(data stored in ACNUC7421 zone)

SWISSPROT: B7UKX0_ECO27

ID   B7UKX0_ECO27            Unreviewed;       546 AA.
AC   B7UKX0;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   08-MAY-2019, entry version 59.
DE   SubName: Full=Phosphoglucomutase {ECO:0000313|EMBL:CAS08128.1};
GN   Name=pgm {ECO:0000313|EMBL:CAS08128.1};
GN   OrderedLocusNames=E2348C_0580 {ECO:0000313|EMBL:CAS08128.1};
OS   Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=574521 {ECO:0000313|EMBL:CAS08128.1, ECO:0000313|Proteomes:UP000008205};
RN   [1] {ECO:0000313|EMBL:CAS08128.1, ECO:0000313|Proteomes:UP000008205}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E2348/69 / EPEC {ECO:0000313|Proteomes:UP000008205};
RX   PubMed=18952797; DOI=10.1128/JB.01238-08;
RA   Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T.,
RA   Henderson I.R., Harris D., Asadulghani M., Kurokawa K., Dean P.,
RA   Kenny B., Quail M.A., Thurston S., Dougan G., Hayashi T., Parkhill J.,
RA   Frankel G.;
RT   "Complete genome sequence and comparative genome analysis of
RT   enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL   J. Bacteriol. 191:347-354(2009).
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|SAAS:SAAS00609101};
CC   -!- SIMILARITY: Belongs to the phosphohexose mutase family.
CC       {ECO:0000256|RuleBase:RU004326, ECO:0000256|SAAS:SAAS00551227}.
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DR   EMBL; FM180568; CAS08128.1; -; Genomic_DNA.
DR   RefSeq; WP_001339347.1; NC_011601.1.
DR   EnsemblBacteria; CAS08128; CAS08128; E2348C_0580.
DR   KEGG; ecg:E2348C_0580; -.
DR   HOGENOM; HOG000268677; -.
DR   KO; K01835; -.
DR   OMA; DIYKIYA; -.
DR   BioCyc; ECOL574521:E2348C_RS03075-MONOMER; -.
DR   Proteomes; UP000008205; Chromosome.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0004614; F:phosphoglucomutase activity; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd05801; PGM_like3; 1.
DR   InterPro; IPR005844; A-D-PHexomutase_a/b/a-I.
DR   InterPro; IPR016055; A-D-PHexomutase_a/b/a-I/II/III.
DR   InterPro; IPR005845; A-D-PHexomutase_a/b/a-II.
DR   InterPro; IPR005846; A-D-PHexomutase_a/b/a-III.
DR   InterPro; IPR005843; A-D-PHexomutase_C.
DR   InterPro; IPR036900; A-D-PHexomutase_C_sf.
DR   InterPro; IPR016066; A-D-PHexomutase_CS.
DR   InterPro; IPR005852; PGlcMutase_a-D-Glc-sp.
DR   Pfam; PF02878; PGM_PMM_I; 1.
DR   Pfam; PF02879; PGM_PMM_II; 1.
DR   Pfam; PF02880; PGM_PMM_III; 1.
DR   Pfam; PF00408; PGM_PMM_IV; 1.
DR   SUPFAM; SSF53738; SSF53738; 3.
DR   SUPFAM; SSF55957; SSF55957; 1.
DR   TIGRFAMs; TIGR01132; pgm; 1.
DR   PROSITE; PS00710; PGM_PMM; 1.
PE   3: Inferred from homology;
DR   PRODOM; B7UKX0.
DR   SWISS-2DPAGE; B7UKX0.
KW   Complete proteome {ECO:0000313|Proteomes:UP000008205};
KW   Isomerase {ECO:0000256|SAAS:SAAS01085081};
KW   Magnesium {ECO:0000256|RuleBase:RU004326,
KW   ECO:0000256|SAAS:SAAS00436074};
KW   Metal-binding {ECO:0000256|RuleBase:RU004326,
KW   ECO:0000256|SAAS:SAAS00436123}.
FT   DOMAIN       40    180       PGM_PMM_I. {ECO:0000259|Pfam:PF02878}.
FT   DOMAIN      210    317       PGM_PMM_II. {ECO:0000259|Pfam:PF02879}.
FT   DOMAIN      320    440       PGM_PMM_III. {ECO:0000259|Pfam:PF02880}.
FT   DOMAIN      489    538       PGM_PMM_IV. {ECO:0000259|Pfam:PF00408}.
SQ   SEQUENCE   546 AA;  58393 MW;  5B6EF02192937DF8 CRC64;
     MAIHNRAGQP AQQSDLINVA QLTAQYYVLK PEAGNAEHAV KFGTSGHRGS AARHSFNEPH
     ILAIAQAIAE ERAKNGITGP CYVGKDTHAL SEPAFISVLE VLAANGVDVI VQENNGFTPT
     PAISNAILVH NKKGGPLADG IVITPSHNPP EDGGIKYNPP NGGPADTNVT KVVEDKANAL
     MADGLKGVKR ISLDEAMASG HVKEQDLVQP FVEGLADIVD MAAIQKAGLT LGVDPLGGSG
     IEYWKRIGEY YNLNLTIVND QVDQTFRFMH LDKDGAIRMD CSSECAMAGL LALRDKFDLA
     FANDPDYDRH GIVTPAGLMN PNHYLAVAIN YLFQHRPQWG KDVAVGKTLV SSAMIDRVVN
     DLGRKLVEVP VGFKWFVDGL FDGSFGFGGE ESAGASFLRF DGTPWSTDKD GIIMCLLAAE
     ITAVTGKNPQ EHYNELAKRF GAPSYNRLQA AATSAQKAAL SKLSPEMVSA STLAGDPITA
     RLTVAPGNGA SIGGLKVMTD NGWFAARPSG TEDAYKIYCE SFLGEEHRKQ IEKEAVEIVS
     EVLKNA
//

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