEMHH NEVMGWSNPE LRNKFVYLLM
     FDEKDHHRVK LRVDITKKIL EDFGVVPIML KGEGNSYLAR SLYLVHLADW VSVFLAELYG
     YDPVPVKTIE RIKEELKKHA
//