ID   PGMI_CALBD              Reviewed;         339 AA.
AC   Q44407; B9MPI2;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 2.
DT   24-JAN-2024, entry version 95.
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=Athe_0619;
OS   Caldicellulosiruptor bescii (strain ATCC BAA-1888 / DSM 6725 / KCTC 15123 /
OS   Z-1320) (Anaerocellum thermophilum).
OC   Bacteria; Bacillota; Clostridia; Caldicellulosiruptorales;
OC   Caldicellulosiruptoraceae; Caldicellulosiruptor.
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].
RC   STRAIN=ATCC BAA-1888 / DSM 6725 / KCTC 15123 / Z-1320;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA   Goodwin L., Pitluck S., Sims D., Meincke L., Brettin T., Detter J.C.,
RA   Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G.,
RA   Kataeva I., Adams M.W.W.;
RT   "Complete sequence of chromosome of Anaerocellum thermophilum DSM 6725.";
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ACM59743.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=CAA93628.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; Z69782; CAA93628.1; ALT_INIT; Genomic_DNA.
DR   EMBL; CP001393; ACM59743.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_015907196.1; NC_012034.1.
DR   AlphaFoldDB; Q44407; -.
DR   SMR; Q44407; -.
DR   STRING; 521460.Athe_0619; -.
DR   GeneID; 31771974; -.
DR   KEGG; ate:Athe_0619; -.
DR   eggNOG; COG2222; Bacteria.
DR   HOGENOM; CLU_059687_0_0_9; -.
DR   Proteomes; UP000007723; 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   Pfam; PF01380; SIS; 1.
DR   SUPFAM; SSF53697; SIS domain; 1.
DR   PROSITE; PS51464; SIS; 1.
PE   3: Inferred from homology;
KW   Isomerase; Multifunctional enzyme.
FT   CHAIN           1..339
FT                   /note="Bifunctional phosphoglucose/phosphomannose
FT                   isomerase"
FT                   /id="PRO_0000227792"
FT   DOMAIN          22..164
FT                   /note="SIS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00797"
FT   ACT_SITE        221
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        237
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        331
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
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
//