ID A0A643FDT9_IDEDE Unreviewed; 447 AA.
AC A0A643FDT9;
DT 22-APR-2020, integrated into UniProtKB/TrEMBL.
DT 22-APR-2020, sequence version 1.
DT 08-OCT-2025, entry version 21.
DE RecName: Full=Phosphoglucosamine mutase {ECO:0000256|ARBA:ARBA00068193, ECO:0000256|HAMAP-Rule:MF_01554};
DE EC=5.4.2.10 {ECO:0000256|ARBA:ARBA00066330, ECO:0000256|HAMAP-Rule:MF_01554};
GN Name=glmM {ECO:0000256|HAMAP-Rule:MF_01554,
GN ECO:0000313|EMBL:KAB0583500.1};
GN ORFNames=F7Q92_07420 {ECO:0000313|EMBL:KAB0583500.1};
OS Ideonella dechloratans.
OC Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
OC Burkholderiales; Sphaerotilaceae; Ideonella.
OX NCBI_TaxID=36863 {ECO:0000313|EMBL:KAB0583500.1, ECO:0000313|Proteomes:UP000430120};
RN [1] {ECO:0000313|EMBL:KAB0583500.1, ECO:0000313|Proteomes:UP000430120}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG 30977 {ECO:0000313|EMBL:KAB0583500.1,
RC ECO:0000313|Proteomes:UP000430120};
RA Tunovic T., Pineiro-Iglesias B., Unosson C., Inganas E., Ohlen M.,
RA Cardew S., Jensie-Markopoulos S., Salva-Serra F., Jaen-Luchoro D.,
RA Karlsson R., Svensson-Stadler L., Chun J., Moore E.;
RT "Draft genome sequences of 48 bacterial type strains from the CCUG.";
RL Submitted (SEP-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the conversion of glucosamine-6-phosphate to
CC glucosamine-1-phosphate. {ECO:0000256|HAMAP-Rule:MF_01554}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-glucosamine 1-phosphate = D-glucosamine 6-phosphate;
CC Xref=Rhea:RHEA:23424, ChEBI:CHEBI:58516, ChEBI:CHEBI:58725;
CC EC=5.4.2.10; Evidence={ECO:0000256|HAMAP-Rule:MF_01554};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01554};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01554};
CC -!- PTM: Activated by phosphorylation. {ECO:0000256|HAMAP-Rule:MF_01554}.
CC -!- SIMILARITY: Belongs to the phosphohexose mutase family.
CC {ECO:0000256|ARBA:ARBA00010231, ECO:0000256|HAMAP-Rule:MF_01554}.
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:KAB0583500.1}.
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DR EMBL; VZPB01000013; KAB0583500.1; -; Genomic_DNA.
DR RefSeq; WP_151123545.1; NZ_CP088081.1.
DR AlphaFoldDB; A0A643FDT9; -.
DR OrthoDB; 9803322at2; -.
DR Proteomes; UP000430120; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008966; F:phosphoglucosamine mutase activity; IEA:UniProtKB-UniRule.
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:UniProtKB-ARBA.
DR GO; GO:0006048; P:UDP-N-acetylglucosamine biosynthetic process; IEA:TreeGrafter.
DR CDD; cd05802; GlmM; 1.
DR FunFam; 3.30.310.50:FF:000001; Phosphoglucosamine mutase; 1.
DR FunFam; 3.40.120.10:FF:000001; Phosphoglucosamine mutase; 1.
DR FunFam; 3.40.120.10:FF:000002; Phosphoglucosamine mutase; 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 HAMAP; MF_01554_B; GlmM_B; 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; IPR006352; GlmM_bact.
DR InterPro; IPR050060; Phosphoglucosamine_mutase.
DR NCBIfam; TIGR01455; glmM; 1.
DR NCBIfam; NF008139; PRK10887.1; 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, ECO:0000256|HAMAP-Rule:MF_01554};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01554};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01554};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|HAMAP-
KW Rule:MF_01554}; Reference proteome {ECO:0000313|Proteomes:UP000430120}.
FT DOMAIN 3..137
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 159..256
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 260..367
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 375..441
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
FT ACT_SITE 104
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01554"
FT BINDING 104
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /note="via phosphate group"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01554"
FT BINDING 243
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01554"
FT BINDING 245
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01554"
FT BINDING 247
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01554"
FT MOD_RES 104
FT /note="Phosphoserine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01554"
SQ SEQUENCE 447 AA; 47719 MW; 97854DC5B0527F33 CRC64;
MARQYFGTDG IRGTVGQFPI TPDFALRLGH AVGQVLQRTA KGRRPTVLIG KDTRISGYML
ESALEAGFAS AGVNVLLTGP LPTPGVAYLT RALRLDLGVV ISASHNAFPD NGIKFFSAKG
EKLPDAWEES VEQALEEPPA WVDSARLGRA RRLDDAQGRY VEFCKSTVSG ELNLKGLKFV
IDAAHGAAYQ VAPAVFHELG GEVTSIGVTP NGMNINAGVG ATSPAALVAA VKEQGANYGI
ALDGDADRLQ LVDNEGRLFN GDELLYVMAM DRKAQGEAVP GVVGTLMTNM AVEVALAEQG
IELVRAKVGD RYVLEELAAR HWLLGGESSG HLLALDRHST GDGIVSALQV LQATQRSGRG
LRALLEGVTL YPQVMINVRL KEGEDWRQNA RLSELTRQVT AELGRLGRVL IRASGTEPVL
RVMVEAREES QARHAAETLA AAARGEC
//
