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Database: UniProt
Entry: A0A0W7WKY7_9RHOB
LinkDB: A0A0W7WKY7_9RHOB
Original site: A0A0W7WKY7_9RHOB 
ID   A0A0W7WKY7_9RHOB        Unreviewed;       543 AA.
AC   A0A0W7WKY7;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=phosphoglucomutase (alpha-D-glucose-1,6-bisphosphate-dependent) {ECO:0000256|ARBA:ARBA00012728};
DE            EC=5.4.2.2 {ECO:0000256|ARBA:ARBA00012728};
GN   ORFNames=AVJ23_09565 {ECO:0000313|EMBL:KUF11280.1};
OS   Pseudoponticoccus marisrubri.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Pseudoponticoccus.
OX   NCBI_TaxID=1685382 {ECO:0000313|EMBL:KUF11280.1, ECO:0000313|Proteomes:UP000054396};
RN   [1] {ECO:0000313|EMBL:KUF11280.1, ECO:0000313|Proteomes:UP000054396}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SJ5A-1 {ECO:0000313|EMBL:KUF11280.1,
RC   ECO:0000313|Proteomes:UP000054396};
RA   Shamseldin A., Moawad H., Abd El-Rahim W.M., Sadowsky M.J.;
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate;
CC         Xref=Rhea:RHEA:23536, ChEBI:CHEBI:58225, ChEBI:CHEBI:58601;
CC         EC=5.4.2.2; Evidence={ECO:0000256|ARBA:ARBA00000443};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SIMILARITY: Belongs to the phosphohexose mutase family.
CC       {ECO:0000256|ARBA:ARBA00010231, ECO:0000256|RuleBase:RU004326}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KUF11280.1}.
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DR   EMBL; LPXO01000004; KUF11280.1; -; Genomic_DNA.
DR   RefSeq; WP_058861944.1; NZ_LPXO01000004.1.
DR   AlphaFoldDB; A0A0W7WKY7; -.
DR   STRING; 1685382.AVJ23_09565; -.
DR   OrthoDB; 9806956at2; -.
DR   Proteomes; UP000054396; Unassembled WGS sequence.
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   Gene3D; 3.40.120.10; Alpha-D-Glucose-1,6-Bisphosphate, subunit A, domain 3; 3.
DR   Gene3D; 3.30.310.50; Alpha-D-phosphohexomutase, C-terminal domain; 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; IPR036900; A-D-PHexomutase_C_sf.
DR   InterPro; IPR016066; A-D-PHexomutase_CS.
DR   InterPro; IPR005841; Alpha-D-phosphohexomutase_SF.
DR   InterPro; IPR045244; PGM.
DR   PANTHER; PTHR22573:SF2; PHOSPHOGLUCOMUTASE; 1.
DR   PANTHER; PTHR22573; PHOSPHOHEXOMUTASE FAMILY MEMBER; 1.
DR   Pfam; PF02878; PGM_PMM_I; 1.
DR   Pfam; PF02879; PGM_PMM_II; 1.
DR   Pfam; PF02880; PGM_PMM_III; 1.
DR   PRINTS; PR00509; PGMPMM.
DR   SUPFAM; SSF55957; Phosphoglucomutase, C-terminal domain; 1.
DR   SUPFAM; SSF53738; Phosphoglucomutase, first 3 domains; 3.
DR   PROSITE; PS00710; PGM_PMM; 1.
PE   3: Inferred from homology;
KW   Magnesium {ECO:0000256|RuleBase:RU004326};
KW   Metal-binding {ECO:0000256|RuleBase:RU004326};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054396}.
FT   DOMAIN          14..153
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          185..286
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          310..407
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..15
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   543 AA;  57912 MW;  FD8EAE4627B7DA8C CRC64;
     MTPKAVSTQP IDGQKPGTSG LRKKTRVFME PNYLENYVQS IFDGIGGVRG KRLVVGGDGR
     YFNAEAIQTI LQMAAANGAA HCWVGQGGIL STPAASHLIR SLEADGGLIL SASHNPGGID
     EDFGLKYNGP NGGPASETVT ARIFARTREI DSYHVVEAEP VDLSALGRQE LAGMTVEIVD
     PVADYAALME TLFDFDALRG LFAGGFRMRF DAMHAVTGPY ATEILENRLG APEGTVMNGT
     PLPDFGRGHP DPNPIWARDL MNCMYGSGAP DFGAASDGDG DRNMIVGRKC YVSPSDSLAV
     LTDLAHLAPG YADGLAGVAR SMPTSTAVDR VAKAKGFACF ETPTGWKFFG NLLDNGDVTL
     CGEESAGTGS NHVREKDGLW AVLLWLNILA ATGKSVAELM RDHWQRYGRN YYSRHDYEAV
     DSEAAHALMD DLRGRLAELP GKSFGPLTVS EADEFAYDDP VDGSRAEGQG LRIHFTSGGR
     VVFRLSGTGT QGATLRVYLE QLETAPDVLD QDPQAALSDM IAAADEIAGI SRRTGRSGPD
     VVT
//
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