PGMI_AQUAE
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 03-AUG-2022, entry version 97.
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; 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 OMA; FPELNHN; -.
DR OrthoDB; 1179564at2; -.
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 Pfam; PF10432; bact-PGI_C; 1.
DR Pfam; PF01380; SIS; 1.
DR SUPFAM; SSF53697; SSF53697; 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
