ID   PGMI_SULAC              Reviewed;         306 AA.
AC   Q4JCA7;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   16-JUN-2009, entry version 23.
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=Phosphoglucose isomerase;
DE            Short=PGI;
DE   AltName: Full=Mannose-6-phosphate isomerase;
DE            EC=5.3.1.8;
DE   AltName: Full=Phosphomannose isomerase;
DE            Short=PMI;
GN   OrderedLocusNames=Saci_0151;
OS   Sulfolobus acidocaldarius.
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=2285;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33909 / DSM 639 / IFO 15157 / JCM 8929 / NCIB 11770;
RX   PubMed=15995215; DOI=10.1128/JB.187.14.4992-4999.2005;
RA   Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E.,
RA   Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.;
RT   "The genome of Sulfolobus acidocaldarius, a model organism of the
RT   Crenarchaeota.";
RL   J. Bacteriol. 187:4992-4999(2005).
CC   -!- FUNCTION: Catalyzes the isomerization of both glucose 6-phosphate
CC       and epimeric mannose 6-phosphate at a similar catalytic efficiency
CC       (By similarity).
CC   -!- CATALYTIC ACTIVITY: D-glucose 6-phosphate = D-fructose 6-
CC       phosphate.
CC   -!- CATALYTIC ACTIVITY: D-mannose 6-phosphate = D-fructose 6-
CC       phosphate.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SIMILARITY: Belongs to the PGI/PMI family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP000077; AAY79572.1; -; Genomic_DNA.
DR   RefSeq; YP_254865.1; -.
DR   GeneID; 3474403; -.
DR   GenomeReviews; CP000077_GR; Saci_0151.
DR   KEGG; sai:Saci_0151; -.
DR   NMPDR; fig|330779.3.peg.254; -.
DR   HOGENOM; Q4JCA7; -.
DR   OMA; Q4JCA7; HNEIELY.
DR   BioCyc; SACI330779:SACI_0151-MON; -.
DR   BRENDA; 5.3.1.8; 434.
DR   BRENDA; 5.3.1.9; 434.
DR   GO; GO:0004347; F:glucose-6-phosphate isomerase activity; IEA:EC.
DR   GO; GO:0004476; F:mannose-6-phosphate isomerase activity; IEA:EC.
DR   GO; GO:0005529; F:sugar binding; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   InterPro; IPR011857; Glu6P/Mann6P_isomerase.
DR   InterPro; IPR019490; Glu6P/Mann6P_isomerase_C.
DR   InterPro; IPR001347; SIS.
DR   Pfam; PF10432; bact-PGI_C; 1.
DR   Pfam; PF01380; SIS; 1.
DR   TIGRFAMs; TIGR02128; G6PI_arch; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Isomerase; Multifunctional enzyme.
FT   CHAIN         1    306       Bifunctional
FT                                phosphoglucose/phosphomannose isomerase.
FT                                /FTId=PRO_0000227795.
FT   ACT_SITE    200    200       Proton acceptor (By similarity).
FT   ACT_SITE    216    216       Proton donor (By similarity).
FT   ACT_SITE    296    296       Proton acceptor (Probable).
SQ   SEQUENCE   306 AA;  34158 MW;  771F0D94933A67A4 CRC64;
     MSNVYERWKE FYEDAISRDI PGVKTAEKIA YFGIGGSGIP GEVLKLLDLP VEYKLFRSYK
     VNVDSKTTVV AVSYSGNTAE TLAGVKRAQE LGVKEIIVIT SGGKLKEIAE SKGYPLLSLP
     QGYQTRFIFP YIFTYLVRIL NQSTGSNYRV QDLVDGIQDN FTMLSEVSTR IANRITGKVP
     IFYASDLLPI AERFKQEVNE NAKYPAFFSQ LPEANHNEIE LYSSQQGNQF IPIVIPSDKI
     DEATASLINA ELIYPPYKSI LKNISGMFLI AGLASVKLAS QLNIKAEELR IIPKIRERTH
     NLLMGG
//