ID A0A917FYC0_9NOCA Unreviewed; 443 AA.
AC A0A917FYC0;
DT 22-FEB-2023, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2023, sequence version 1.
DT 28-JAN-2026, entry version 15.
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:GGG14007.1};
GN ORFNames=GCM10007304_30090 {ECO:0000313|EMBL:GGG14007.1};
OS Rhodococcoides trifolii.
OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Nocardiaceae; Rhodococcoides.
OX NCBI_TaxID=908250 {ECO:0000313|EMBL:GGG14007.1, ECO:0000313|Proteomes:UP000654257};
RN [1] {ECO:0000313|EMBL:GGG14007.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CCM 7905 {ECO:0000313|EMBL:GGG14007.1};
RX PubMed=25193709;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Walter F., Albersmeier A., Kalinowski J., Ruckert C.;
RT "Complete genome sequence of Corynebacterium casei LMG S-19264T (=DSM
RT 44701T), isolated from a smear-ripened cheese.";
RL Int. J. Syst. Evol. Microbiol. 189:76-77(2014).
RN [2] {ECO:0000313|EMBL:GGG14007.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CCM 7905 {ECO:0000313|EMBL:GGG14007.1};
RA Sun Q., Sedlacek I.;
RL Submitted (SEP-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 -!- 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};
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:GGG14007.1}.
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DR EMBL; BMCU01000003; GGG14007.1; -; Genomic_DNA.
DR RefSeq; WP_188545662.1; NZ_BMCU01000003.1.
DR AlphaFoldDB; A0A917FYC0; -.
DR Proteomes; UP000654257; 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; IPR005841; Alpha-D-phosphohexomutase_SF.
DR InterPro; IPR006352; GlmM_bact.
DR InterPro; IPR050060; Phosphoglucosamine_mutase.
DR NCBIfam; TIGR01455; 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, 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:UP000654257}.
FT DOMAIN 3..136
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 158..251
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 256..365
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 372..438
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
FT ACT_SITE 102
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01554"
FT BINDING 102
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 239
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01554"
FT BINDING 241
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
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 MOD_RES 102
FT /note="Phosphoserine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01554"
SQ SEQUENCE 443 AA; 45335 MW; 811BF90EFF9CA655 CRC64;
MGRLFGTDGV RGLANRELTP ELALSLGNAA AHVLADGAAT ARPVAVVGRD PRASGEMLEA
AVTAGLTAAG VDVLLVGVLP TPAVAFLTDA YDAALGVMIS ASHNAMPDNG IKIFAGGGHK
LDDTVEDRIE QQMSTTGTRP VGADIGRVRT ADDALELYLK HLGTAVRTSL TGITVVVDCA
HGAASIAAPE AYRAAGATVI AINADPDGIN INDGCGSTHL DVLQRAVLHH GADLGLAHDG
DADRCLAVDS GGDIVDGDAI MAVLALAMRD AGELAEDTLV ATVMSNLGLH IAMREQGITL
RTTAVGDRYV LEELRAGNFS LGGEQSGHIV LPSSGTTGDG ILTGLSVMSR MAQTSRSLTE
LASVMRTLPQ VLVNVTVGDK AAVAAARDVL DAVTTAEKEL GDEGRVLLRP SGTEQLVRVM
VEAGEQSTAR RLADSIAAVV QSV
//
