GLMM_PYRAB
ID GLMM_PYRAB Reviewed; 451 AA.
AC Q9UZT5; G8ZJL2;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 108.
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=PYRAB10610;
GN ORFNames=PAB1666;
OS Pyrococcus abyssi (strain GE5 / Orsay).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=272844;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GE5 / Orsay;
RX PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA Weissenbach J., Zivanovic Y., Forterre P.;
RT "An integrated analysis of the genome of the hyperthermophilic archaeon
RT Pyrococcus abyssi.";
RL Mol. Microbiol. 47:1495-1512(2003).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=GE5 / Orsay;
RX PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA Gao J., Wang J.;
RT "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT Pyrococcus furiosus DSM 3638.";
RL Curr. Microbiol. 64:118-129(2012).
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; AJ248286; CAB49971.1; -; Genomic_DNA.
DR EMBL; HE613800; CCE70471.1; -; Genomic_DNA.
DR PIR; F75083; F75083.
DR RefSeq; WP_010868179.1; NC_000868.1.
DR AlphaFoldDB; Q9UZT5; -.
DR SMR; Q9UZT5; -.
DR STRING; 272844.PAB1666; -.
DR EnsemblBacteria; CAB49971; CAB49971; PAB1666.
DR GeneID; 1496416; -.
DR KEGG; pab:PAB1666; -.
DR PATRIC; fig|272844.11.peg.1116; -.
DR eggNOG; arCOG00767; Archaea.
DR HOGENOM; CLU_016950_7_1_2; -.
DR OMA; KCSQVMY; -.
DR OrthoDB; 58941at2157; -.
DR PhylomeDB; Q9UZT5; -.
DR Proteomes; UP000000810; Chromosome.
DR Proteomes; UP000009139; 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..451
FT /note="Probable phosphoglucosamine mutase"
FT /id="PRO_0000337822"
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 451 AA; 49786 MW; F337BA57646E7269 CRC64;
MGKYFGTSGI REVVNEKLTP ELALKVGLAL GTYLNGGRVV IGNDTRTSSE MLKKAVISGL
LASGVDVIDI GLAPTPLVGF AIKLYDADAG VTITASHNPP EYNGIKVWDR NGMAYTPEKE
RELERIIEEE KFKRAPWNEI GQLKQANPRE EYIEAIMKEI KLDNSYTVVI DPGNGAGSII
SPYLHRELGN RVITINSDPH GFFVRELEPN KESLSMLAKT VKALKADIGI AHDGDADRVG
VVDENGEFVE YEVMLSLIAG YMLRKYGKGK VVTTVDAGFA LDDYVRGLGG EVVRTRVGDV
AVAEELMKHG GVFGGEPSGT WIMPQWNLTP DGIFAGALVL EMIDRLGLIG ELAKEVPRYV
TLRKKIPCPN DLKAKAMEEI AKLIPREFSY EREITIDGIR IENDDWWILF RPSGTEPIMR
ITLEAHTKER AESLMEKAEK LVKDAIKKAS S
