GenomeNet

Database: UniProt
Entry: Q5L588
LinkDB: Q5L588
Original site: Q5L588 
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   19-FEB-2014, entry version 52.
DE   RecName: Full=Phosphoglucosamine mutase;
DE            EC=5.4.2.10;
GN   Name=glmM; OrderedLocusNames=CAB757;
OS   Chlamydophila abortus (strain DSM 27085 / 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=DSM 27085 / 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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
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; HTTGDGI; -.
DR   OrthoDB; EOG6TN467; -.
DR   ProtClustDB; PRK14314; -.
DR   BioCyc; CABO218497:GJB0-780-MONOMER; -.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0008966; F:phosphoglucosamine mutase activity; IEA:UniProtKB-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; SSF53738; 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
//
DBGET integrated database retrieval system