ID Q9RZA7_DEIRA Unreviewed; 473 AA.
AC Q9RZA7;
DT 01-MAY-2000, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2000, sequence version 1.
DT 27-MAR-2024, entry version 141.
DE SubName: Full=Phospho-sugar mutase, putative {ECO:0000313|EMBL:AAF12264.1};
GN OrderedLocusNames=DR_A0047 {ECO:0000313|EMBL:AAF12264.1};
OS Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / CCUG
OS 27074 / LMG 4051 / NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1).
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=243230 {ECO:0000313|EMBL:AAF12264.1, ECO:0000313|Proteomes:UP000002524};
RN [1] {ECO:0000313|EMBL:AAF12264.1, ECO:0000313|Proteomes:UP000002524}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 /
RC NCIMB 9279 / R1 / VKM B-1422 {ECO:0000313|Proteomes:UP000002524};
RX PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA Vamathevan J.J., Lam P., McDonald L., Utterback T., Zalewski C.,
RA Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA Ketchum K.A., Nelson K.E., Salzberg S., Smith H.O., Venter J.C.,
RA Fraser C.M.;
RT "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT R1.";
RL Science 286:1571-1577(1999).
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; AE001825; AAF12264.1; -; Genomic_DNA.
DR PIR; A75598; A75598.
DR RefSeq; NP_285371.1; NC_001264.1.
DR RefSeq; WP_010889307.1; NZ_JMLF01000008.1.
DR AlphaFoldDB; Q9RZA7; -.
DR STRING; 243230.DR_A0047; -.
DR PaxDb; 243230-DR_A0047; -.
DR EnsemblBacteria; AAF12264; AAF12264; DR_A0047.
DR GeneID; 69518939; -.
DR KEGG; dra:DR_A0047; -.
DR PATRIC; fig|243230.17.peg.2931; -.
DR eggNOG; COG1109; Bacteria.
DR HOGENOM; CLU_016950_7_1_0; -.
DR InParanoid; Q9RZA7; -.
DR OrthoDB; 9806956at2; -.
DR Proteomes; UP000002524; Chromosome II.
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; cd05800; PGM_like2; 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; 2.
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:UP000002524}.
FT DOMAIN 3..137
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 152..254
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 260..372
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 412..464
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 473 AA; 51073 MW; C3D8DAC43818BEB1 CRC64;
MPIKFGTDGW RDIIAEDFTF ENVRTVARAH AQVLRSSGAR SVAVGFDTRF QGQAFARVVA
EVMAAQGLDV WLAQDYLPTP ALSFAVVHHG AGGGVMITAS HNPPQYSGYK IKGSYGGSAT
PAVVAQVEAA LATAESYDGP RGEIRPLDIR QAYYEQLDRQ LDLETLREYR GKVIHDPMGG
AACGWLTGYA QHAGLQLELE EMHGRPDPLF YGVNPEPIPQ NLGELTERLT RESAPTLGVI
TDGDADRVGA ITAGGHFFNS HQIFAVLIKH LYGRGVRGRV VKTVSGSRVI ELLAETLGLE
LLETPVGFKY ITDAFLEGQQ DESKAVLMGG EESGGLSSRG HIPERDGLLN SLLMIEAVAA
SGQSLDELFA EIEREVGFRH VYDRADLHLS EAFDKSALMQ AAQGYREVAG QAVTGIKTTD
GVKLALAGDA SVMFRASGTE PVVRVYVEAQ TPEMVQAVLT EAVQRVRSFD PMS
//