ID GLMM_CHLAB Reviewed; 458 AA.
AC Q5L588;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2005, sequence version 1.
DT 01-MAY-2013, entry version 49.
DE RecName: Full=Phosphoglucosamine mutase;
DE EC=5.4.2.10;
GN Name=glmM; OrderedLocusNames=CAB757;
OS Chlamydophila abortus (strain S26/3).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydophila.
OX NCBI_TaxID=218497;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S26/3;
RX PubMed=15837807; DOI=10.1101/gr.3684805;
RA Thomson N.R., Yeats C., Bell K., Holden M.T.G., Bentley S.D.,
RA Livingstone M., Cerdeno-Tarraga A.-M., Harris B., Doggett J.,
RA Ormond D., Mungall K., Clarke K., Feltwell T., Hance Z., Sanders M.,
RA Quail M.A., Price C., Barrell B.G., Parkhill J., Longbottom D.;
RT "The Chlamydophila abortus genome sequence reveals an array of
RT variable proteins that contribute to interspecies variation.";
RL Genome Res. 15:629-640(2005).
CC -!- FUNCTION: Catalyzes the conversion of glucosamine-6-phosphate to
CC glucosamine-1-phosphate (By similarity).
CC -!- CATALYTIC ACTIVITY: Alpha-D-glucosamine 1-phosphate = D-
CC glucosamine 6-phosphate.
CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity).
CC -!- PTM: Activated by phosphorylation (By similarity).
CC -!- SIMILARITY: Belongs to the phosphohexose mutase family.
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DR EMBL; CR848038; CAH64204.1; -; Genomic_DNA.
DR RefSeq; YP_220154.1; NC_004552.2.
DR ProteinModelPortal; Q5L588; -.
DR STRING; 218497.CAB757; -.
DR EnsemblBacteria; CAH64204; CAH64204; CAB757.
DR GeneID; 3337868; -.
DR KEGG; cab:CAB757; -.
DR PATRIC; 20203043; VBIChlAbo21869_0822.
DR eggNOG; COG1109; -.
DR HOGENOM; HOG000268678; -.
DR KO; K03431; -.
DR OMA; TRINDAT; -.
DR ProtClustDB; PRK14314; -.
DR BioCyc; CABO218497:GJB0-780-MONOMER; -.
DR GO; GO:0000287; F:magnesium ion binding; IEA:HAMAP.
DR GO; GO:0008966; F:phosphoglucosamine mutase activity; IEA:HAMAP.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 3.40.120.10; -; 3.
DR HAMAP; MF_01554_B; GlmM_B; 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; IPR016066; A-D-PHexomutase_CS.
DR InterPro; IPR005841; Alpha-D-phosphohexomutase_SF.
DR InterPro; IPR006352; GlmM.
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; A-D-PHexomutase_a/b/a-I/II/III; 3.
DR TIGRFAMs; TIGR01455; glmM; 1.
DR PROSITE; PS00710; PGM_PMM; 1.
PE 3: Inferred from homology;
KW Complete proteome; Isomerase; Magnesium; Metal-binding;
KW Phosphoprotein.
FT CHAIN 1 458 Phosphoglucosamine mutase.
FT /FTId=PRO_0000147870.
FT ACT_SITE 106 106 Phosphoserine intermediate (By
FT similarity).
FT METAL 106 106 Magnesium; via phosphate group (By
FT similarity).
FT METAL 247 247 Magnesium (By similarity).
FT METAL 249 249 Magnesium (By similarity).
FT METAL 251 251 Magnesium (By similarity).
FT MOD_RES 106 106 Phosphoserine (By similarity).
SQ SEQUENCE 458 AA; 49591 MW; F204150A96F2D363 CRC64;
MTKEVKQLFG TDGVRGKANY EPMTVELSVL LGKAVAGVLQ ESKSGKHRVV VGKDTRLSGY
MFENALVAGL TSMGIETLVL GPIPTPGVAF ITRAYRADAG IMISASHNPY WDNGIKIFSS
EGFKISDVIE RRIEQMVALK EFGNFPDDCA VGKNKRVVDA MGRYIEFAKA TFPRGRTLKG
LKIVLDCAHG AAYKVAPSVF EELDAEVICY GCEPTGSNIN DNCGALFPSV IQKAVIEHKA
DVGIALDGDG DRVIMVDEKG HIVDGDMILS ICANDLKKKD LLRGNRVIAT VMTNFGVLKY
LESVGIEALI SPVGDRHVLQ NMLEYEVNLG GEQSGHMIFL DYNTTGDGIV SALQVLRIMI
ESESTLSDLT SLIVKSPQAL INVAVKEKIP LDTLPLVQEA LRDVRSSLGD SGRVLLRYSG
TENICRVMVE GLKKHQVDSL AKTIADIVDS ELGVGMVE
//
