ID A0A5C6MDU3_9PLAN Unreviewed; 449 AA.
AC A0A5C6MDU3;
DT 13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2019, sequence version 1.
DT 02-APR-2025, entry version 17.
DE SubName: Full=Phosphoglucosamine mutase {ECO:0000313|EMBL:TWW12378.1};
GN ORFNames=E3A20_01700 {ECO:0000313|EMBL:TWW12378.1};
OS Planctomyces bekefii.
OC Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
OC Planctomycetales; Planctomycetaceae; Planctomyces.
OX NCBI_TaxID=1653850 {ECO:0000313|EMBL:TWW12378.1, ECO:0000313|Proteomes:UP000321083};
RN [1] {ECO:0000313|EMBL:TWW12378.1, ECO:0000313|Proteomes:UP000321083}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Phe10_nw2017 {ECO:0000313|EMBL:TWW12378.1};
RA Svetlana D.N., Overmann J.;
RT "100 year-old enigma solved: identification of Planctomyces bekefii, the
RT type genus and species of the phylum Planctomycetes.";
RL Submitted (AUG-2019) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:TWW12378.1, ECO:0000313|Proteomes:UP000321083}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Phe10_nw2017 {ECO:0000313|EMBL:TWW12378.1};
RA Henke P.;
RL Submitted (AUG-2019) 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}.
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:TWW12378.1}.
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DR EMBL; SRHE01000015; TWW12378.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5C6MDU3; -.
DR Proteomes; UP000321083; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008966; F:phosphoglucosamine mutase activity; IEA:InterPro.
DR GO; GO:0004615; F:phosphomannomutase activity; IEA:TreeGrafter.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:TreeGrafter.
DR GO; GO:0006048; P:UDP-N-acetylglucosamine biosynthetic process; IEA:TreeGrafter.
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; IPR005841; Alpha-D-phosphohexomutase_SF.
DR InterPro; IPR024086; GlmM_arc-type.
DR InterPro; IPR050060; Phosphoglucosamine_mutase.
DR NCBIfam; TIGR03990; Arch_GlmM; 1.
DR PANTHER; PTHR42946:SF1; PHOSPHOGLUCOMUTASE (ALPHA-D-GLUCOSE-1,6-BISPHOSPHATE-DEPENDENT); 1.
DR PANTHER; PTHR42946; PHOSPHOHEXOSE MUTASE; 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.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000321083}.
FT DOMAIN 9..131
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 154..252
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 260..362
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 373..437
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 449 AA; 47819 MW; BC3AF22497B11AB5 CRC64;
MATRILSISG LRGVIGDGLD PVYTSRFAAA LGTMFCGGKV VLARDGRSTG PMLHHAVVSG
LLATGCDVLD AGVCTTPTCG VLVQHHKAAG GLQITTSHNP IEWNGLKPFA PDGSVFNRDL
GQQLLQILEQ DSIAWRNWSG LGSVVTLQNP AQVHIDKVLS LVNAETIRQR RFKVVLDCNH
GSGAVGGPQL LQALGCEVVV LGGTPDGRFE HIPEPVEKNL GDLCQAVVKH SADAGFAQDP
DADRLAIVDE TGRYIGEELT LALAADFVLE KLKGPFVVNG STSRVTADIA AKHGCQFHRS
YVGEAHVCAK MRSVQAVLGG EGNGGVIEPR IGYVRDSLVS MAYVLAGLAA GKRRLSQWAD
SLPFYTIVKD RIECPASKTE VACAALRNAF PDAEAREGDG LRLDWNDRWV QVRASNTEPI
IRIIAEAPET AAAVSLIDRA MQVVRKAVS
//
