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Database: UniProt
Entry: Q2N656_ERYLH
LinkDB: Q2N656_ERYLH
Original site: Q2N656_ERYLH 
ID   Q2N656_ERYLH            Unreviewed;       469 AA.
AC   Q2N656;
DT   07-FEB-2006, integrated into UniProtKB/TrEMBL.
DT   07-FEB-2006, sequence version 1.
DT   27-MAR-2024, entry version 99.
DE   SubName: Full=Phosphoglucomutase {ECO:0000313|EMBL:ABC64835.1};
GN   OrderedLocusNames=ELI_13715 {ECO:0000313|EMBL:ABC64835.1};
OS   Erythrobacter litoralis (strain HTCC2594).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Erythrobacter.
OX   NCBI_TaxID=314225 {ECO:0000313|EMBL:ABC64835.1, ECO:0000313|Proteomes:UP000008808};
RN   [1] {ECO:0000313|Proteomes:UP000008808}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTCC2594 {ECO:0000313|Proteomes:UP000008808};
RX   PubMed=19168610; DOI=10.1128/JB.00026-09;
RA   Oh H.M., Giovannoni S.J., Ferriera S., Johnson J., Cho J.C.;
RT   "Complete genome sequence of Erythrobacter litoralis HTCC2594.";
RL   J. Bacteriol. 191:2419-2420(2009).
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}.
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DR   EMBL; CP000157; ABC64835.1; -; Genomic_DNA.
DR   RefSeq; WP_011415657.1; NC_007722.1.
DR   AlphaFoldDB; Q2N656; -.
DR   STRING; 314225.ELI_13715; -.
DR   KEGG; eli:ELI_13715; -.
DR   eggNOG; COG1109; Bacteria.
DR   HOGENOM; CLU_016950_9_1_5; -.
DR   OrthoDB; 9803322at2; -.
DR   Proteomes; UP000008808; Chromosome.
DR   GO; GO:0016868; F:intramolecular phosphotransferase activity; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd03089; PMM_PGM; 1.
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; 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   PANTHER; PTHR43771:SF2; PHOSPHOGLUCOMUTASE; 1.
DR   PANTHER; PTHR43771; PHOSPHOMANNOMUTASE; 1.
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; 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   Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|RuleBase:RU004326};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU004326};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008808}.
FT   DOMAIN          10..122
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          155..257
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          261..370
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          377..456
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   469 AA;  50163 MW;  584F9F61524076BF CRC64;
     MSHTFDPTIL REYDIRGVIG ETLEADDARA IGRSFGSMLR RAGGSTVAVG YDGRVSSPML
     EHALVEGLAA SGCNVVRIGM GATPMLYFAE ASSEQVDGGI QITGSHNPPN YNGFKMVFQG
     RPFFGRDIQD LGAVSAAGDW MDGTGSIADL DILDTYVTRM LAALDGIDGE ALAGMKIGWD
     AGNGAAGPAL EKLVARLPGE HHLLFTEVDG HFPNHHPDPT VEANLADLKA LVAGKNLDFG
     VAFDGDGDRI GAIDGEGRVI WGDQLLMIYA EDLLGRLPNA TIIADVKASR ALFDHVEKHG
     GSPVMWKTGH SLIKSKMKET GSPLAGEMSG HVFFADTYYG FDDALYAGLR LMAASARLGK
     SVTQLRSDMP QMINTPEMRF QVDESRKFAA IDEVKQRLGS GADGVEVNDT DGVRVTTPDG
     WWLLRASNTQ DVLVARAEGD SEKAVERLMA QIDEQLALSG LERGESAGH
//
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