ID A0A7W7VKP6_9ACTN Unreviewed; 451 AA.
AC A0A7W7VKP6;
DT 02-JUN-2021, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 1.
DT 28-JAN-2026, entry version 19.
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 ORFNames=FHS44_000989 {ECO:0000313|EMBL:MBB4913917.1};
OS Streptosporangium saharense.
OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Streptosporangiaceae; Streptosporangium.
OX NCBI_TaxID=1706840 {ECO:0000313|EMBL:MBB4913917.1, ECO:0000313|Proteomes:UP000552644};
RN [1] {ECO:0000313|EMBL:MBB4913917.1, ECO:0000313|Proteomes:UP000552644}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 8840 {ECO:0000313|EMBL:MBB4913917.1,
RC ECO:0000313|Proteomes:UP000552644};
RA Whitman W.;
RT "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT soil and plant-associated and newly described type strains.";
RL Submitted (AUG-2020) 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 ECO:0000256|RuleBase:RU004327}.
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|ARBA:ARBA00050364,
CC ECO:0000256|HAMAP-Rule:MF_01554, ECO:0000256|RuleBase:RU004327};
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 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:MBB4913917.1}.
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DR EMBL; JACHJP010000001; MBB4913917.1; -; Genomic_DNA.
DR RefSeq; WP_184712631.1; NZ_JACHJP010000001.1.
DR AlphaFoldDB; A0A7W7VKP6; -.
DR Proteomes; UP000552644; 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:TreeGrafter.
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; IPR016066; A-D-PHexomutase_CS.
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.
DR PROSITE; PS00710; PGM_PMM; 1.
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:UP000552644}.
FT DOMAIN 3..140
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 163..259
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 263..373
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 380..444
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
FT ACT_SITE 109
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01554"
FT BINDING 109
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 246
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01554"
FT BINDING 248
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01554"
FT BINDING 250
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01554"
FT MOD_RES 109
FT /note="Phosphoserine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01554"
SQ SEQUENCE 451 AA; 46823 MW; BCC6F302AA52FC46 CRC64;
MGRLFGTDGV RGVAGRDLTA EFAMDLSVAA AHALGDAGAF NASVGRRGRP VAVVGRDPRA
SGEFLEAAVV AGLASSGVDV LRLGVLPTPA VAYLTTALGA DMGVMISASH NPAPDNGIKF
LTRGGYKLPD TVENEIEERL GEKWDRPVGA EVGRVREAYG EADRYVSHLL STVSGRLDGL
NVVLDCAHGA AHVVAPEALR RAGATVETIG TRPDGLNINA GCGSTHLDKL QQVVVSRGAD
LGIAYDGDAD RCLAVSHTGE VVDGDQIMAI LATSMHAEGK LVGDTVVATV MSNLGFKIAM
RNAGIDVIET AVGDRYVLEA MRAGGYNLGG EQSGHVLLLD HATTGDGLLT SLHLLSVVAR
EGRPLAELAS VMTRLPQILV NVKDVDRAKA SVPELSAAVA AVELELGETG RVLIRPSGTE
PMIRVMVEAS SAEQAERMAG HLAEVVRTAC V
//
