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Database: UniProt
Entry: A0A1D9GVG4_9BURK
LinkDB: A0A1D9GVG4_9BURK
Original site: A0A1D9GVG4_9BURK 
ID   A0A1D9GVG4_9BURK        Unreviewed;       461 AA.
AC   A0A1D9GVG4;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Phosphomannomutase/phosphoglucomutase {ECO:0000313|EMBL:AOY91544.1};
GN   ORFNames=BKK79_06730 {ECO:0000313|EMBL:AOY91544.1};
OS   Cupriavidus sp. USMAA2-4.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=876364 {ECO:0000313|EMBL:AOY91544.1, ECO:0000313|Proteomes:UP000178101};
RN   [1] {ECO:0000313|EMBL:AOY91544.1, ECO:0000313|Proteomes:UP000178101}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=USMAA2-4 {ECO:0000313|EMBL:AOY91544.1,
RC   ECO:0000313|Proteomes:UP000178101};
RA   Abdullah A.A.-A., Shafie N.A.H., Lau N.S.;
RT   "Complete genome sequences of three Cupriavidus strains isolated from
RT   various Malaysian environments.";
RL   Submitted (OCT-2016) 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; CP017748; AOY91544.1; -; Genomic_DNA.
DR   RefSeq; WP_071037406.1; NZ_CP017748.1.
DR   AlphaFoldDB; A0A1D9GVG4; -.
DR   STRING; 876364.BKK79_06730; -.
DR   KEGG; cuu:BKK79_06730; -.
DR   Proteomes; UP000178101; Chromosome 1.
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:UP000178101}.
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          372..450
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   461 AA;  49989 MW;  E1DF8E2E688181A2 CRC64;
     MQLDPTIFKA YDIRGIVGKT LTREVARAVG LAFGSTAVEK GERAVVVGRD GRLSGPDLLG
     GLVEGLRAAG LDVIDLGMVA TPMVYFGTYV ELDGQRATSG IMVTGSHNPP DYNGLKMVLA
     GEAIYGDAIQ GLRQRIEAGT FTSGAGGYRQ LDIRRQYIDR ILADVKLARP MKIALDAGNG
     VAGAFVGELF RGLGCEVTEL FCEVDGSFPN HHPDPAHVEN LQDLMRSLRE TDCELGLAFD
     GDGDRLGVVT KDGQVIFPDR QLMLFAEEIL ARNPGQQVIY DVKCTGKLAP WIRQHGGEPL
     MWKTGHSLIK AKLRETGAPI AGEMSGHVFF KDRWYGFDDG LYTGARLLEI LSRHADPSAV
     LNALPNSNST PELQLKCAEG EPFALLDKIR ANATFEGARE VNKIDGVRVE YADGFGLARP
     SNTTPVVVMR FEADNDAALA RIQAQFKRAI LAEKPDAQLS F
//
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