GLMM_METJA
ID GLMM_METJA Reviewed; 448 AA.
AC Q58500; B1A8K6;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Phosphoglucosamine mutase;
DE EC=5.4.2.10;
GN Name=glmM; OrderedLocusNames=MJ1100;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SUBUNIT.
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=18263721; DOI=10.1128/jb.01970-07;
RA Namboori S.C., Graham D.E.;
RT "Acetamido sugar biosynthesis in the Euryarchaea.";
RL J. Bacteriol. 190:2987-2996(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
CC -!- FUNCTION: Catalyzes the conversion of glucosamine-6-phosphate to
CC glucosamine-1-phosphate. {ECO:0000250}.
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;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC -!- SUBUNIT: Forms large aggregates. {ECO:0000269|PubMed:18263721}.
CC -!- PTM: Activated by phosphorylation. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the phosphohexose mutase family. {ECO:0000305}.
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DR EMBL; EU430076; ABZ91903.1; -; Genomic_DNA.
DR EMBL; L77117; AAB99103.1; -; Genomic_DNA.
DR PIR; C64437; C64437.
DR RefSeq; WP_010870612.1; NC_000909.1.
DR AlphaFoldDB; Q58500; -.
DR SMR; Q58500; -.
DR STRING; 243232.MJ_1100; -.
DR EnsemblBacteria; AAB99103; AAB99103; MJ_1100.
DR GeneID; 1451997; -.
DR KEGG; mja:MJ_1100; -.
DR eggNOG; arCOG00767; Archaea.
DR HOGENOM; CLU_016950_7_1_2; -.
DR InParanoid; Q58500; -.
DR OMA; PITCFKA; -.
DR OrthoDB; 58941at2157; -.
DR PhylomeDB; Q58500; -.
DR Proteomes; UP000000805; 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:0004615; F:phosphomannomutase activity; IBA:GO_Central.
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 1: Evidence at protein level;
KW Isomerase; Magnesium; Metal-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1..448
FT /note="Phosphoglucosamine mutase"
FT /id="PRO_0000148029"
FT ACT_SITE 89
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000250"
FT BINDING 89
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /note="via phosphate group"
FT /evidence="ECO:0000250"
FT BINDING 232
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 234
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 236
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT MOD_RES 89
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT CONFLICT 209
FT /note="L -> I (in Ref. 1; ABZ91903)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 448 AA; 50099 MW; FBC7EF17A73DF9B4 CRC64;
MGRLFGTSGI RMKNLSPKIA YKVGLAVAKK YKKVVVGRDT RTTGKLIETA LTAGILNGGG
EVTTINIVPT PVLGFNARNY DVGIMITASH NPPEYNGIKL FNKNGLAFNK KEEDEIEEII
FKEDFIEVEW HSVGEIWEDS RAIRNYMEHI LKNVEINEKF NVVIDCANAS ACLVSPYLFT
DLGCHVISVN SHMDGRFIGR LPEPDEKNLK KTMDMIKGLN MSGDNYIGIA HDGDADRMVA
IDEKGRLADF DKLLAAFSRY MVEKTGNKKI VTTVDASMII DEYLKDLDVE IIRTKVGDVA
VAEEMIKNSA VFGGEPSGTW IHADIHLTPD GILSGLRVLE MLDFYNKKLY EILDEIPSYV
NLREKIPCED DKKEKVMSYV IENGESLFKT VPETVDGARF NLENGWVLIR PSGTEPYIRV
RVEAKNNKDA KELLEKGIKL VKEALSAL
