GLMM_METMP
ID GLMM_METMP Reviewed; 447 AA.
AC Q6LYB4;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Phosphoglucosamine mutase;
DE EC=5.4.2.10;
GN Name=glmM; OrderedLocusNames=MMP1077;
OS Methanococcus maripaludis (strain S2 / LL).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanococcaceae; Methanococcus.
OX NCBI_TaxID=267377;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S2 / LL;
RX PubMed=15466049; DOI=10.1128/jb.186.20.6956-6969.2004;
RA Hendrickson E.L., Kaul R., Zhou Y., Bovee D., Chapman P., Chung J.,
RA Conway de Macario E., Dodsworth J.A., Gillett W., Graham D.E., Hackett M.,
RA Haydock A.K., Kang A., Land M.L., Levy R., Lie T.J., Major T.A.,
RA Moore B.C., Porat I., Palmeiri A., Rouse G., Saenphimmachak C., Soell D.,
RA Van Dien S., Wang T., Whitman W.B., Xia Q., Zhang Y., Larimer F.W.,
RA Olson M.V., Leigh J.A.;
RT "Complete genome sequence of the genetically tractable hydrogenotrophic
RT methanogen Methanococcus maripaludis.";
RL J. Bacteriol. 186:6956-6969(2004).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PTM, PH DEPENDENCE, AND SUBUNIT.
RC STRAIN=900;
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).
CC -!- FUNCTION: Catalyzes the conversion of glucosamine-6-phosphate to
CC glucosamine-1-phosphate. Also catalyzes the isomerization of glucose-1-
CC phosphate to glucose-6-phosphate, but at a 5-fold lower rate.
CC {ECO:0000269|PubMed:18263721}.
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:0000269|PubMed:18263721};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:18263721};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000269|PubMed:18263721};
CC -!- SUBUNIT: Monomer. Also forms large aggregates.
CC {ECO:0000269|PubMed:18263721}.
CC -!- PTM: Activated by phosphorylation. Glucose-1,6-bisphosphate or
CC fructose-1,6-bisphosphate can activate the enzyme in vitro. However,
CC since glucose-1,6-bisphosphate is not believed to form in methanogens,
CC the physiologically relevant activator might be a serine kinase
CC protein.
CC -!- SIMILARITY: Belongs to the phosphohexose mutase family. {ECO:0000305}.
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DR EMBL; BX950229; CAF30633.1; -; Genomic_DNA.
DR RefSeq; WP_011171021.1; NC_005791.1.
DR AlphaFoldDB; Q6LYB4; -.
DR SMR; Q6LYB4; -.
DR STRING; 267377.MMP1077; -.
DR EnsemblBacteria; CAF30633; CAF30633; MMP1077.
DR GeneID; 2762645; -.
DR KEGG; mmp:MMP1077; -.
DR PATRIC; fig|267377.15.peg.1110; -.
DR eggNOG; arCOG00767; Archaea.
DR HOGENOM; CLU_016950_7_1_2; -.
DR OMA; KCSQVMY; -.
DR OrthoDB; 58941at2157; -.
DR BioCyc; MMAR267377:MMP_RS05570-MON; -.
DR BRENDA; 5.4.2.10; 3262.
DR Proteomes; UP000000590; Chromosome.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008966; F:phosphoglucosamine mutase activity; IDA:CACAO.
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..447
FT /note="Phosphoglucosamine mutase"
FT /id="PRO_0000337813"
FT ACT_SITE 88
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000250"
FT BINDING 88
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /note="via phosphate group"
FT /evidence="ECO:0000250"
FT BINDING 231
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
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 MOD_RES 88
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 447 AA; 49384 MW; F50B41234C5B6EAA CRC64;
MKLFGTSGIR MKNLDPLIAY KVGFAISKNF KKAVIGRDTR TTGNLIESAI TAGLLNGGCD
VTTIGMVPTP VLGYSAKDYD LGIMITASHN PPEYNGIKLF NKNGTAFDPK QEKELENIIN
NDDFNECTWD NIGCVVEDKT AVKKYFEYIL QNLNLNTNFN VVVDCANAAG CVVSPNIFTE
AGCKVISVNS HCDGRFVGRM PEPNETNLKE TVDIIKGLNS NGRNYVGIAH DGDADRMIAI
DELGRVTDFD KLLAAFCKYL VQKTGADKIV TTVDASMAIE EYLNEFGAKV IRTKIGDVAV
AEELEKTGAI FGGEPSGTWI HRDIHLTPDG ILSGLRVLEM MEFYGKKLHE IIDEVPSYCN
MREKISCPDN LKQNVMDYVS KEGEKIFEKK PETLDGVRFS FENGWILIRP SGTESYVRVR
VEAKEKDFAE KLMKTGISMV KTGISGK
