ID   PGMI_ANATD              Reviewed;         339 AA.
AC   Q44407; B9MPI2;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 2.
DT   16-JUN-2009, entry version 37.
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=Athe_0619;
OS   Anaerocellum thermophilum (strain DSM 6725 / Z-1320).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Anaerocellum group;
OC   Anaerocellum.
OX   NCBI_TaxID=521460;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Zverlov V.V., Bronnenmeier K., Velikodvorskaya G.A.;
RL   Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Sims D., Meincke L., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ovchinnikova G., Kataeva I., Adams M.W.W.;
RT   "Complete sequence of chromosome of Anaerocellum thermophilum DSM
RT   6725.";
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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.
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DR   EMBL; Z69782; CAA93628.1; ALT_INIT; Genomic_DNA.
DR   EMBL; CP001393; ACM59743.1; ALT_INIT; Genomic_DNA.
DR   GenomeReviews; CP001393_GR; Athe_0619.
DR   KEGG; ate:Athe_0619; -.
DR   BRENDA; 5.3.1.8; 97802.
DR   BRENDA; 5.3.1.9; 97802.
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    339       Bifunctional
FT                                phosphoglucose/phosphomannose isomerase.
FT                                /FTId=PRO_0000227792.
FT   ACT_SITE    221    221       Proton acceptor (By similarity).
FT   ACT_SITE    237    237       Proton donor (By similarity).
FT   ACT_SITE    331    331       Proton acceptor (By similarity).
SQ   SEQUENCE   339 AA;  37787 MW;  7C5EE355D649B091 CRC64;
     MFESVYNLPE QIQKAYEIGK NISVNVKAED IDKVVITGLG GSAIGGNLLR VFVLDKCKIP
     VIVNRDYVLP AYVDSKTLVI ASSYSGNTEE TLSAYQDAKA KGAKIIAITT GGKLKEFAEK
     DGFDVITIPS GLQPRAALGY SFIPLLMLFV KLGLIEPVDD QIEETVKVLS DLRERYKPEV
     PEEKNLAKRL TLKLWNKLPI IYGISGTTEV IAERWKGQIC ENSKSPAYFN VFSELNHNEI
     VGTESPKHIL GLFEIVMLHD TEDHKRNAIR MDITKDLIKG VVSGVNDIYS IGNSRLARMF
     SLIYLGDYVS LYLATLYQND PTPVKKIDIL KNKLAEIKD
//