ID A0A0F0FTT3_9BURK Unreviewed; 461 AA.
AC A0A0F0FTT3;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Phosphoglucomutase {ECO:0000313|EMBL:KJK25742.1};
DE EC=5.4.2.2 {ECO:0000313|EMBL:KJK25742.1};
DE EC=5.4.2.8 {ECO:0000313|EMBL:KJK25742.1};
GN ORFNames=UB46_03570 {ECO:0000313|EMBL:KJK25742.1};
OS Burkholderiaceae bacterium 16.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae.
OX NCBI_TaxID=1619952 {ECO:0000313|EMBL:KJK25742.1, ECO:0000313|Proteomes:UP000033515};
RN [1] {ECO:0000313|EMBL:KJK25742.1, ECO:0000313|Proteomes:UP000033515}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=16 {ECO:0000313|EMBL:KJK25742.1,
RC ECO:0000313|Proteomes:UP000033515};
RA Roco C.A., Bergaust L., Bakken L., Yavitt J., Shapleigh J.P.;
RT "The modularity of denitrifying soil bacteria: using gas kinetics and
RT genome sequencing to connect denitrifier phenotype to genotype.";
RL Submitted (FEB-2015) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KJK25742.1}.
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DR EMBL; JYOD01000008; KJK25742.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F0FTT3; -.
DR STRING; 1619952.UB46_03570; -.
DR PATRIC; fig|1619952.3.peg.8144; -.
DR Proteomes; UP000033515; Unassembled WGS sequence.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004614; F:phosphoglucomutase activity; IEA:UniProtKB-EC.
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:KJK25742.1};
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 372..450
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 461 AA; 49820 MW; D81C97AEE1D45AA9 CRC64;
MQIDPSIFKA YDIRGIVGKT LTRDVARAIG LSFGSAAAEQ GERAVVVGRD GRLSGPDLLG
GLVEGLRAAG MDVIDLGMVA TPMVYFGTNV DLAGLRATSG IMVTGSHNPP DYNGFKMVLA
GKAIYGEQIQ ALRQRIEAGQ FASGAGGYQQ VDIRQPYLDR IVGDVKLARP MKIALDAGNG
VAGAFVGDLF RALGCEVTEL FCEVDGNFPN HHPDPAHVEN LQDLMRCLKD TDCELGLAFD
GDGDRLGVVT KDGQVIFPDR QLMLFAEEIL SRNPGQQIIY DVKCTGKLAP WIRQHGGEPL
MWKTGHSLVK AKLKETGAPL AGEMSGHVFF KDRWYGFDDG LYTGARLLEI LSKHADPSAV
LNALPNSNCT PELQLKCAEG EAFTLLDKIR ANAKFDGARE VITIDGVRVE YADGFGLARP
SNTTPVVVMR FEADNDAALA RIQAEFKRVI LAEKPDAQLP F
//
