GLMM_METS3
ID GLMM_METS3 Reviewed; 445 AA.
AC A5UKY3;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 2.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Probable phosphoglucosamine mutase {ECO:0000255|HAMAP-Rule:MF_01554};
DE EC=5.4.2.10 {ECO:0000255|HAMAP-Rule:MF_01554};
GN Name=glmM {ECO:0000255|HAMAP-Rule:MF_01554}; OrderedLocusNames=Msm_0656;
OS Methanobrevibacter smithii (strain ATCC 35061 / DSM 861 / OCM 144 / PS).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanobrevibacter.
OX NCBI_TaxID=420247;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35061 / DSM 861 / OCM 144 / PS;
RX PubMed=17563350; DOI=10.1073/pnas.0704189104;
RA Samuel B.S., Hansen E.E., Manchester J.K., Coutinho P.M., Henrissat B.,
RA Fulton R., Latreille P., Kim K., Wilson R.K., Gordon J.I.;
RT "Genomic and metabolic adaptations of Methanobrevibacter smithii to the
RT human gut.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:10643-10648(2007).
CC -!- FUNCTION: Catalyzes the conversion of glucosamine-6-phosphate to
CC glucosamine-1-phosphate. {ECO:0000255|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:0000255|HAMAP-Rule:MF_01554};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01554};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01554};
CC -!- PTM: Activated by phosphorylation. {ECO:0000255|HAMAP-Rule:MF_01554}.
CC -!- SIMILARITY: Belongs to the phosphohexose mutase family.
CC {ECO:0000255|HAMAP-Rule:MF_01554}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABQ86861.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000678; ABQ86861.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; A5UKY3; -.
DR SMR; A5UKY3; -.
DR STRING; 420247.Msm_0656; -.
DR EnsemblBacteria; ABQ86861; ABQ86861; Msm_0656.
DR KEGG; msi:Msm_0656; -.
DR PATRIC; fig|420247.28.peg.653; -.
DR eggNOG; arCOG00767; Archaea.
DR HOGENOM; CLU_016950_7_1_2; -.
DR Proteomes; UP000001992; Chromosome.
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:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd03087; PGM_like1; 1.
DR HAMAP; MF_01554_A; GlmM_A; 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; IPR023666; GlmM_arc.
DR InterPro; IPR024086; GlmM_arc-type.
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; SSF53738; SSF53738; 3.
DR SUPFAM; SSF55957; SSF55957; 1.
DR TIGRFAMs; TIGR03990; Arch_GlmM; 1.
DR PROSITE; PS00710; PGM_PMM; 1.
PE 3: Inferred from homology;
KW Isomerase; Magnesium; Metal-binding; Phosphoprotein.
FT CHAIN 1..445
FT /note="Probable phosphoglucosamine mutase"
FT /id="PRO_0000337810"
FT ACT_SITE 99
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01554"
FT BINDING 99
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /note="via phosphate group"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01554"
FT BINDING 238
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01554"
FT BINDING 240
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01554"
FT BINDING 242
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01554"
FT MOD_RES 99
FT /note="Phosphoserine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01554"
SQ SEQUENCE 445 AA; 47984 MW; 4668CB0DB6B77748 CRC64;
MAVKKLFGTS GIRGKINSEV TCELALNVGK SLACYLGNEG TVVLGYDTRT TNVMLDQAIC
AGLLESGVDV IKIGMVPTPL VGYATDKLGA DAGVMLTASH NPSQYNGIKI WNANGMAYTS
AQEAKIEEIY SNESYTSVSW DKVGSLRVNE EIKGRYIDDL VGMVNIKPGL KVVIDCASGA
GSEISPLVFR KAGCEVTTLN SQPDGFFPGR NPEPNAENLQ NLMKTVVAIG ADLGIAHDGD
ADRMITIDEN GDISPFDSLL ALMSKEFDGD IVTTVDAGLC MDESVKGNVL RTKVGDVNVA
EVIIEKDAAF GGEPSGTWLH PDFCMCPDGI LSGLRMAELV SNKGKLSELL LEIPSYPNIR
EKIICSKEAK TAVMENMEDL LKDSFDDIKE INSIDGVRLT FNDDSWVLVR PSGTEDYIRI
TLESKDSTKA QAIKETCVKI IKENI