ID   GLMM_PYRFU              Reviewed;         452 AA.
AC   Q8U2H4;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 103.
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=PF0861;
OS   Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=186497;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX   PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA   Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA   DiRuggiero J., Robb F.T.;
RT   "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT   horikoshii inferred from complete genomic sequences.";
RL   Genetics 152:1299-1305(1999).
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}.
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DR   EMBL; AE009950; AAL80985.1; -; Genomic_DNA.
DR   RefSeq; WP_011011993.1; NZ_CP023154.1.
DR   AlphaFoldDB; Q8U2H4; -.
DR   SMR; Q8U2H4; -.
DR   STRING; 186497.PF0861; -.
DR   EnsemblBacteria; AAL80985; AAL80985; PF0861.
DR   GeneID; 41712669; -.
DR   KEGG; pfu:PF0861; -.
DR   PATRIC; fig|186497.12.peg.911; -.
DR   eggNOG; arCOG00767; Archaea.
DR   HOGENOM; CLU_016950_7_1_2; -.
DR   OMA; KCSQVMY; -.
DR   OrthoDB; 58941at2157; -.
DR   PhylomeDB; Q8U2H4; -.
DR   Proteomes; UP000001013; 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; Reference proteome.
FT   CHAIN           1..452
FT                   /note="Probable phosphoglucosamine mutase"
FT                   /id="PRO_0000337823"
FT   ACT_SITE        96
FT                   /note="Phosphoserine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01554"
FT   BINDING         96
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         233
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01554"
FT   BINDING         235
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01554"
FT   BINDING         237
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01554"
FT   MOD_RES         96
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01554"
SQ   SEQUENCE   452 AA;  49819 MW;  84C57B23326C51A9 CRC64;
     MGKYFGTSGI REVVNEKLTP ELALKVGLAL GTYLGEGRVV VGIDTRTSSE MIKHALVSGL
     LATGIEVVDI GLAPTPLTGF AIKLYNADAG VTITASHNPP NYNGIKVWDR NGMAYTPDKE
     SELERIIEEE TFKRVSWMEI GEVIKADPKK EYIKNAVEQI NLENSYTVVV DSGNGAGSIV
     SPYLQRELGN KVISLNSHPT GFFVRELEPN RKSLDMLSKV VREVGADVGI AHDGDADRIG
     VVDDQGNFVD YEVMLSLIAG YMIEKYGKGK VVTTVDAGFA LDDYLKPRGG EVIRTKVGDV
     AVAYELSKHG GVFGGEPSGT WIIPQWNLTP DGIFAGALVV EMIDKLGPIS ELAKEVPRYV
     TLREKIPCPN ELKQKVMRII EKLALQNFEY KNLIDIDGIR IENEEWWILF RPSGTEPIMR
     ITLEAHTKEK AEELMKKARG LVKEAIEKAK LS