ID   GLMM_THEKO              Reviewed;         449 AA.
AC   Q68BJ7;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Probable phosphoglucosamine mutase;
DE            EC=5.4.2.10;
GN   Name=glmM; OrderedLocusNames=TK2185;
OS   Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS   (Pyrococcus kodakaraensis (strain KOD1)).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=69014;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND NO FUNCTION AS A PGM/PMM.
RC   STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX   PubMed=15342576; DOI=10.1128/jb.186.18.6070-6076.2004;
RA   Rashid N., Kanai T., Atomi H., Imanaka T.;
RT   "Among multiple phosphomannomutase gene orthologues, only one gene encodes
RT   a protein with phosphoglucomutase and phosphomannomutase activities in
RT   Thermococcus kodakaraensis.";
RL   J. Bacteriol. 186:6070-6076(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX   PubMed=15710748; DOI=10.1101/gr.3003105;
RA   Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT   "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT   kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL   Genome Res. 15:352-363(2005).
CC   -!- FUNCTION: Catalyzes the conversion of glucosamine-6-phosphate to
CC       glucosamine-1-phosphate (By similarity). Does not display
CC       phosphoglucomutase (PGM) or phosphomannomutase (PMM) activities.
CC       {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   -!- PTM: Activated by phosphorylation. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the phosphohexose mutase family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AB126240; BAD42439.1; -; Genomic_DNA.
DR   EMBL; AP006878; BAD86374.1; -; Genomic_DNA.
DR   RefSeq; WP_011251135.1; NC_006624.1.
DR   AlphaFoldDB; Q68BJ7; -.
DR   SMR; Q68BJ7; -.
DR   STRING; 69014.TK2185; -.
DR   EnsemblBacteria; BAD86374; BAD86374; TK2185.
DR   GeneID; 3235556; -.
DR   KEGG; tko:TK2185; -.
DR   PATRIC; fig|69014.16.peg.2140; -.
DR   eggNOG; arCOG00767; Archaea.
DR   HOGENOM; CLU_016950_7_1_2; -.
DR   InParanoid; Q68BJ7; -.
DR   OMA; KCSQVMY; -.
DR   OrthoDB; 58941at2157; -.
DR   PhylomeDB; Q68BJ7; -.
DR   Proteomes; UP000000536; 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..449
FT                   /note="Probable phosphoglucosamine mutase"
FT                   /id="PRO_0000337825"
FT   ACT_SITE        96
FT                   /note="Phosphoserine intermediate"
FT                   /evidence="ECO:0000250"
FT   BINDING         96
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /note="via phosphate group"
FT                   /evidence="ECO:0000250"
FT   BINDING         233
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         235
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         237
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         96
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   449 AA;  48662 MW;  C43487171FA68435 CRC64;
     MGKYFGTSGI REVFNEKLTP ELALKVGKAL GTYLGGGKVV IGKDTRTSGD VIKSAVISGL
     LSTGVDVIDI GLAPTPLTGF AIKLYGADAG VTITASHNPP EYNGIKVWQA NGMAYTSEME
     RELESIMDSG NFKKAPWNEI GTLRRADPSE EYINAALKFV KLENSYTVVL DSGNGAGSVV
     SPYLQRELGN RVISLNSHPS GFFVRELEPN AKSLSALAKT VRVMKADVGI AHDGDADRIG
     VVDDQGNFVE YEVMLSLIAG YMLRKFGKGK IVTTVDAGFA LDDYLRPLGG EVIRTRVGDV
     AVADELAKHG GVFGGEPSGT WIIPQWNLTP DGIFAGALVL EMIDRLGPIS ELAKEVPRYV
     TLRAKIPCPN EKKAKAMEII AREALKTFDY EGLIDIDGIR IENGDWWILF RPSGTEPIMR
     ITLEAHEEEK AKELMGKAER LVKKAISEA