ID   PGMI_THEVO              Reviewed;         304 AA.
AC   Q978F3;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   25-MAY-2022, entry version 88.
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=TV1464; ORFNames=TVG1514630;
OS   Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC
OS   15438 / GSS1).
OC   Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC   Thermoplasmataceae; Thermoplasma.
OX   NCBI_TaxID=273116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1;
RX   PubMed=11121031; DOI=10.1073/pnas.97.26.14257;
RA   Kawashima T., Amano N., Koike H., Makino S., Higuchi S., Kawashima-Ohya Y.,
RA   Watanabe K., Yamazaki M., Kanehori K., Kawamoto T., Nunoshiba T.,
RA   Yamamoto Y., Aramaki H., Makino K., Suzuki M.;
RT   "Archaeal adaptation to higher temperatures revealed by genomic sequence of
RT   Thermoplasma volcanium.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:14257-14262(2000).
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; BA000011; BAB60606.1; -; Genomic_DNA.
DR   RefSeq; WP_010917694.1; NC_002689.2.
DR   AlphaFoldDB; Q978F3; -.
DR   SMR; Q978F3; -.
DR   STRING; 273116.14325703; -.
DR   EnsemblBacteria; BAB60606; BAB60606; BAB60606.
DR   GeneID; 1442154; -.
DR   KEGG; tvo:TVG1514630; -.
DR   eggNOG; arCOG00052; Archaea.
DR   HOGENOM; CLU_059687_0_0_2; -.
DR   OMA; FPELNHN; -.
DR   OrthoDB; 55807at2157; -.
DR   PhylomeDB; Q978F3; -.
DR   Proteomes; UP000001017; 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.
FT   CHAIN           1..304
FT                   /note="Bifunctional phosphoglucose/phosphomannose
FT                   isomerase"
FT                   /id="PRO_0000227798"
FT   DOMAIN          16..147
FT                   /note="SIS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00797"
FT   ACT_SITE        196
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        212
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        300
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   304 AA;  34558 MW;  09BD551B9A286EA6 CRC64;
     MQFSEELLTL KDQVRFDKSF KVGKYDKIVI AGMGGSGIAG RIFSEIYDEK PVFLVDDYDI
     PSFVDDKTEF IAISYSGNTE ETISASEEAA KKHANVHAIT SGGSLSKMGF DTIIIPSGLQ
     PRSSIGYLLM PLVNTFIKPK IGDVDEAYRL LSETDKDNEE EKSIASEIYN GEHIPVIYGS
     RPFRAIAYRW KTQFNENAKV LAYSNYFSEL NHNDTMPLKD TYRKDEFYFL VFRSDDSRFS
     KRITVTEKIT GNSFRMVDVR GSSLLAKLFY LIHFGDYLTY HLAELRGVDP QDVSLIEKLK
     KEIA