PGMI_THEAC
ID PGMI_THEAC Reviewed; 310 AA.
AC Q9HIC2;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 98.
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=Ta1419;
OS Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC
OS 15155 / AMRC-C165).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Thermoplasmataceae; Thermoplasma.
OX NCBI_TaxID=273075;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX PubMed=11029001; DOI=10.1038/35035069;
RA Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C.,
RA Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.;
RT "The genome sequence of the thermoacidophilic scavenger Thermoplasma
RT acidophilum.";
RL Nature 407:508-513(2000).
RN [2]
RP CHARACTERIZATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=14551194; DOI=10.1074/jbc.m309849200;
RA Hansen T., Wendor ff D., Schoenheit P.;
RT "Bifunctional phosphoglucose/phosphomannose isomerases from the archaea
RT Aeropyrum pernix and Thermoplasma acidophilum constitute a novel enzyme
RT family within the phosphoglucose isomerase superfamily.";
RL J. Biol. Chem. 279:2262-2272(2004).
CC -!- FUNCTION: Catalyzes the isomerization of both glucose 6-phosphate and
CC epimeric mannose 6-phosphate at a similar catalytic efficiency.
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 -!- ACTIVITY REGULATION: Inhibited by erythrose 4-phosphate and 6-
CC phosphogluconate.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.72 mM for glucose 6-phosphate {ECO:0000269|PubMed:14551194};
CC KM=0.2 mM for fructose 6-phosphate {ECO:0000269|PubMed:14551194};
CC KM=0.25 mM for mannose 6-phosphate {ECO:0000269|PubMed:14551194};
CC Vmax=83 mmol/min/mg enzyme with glucose 6-phosphate as substrate (at
CC 50 degrees Celsius) {ECO:0000269|PubMed:14551194};
CC Vmax=57 mmol/min/mg enzyme with fructose 6-phosphate as substrate (at
CC 50 degrees Celsius) {ECO:0000269|PubMed:14551194};
CC Vmax=75 mmol/min/mg enzyme with mannose 6-phosphate as substrate (at
CC 50 degrees Celsius) {ECO:0000269|PubMed:14551194};
CC pH dependence:
CC Optimum pH is 7.6. {ECO:0000269|PubMed:14551194};
CC Temperature dependence:
CC Optimum temperature is 75 degrees Celsius.
CC {ECO:0000269|PubMed:14551194};
CC -!- SUBUNIT: Homodimer.
CC -!- SIMILARITY: Belongs to the PGI/PMI family. {ECO:0000305}.
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DR EMBL; AL445067; CAC12539.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9HIC2; -.
DR SMR; Q9HIC2; -.
DR STRING; 273075.Ta1419; -.
DR PRIDE; Q9HIC2; -.
DR EnsemblBacteria; CAC12539; CAC12539; CAC12539.
DR KEGG; tac:Ta1419; -.
DR eggNOG; arCOG00052; Archaea.
DR HOGENOM; CLU_059687_0_0_2; -.
DR OMA; FPELNHN; -.
DR BRENDA; 5.3.1.8; 6324.
DR BRENDA; 5.3.1.9; 6324.
DR SABIO-RK; Q9HIC2; -.
DR Proteomes; UP000001024; 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 SUPFAM; SSF53697; SSF53697; 1.
DR PROSITE; PS51464; SIS; 1.
PE 1: Evidence at protein level;
KW Isomerase; Multifunctional enzyme; Reference proteome.
FT CHAIN 1..310
FT /note="Bifunctional phosphoglucose/phosphomannose
FT isomerase"
FT /id="PRO_0000227545"
FT DOMAIN 22..152
FT /note="SIS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00797"
FT ACT_SITE 202
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 218
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 306
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
SQ SEQUENCE 310 AA; 35045 MW; A88423F901339B1F CRC64;
MLRSHCMEFS EELKTLKDQV RFDGSFRTGT FSNIVIAGMG GSGIAGRIFS EMYSAKPVFV
CDDYHIPEFV DGNTEFIAVS YSGNTEETLS AAEEAIKKGA KVHAITSGGR LSEMGVDTIK
IPGGLQPRSA VGYLTMPIIN TFIRPKHEDI EEAAGLLSDL DKNNTVQENI ATEIYAGRRI
PVIYGSTPYR SVAYRWKTQF NENAKILAYS NYFSELNHND TMPLRDTYRK DEFYFMAFDS
TDERIRKRIE VTQKITGTSF KKIEARGSSL IARIFYLIHF GDYVTYHLAR IRNVDPQDVS
AIEDLKKRIS
