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Database: UniProt
Entry: Q8EG54_SHEON
LinkDB: Q8EG54_SHEON
Original site: Q8EG54_SHEON 
ID   Q8EG54_SHEON            Unreviewed;       573 AA.
AC   Q8EG54;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2003, sequence version 1.
DT   27-MAR-2024, entry version 123.
DE   SubName: Full=Phosphoglucomutase/phosphomannomutase family protein {ECO:0000313|EMBL:AAN54809.1};
GN   OrderedLocusNames=SO_1755 {ECO:0000313|EMBL:AAN54809.1};
OS   Shewanella oneidensis (strain MR-1).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=211586 {ECO:0000313|EMBL:AAN54809.1, ECO:0000313|Proteomes:UP000008186};
RN   [1] {ECO:0000313|EMBL:AAN54809.1, ECO:0000313|Proteomes:UP000008186}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MR-1 {ECO:0000313|EMBL:AAN54809.1,
RC   ECO:0000313|Proteomes:UP000008186};
RX   PubMed=12368813; DOI=10.1038/nbt749;
RA   Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C.,
RA   Read T.D., Eisen J.A., Seshadri R., Ward N., Methe B., Clayton R.A.,
RA   Meyer T., Tsapin A., Scott J., Beanan M., Brinkac L., Daugherty S.,
RA   DeBoy R.T., Dodson R.J., Durkin A.S., Haft D.H., Kolonay J.F., Madupu R.,
RA   Peterson J.D., Umayam L.A., White O., Wolf A.M., Vamathevan J., Weidman J.,
RA   Impraim M., Lee K., Berry K., Lee C., Mueller J., Khouri H., Gill J.,
RA   Utterback T.R., McDonald L.A., Feldblyum T.V., Smith H.O., Venter J.C.,
RA   Nealson K.H., Fraser C.M.;
RT   "Genome sequence of the dissimilatory metal ion-reducing bacterium
RT   Shewanella oneidensis.";
RL   Nat. Biotechnol. 20:1118-1123(2002).
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; AE014299; AAN54809.1; -; Genomic_DNA.
DR   RefSeq; NP_717365.1; NC_004347.2.
DR   RefSeq; WP_011071884.1; NZ_CP053946.1.
DR   AlphaFoldDB; Q8EG54; -.
DR   STRING; 211586.SO_1755; -.
DR   PaxDb; 211586-SO_1755; -.
DR   KEGG; son:SO_1755; -.
DR   PATRIC; fig|211586.12.peg.1686; -.
DR   eggNOG; COG1109; Bacteria.
DR   HOGENOM; CLU_016950_0_2_6; -.
DR   OrthoDB; 9803322at2; -.
DR   PhylomeDB; Q8EG54; -.
DR   BioCyc; SONE211586:G1GMP-1607-MONOMER; -.
DR   Proteomes; UP000008186; Chromosome.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0008973; F:phosphopentomutase activity; IBA:GO_Central.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0006166; P:purine ribonucleoside salvage; IBA:GO_Central.
DR   CDD; cd05799; PGM2; 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; PTHR45745:SF1; PHOSPHOGLUCOMUTASE 2A-RELATED; 1.
DR   PANTHER; PTHR45745; PHOSPHOMANNOMUTASE 45A; 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:UP000008186}.
FT   DOMAIN          45..184
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          219..317
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          326..443
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          498..542
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   573 AA;  62212 MW;  4509E15A4996A9B7 CRC64;
     MNTHLQLQIQ HWLKNDPDPS TQAQLQALID SGNEAELAAR FAGRLEFGTA GLRGVVGAGP
     MGMNRLVIRQ TSAGLGAYLL EQIHDVAERG VVIGYDGRHD SYTFAHDTAS VLTAMGIKVR
     LTAKVAPTPL VAFGVKHFNA AAGIVVTASH NPPQYNGYKV YWENGAQIIP PHDSGIAAKI
     EQAATQAIPF MELDDAIKQG KLIWLNDDYY ETYRRGVMHA KVLQNHTAPE KVSLAYTAMH
     GVGADMAETV LKDAGFTQVY SVAAQREPDG DFPTVNFPNP EEKGAMDLVI AEAKKHSAML
     ACANDPDADR FAVAVRKDDG EYQMLTGDQV GVLFGHYLLS HASADQRLVG TTIVSSSLLS
     KIANGFGVES YTTLTGFKWL MNVGIAQSQP DNQFLFAYEE ALGYTVGNMV WDKDGLSALV
     AFAQLTAELA AKGQTIWDRL EQIYREQGFH LNAQASIALK PETPNIGAYL REHPPLTIGE
     HAVVSTDDLK ALSRRFADGK VENINLPASD VLTYRLSNGA RVIVRPSGTE PKIKCYYEVV
     EPMTAQDTLA TAQARATQAM EAFISAHQAS LPK
//
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