ID   Q474Q8_CUPPJ            Unreviewed;       461 AA.
AC   Q474Q8;
DT   13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2005, sequence version 1.
DT   27-MAR-2024, entry version 108.
DE   SubName: Full=Phosphomannomutase {ECO:0000313|EMBL:AAZ60125.1};
DE            EC=5.4.2.8 {ECO:0000313|EMBL:AAZ60125.1};
GN   OrderedLocusNames=Reut_A0745 {ECO:0000313|EMBL:AAZ60125.1};
OS   Cupriavidus pinatubonensis (strain JMP 134 / LMG 1197) (Cupriavidus necator
OS   (strain JMP 134)).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=264198 {ECO:0000313|EMBL:AAZ60125.1};
RN   [1] {ECO:0000313|EMBL:AAZ60125.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=JMP134 {ECO:0000313|EMBL:AAZ60125.1};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Goltsman E., Martinez M., Schmutz J.,
RA   Larimer F., Land M., Lykidis A., Richardson P.;
RT   "Complete sequence of Chromosome1 of Ralstonia eutropha JMP134.";
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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; CP000090; AAZ60125.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q474Q8; -.
DR   STRING; 264198.Reut_A0745; -.
DR   KEGG; reu:Reut_A0745; -.
DR   eggNOG; COG1109; Bacteria.
DR   HOGENOM; CLU_016950_9_1_4; -.
DR   OrthoDB; 9803322at2; -.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0004615; F:phosphomannomutase activity; IEA:UniProtKB-EC.
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, ECO:0000313|EMBL:AAZ60125.1};
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}.
FT   DOMAIN          7..141
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          156..253
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          258..364
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          374..450
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   461 AA;  49887 MW;  1EA8A462017B28B0 CRC64;
     MQIDPSIFKA YDIRGIVGKT LTRDVARLIG LSFGSAAAEA GEKAVVVGRD GRLSGPDLIG
     GLVDGLRATG MDVIDLGMVA TPMVYFGTNI ELDGVKATSG IMVTGSHNPP DYNGFKMVLA
     GKAIYGEQIQ GLRQRIEAGN FANGAGAYRQ CDVRQQYLDR ITSDVKLARP MKIALDAGNG
     VAGAFVGDLF RGLGCEVTEL FCDVDGNFPN HHPDPAHVEN LQDLMKCLHE TDCELGLAFD
     GDGDRLGVVT KDGQVIFPDR QLMLFAEEIL ARNPGAQVIY DVKCTGKLAP WIRAHGGEPL
     MWKTGHSLVK AKLKETGAPI AGEMSGHVFF KDRWYGFDDG LYTGARLLEI LSRHTDPSAV
     LNALPNANNT PELQLKCVEG EPFTLLDKIK ANARFEGARE VITIDGVRVE YPDGFGLARP
     SNTTPVVVMR FEADNDAALA RIQAEFKRVI LAEKPDAKLP F
//