(data stored in ACNUC29543 zone)

SWISSPROT: A5GQZ6_SYNR3

ID   A5GQZ6_SYNR3            Unreviewed;       553 AA.
AC   A5GQZ6;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   12-JUN-2007, sequence version 1.
DT   08-MAY-2019, entry version 74.
DE   SubName: Full=Phosphoglucomutase {ECO:0000313|EMBL:CAK27305.1};
DE            EC=5.4.2.2 {ECO:0000313|EMBL:CAK27305.1};
GN   Name=pmg {ECO:0000313|EMBL:CAK27305.1};
GN   OrderedLocusNames=SynRCC307_0402 {ECO:0000313|EMBL:CAK27305.1};
OS   Synechococcus sp. (strain RCC307).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=316278 {ECO:0000313|EMBL:CAK27305.1, ECO:0000313|Proteomes:UP000001115};
RN   [1] {ECO:0000313|Proteomes:UP000001115}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCC307 {ECO:0000313|Proteomes:UP000001115};
RG   Genoscope;
RL   Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
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; CT978603; CAK27305.1; -; Genomic_DNA.
DR   RefSeq; WP_011934820.1; NC_009482.1.
DR   STRING; 316278.SynRCC307_0402; -.
DR   EnsemblBacteria; CAK27305; CAK27305; SynRCC307_0402.
DR   KEGG; syr:SynRCC307_0402; -.
DR   eggNOG; ENOG4107REA; Bacteria.
DR   eggNOG; COG0033; LUCA.
DR   HOGENOM; HOG000009550; -.
DR   KO; K01835; -.
DR   OMA; DIYKIYA; -.
DR   OrthoDB; 637615at2; -.
DR   BioCyc; SSP316278:G1GJL-400-MONOMER; -.
DR   Proteomes; UP000001115; Chromosome.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0004614; F:phosphoglucomutase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
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; IPR005841; Alpha-D-phosphohexomutase_SF.
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   PRINTS; PR00509; PGMPMM.
DR   SUPFAM; SSF53738; SSF53738; 3.
DR   SUPFAM; SSF55957; SSF55957; 1.
DR   PROSITE; PS00710; PGM_PMM; 1.
PE   3: Inferred from homology;
DR   PRODOM; A5GQZ6.
DR   SWISS-2DPAGE; A5GQZ6.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001115};
KW   Isomerase {ECO:0000256|SAAS:SAAS01085081,
KW   ECO:0000313|EMBL:CAK27305.1};
KW   Magnesium {ECO:0000256|RuleBase:RU004326,
KW   ECO:0000256|SAAS:SAAS00436074};
KW   Metal-binding {ECO:0000256|RuleBase:RU004326,
KW   ECO:0000256|SAAS:SAAS00436123};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001115}.
FT   DOMAIN       24    161       PGM_PMM_I. {ECO:0000259|Pfam:PF02878}.
FT   DOMAIN      194    296       PGM_PMM_II. {ECO:0000259|Pfam:PF02879}.
FT   DOMAIN      304    417       PGM_PMM_III. {ECO:0000259|Pfam:PF02880}.
FT   DOMAIN      476    512       PGM_PMM_IV. {ECO:0000259|Pfam:PF00408}.
SQ   SEQUENCE   553 AA;  59055 MW;  D982FA1B4C87C831 CRC64;
     MTLSSPSTEF SVQQIKLPEA FQDQKPGTSG LRKSTQQFEQ PHYLESFIEA IFRTLPGVQG
     GTLVVGGDGR YGNRRAIDVI TRMAAAHGLG RIVLTTGGIL STPAASNLIR QRQAIGGIIL
     SASHNPGGPK GDFGVKVNGA NGGPAPESLT DAIYACSQQL DGYRIASGTA LPLDAPAEHQ
     IGALNVEVID GVDDYLQLMQ HLFDFDLISD LLKGSWPMAF DAMHAVTGPY ASKLFEQLLG
     APSGTVRNGR CLEDFGGGHP DPNLTYAKEL ATLLLDGDDY RFGAACDGDG DRNMILGQRC
     FVNPSDSLAV LTANATLVKG YASGLAGVAR SMPTSAAVDV VAKQLGINCF ETPTGWKFFG
     NLLDAGRITL CGEESFGTGS DHIREKDGLW AVLFWLSILA KRQCSVAEVM QQHWSTYGRH
     YYSRHDYEGV ETDRAHGLYN GLRDRLGELT GTSFADSRIA NADDFAYSDP VDGSLTQKQG
     LRLLLEDGSR IILRLSGTGT KGATLRLYLE RYVATGGNLD QNPQQALAGM IAAADALAGI
     RSTTGMDVPT VIT
//

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