ID   PGMI_AERPE              Reviewed;         333 AA.
AC   Q9YE01;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2007, sequence version 2.
DT   13-SEP-2023, entry version 94.
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=APE_0768.1;
OS   Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 /
OS   K1).
OC   Archaea; Thermoproteota; Thermoprotei; Desulfurococcales;
OC   Desulfurococcaceae; Aeropyrum.
OX   NCBI_TaxID=272557;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1;
RX   PubMed=10382966; DOI=10.1093/dnares/6.2.83;
RA   Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K.,
RA   Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A.,
RA   Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S.,
RA   Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A.,
RA   Aoki K., Kubota K., Nakamura Y., Nomura N., Sako Y., Kikuchi H.;
RT   "Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon,
RT   Aeropyrum pernix K1.";
RL   DNA Res. 6:83-101(1999).
RN   [2]
RP   CHARACTERIZATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1;
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=3.5 mM for glucose 6-phosphate {ECO:0000269|PubMed:14551194};
CC         KM=0.44 mM for fructose 6-phosphate {ECO:0000269|PubMed:14551194};
CC         KM=1.1 mM for mannose 6-phosphate {ECO:0000269|PubMed:14551194};
CC         Vmax=225 mmol/min/mg enzyme with glucose 6-phosphate as substrate (at
CC         80 degrees Celsius) {ECO:0000269|PubMed:14551194};
CC         Vmax=195 mmol/min/mg enzyme with fructose 6-phosphate as substrate
CC         (at 80 degrees Celsius) {ECO:0000269|PubMed:14551194};
CC         Vmax=209 mmol/min/mg enzyme with mannose 6-phosphate as substrate (at
CC         80 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 above 98 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; BA000002; BAA79746.2; -; Genomic_DNA.
DR   PIR; B72668; B72668.
DR   AlphaFoldDB; Q9YE01; -.
DR   SMR; Q9YE01; -.
DR   STRING; 272557.APE_0768.1; -.
DR   EnsemblBacteria; BAA79746; BAA79746; APE_0768.1.
DR   KEGG; ape:APE_0768.1; -.
DR   eggNOG; arCOG00052; Archaea.
DR   BRENDA; 5.3.1.8; 171.
DR   BRENDA; 5.3.1.9; 171.
DR   SABIO-RK; Q9YE01; -.
DR   Proteomes; UP000002518; 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   SUPFAM; SSF53697; SIS domain; 1.
DR   PROSITE; PS51464; SIS; 1.
PE   1: Evidence at protein level;
KW   Isomerase; Multifunctional enzyme; Reference proteome.
FT   CHAIN           1..333
FT                   /note="Bifunctional phosphoglucose/phosphomannose
FT                   isomerase"
FT                   /id="PRO_0000227544"
FT   DOMAIN          22..160
FT                   /note="SIS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00797"
FT   ACT_SITE        211
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        227
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        322
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   333 AA;  35942 MW;  3E94DE8CCF7E5DC3 CRC64;
     MEDLYLSWPK WFSEALARYS SLEGALEGVE EIYYCGMGGS GAAGDYIEAL LSIYAPQGPE
     FRVVKDFRPP RPPRHRGYGL VLASYSGNTL ETVECGSLLS PAAGRVVAVT SGGRLLEMAK
     ERGWLVARLP GGILPRVSFP WMLAASTAML SGALGVDLEA LKRLAGGLDT QGLKGEAERL
     AGFISRYRIA SLVTCGPGIP LAVRLKNELA ENAKMPSRLE IYPESSHNDI VALEAAEGLY
     GAVFIWIEHE GSLCPAVLDV VEGIYREYGV DTISIESSAR GGPNATVAEY LSRTLVFGLA
     SVRLALMRGF NPEETPPIDK YKRRLGEALR SQA
//