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Database: UniProt
Entry: Q6FYQ7
LinkDB: Q6FYQ7
Original site: Q6FYQ7 
ID   GLMM_BARQU              Reviewed;         459 AA.
AC   Q6FYQ7;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   26-NOV-2014, entry version 66.
DE   RecName: Full=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};
GN   OrderedLocusNames=BQ11740;
OS   Bartonella quintana (strain Toulouse) (Rochalimaea quintana).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bartonellaceae; Bartonella.
OX   NCBI_TaxID=283165;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Toulouse;
RX   PubMed=15210978; DOI=10.1073/pnas.0305659101;
RA   Alsmark U.C.M., Frank A.C., Karlberg E.O., Legault B.-A., Ardell D.H.,
RA   Canbaeck B., Eriksson A.-S., Naeslund A.K., Handley S.A., Huvet M.,
RA   La Scola B., Holmberg M., Andersson S.G.E.;
RT   "The louse-borne human pathogen Bartonella quintana is a genomic
RT   derivative of the zoonotic agent Bartonella henselae.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9716-9721(2004).
CC   -!- FUNCTION: Catalyzes the conversion of glucosamine-6-phosphate to
CC       glucosamine-1-phosphate. {ECO:0000255|HAMAP-Rule:MF_01554}.
CC   -!- CATALYTIC ACTIVITY: Alpha-D-glucosamine 1-phosphate = D-
CC       glucosamine 6-phosphate. {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-
CC       Rule:MF_01554};
CC   -!- PTM: Activated by phosphorylation. {ECO:0000255|HAMAP-
CC       Rule:MF_01554}.
CC   -!- SIMILARITY: Belongs to the phosphohexose mutase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01554}.
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DR   EMBL; BX897700; CAF26633.1; -; Genomic_DNA.
DR   RefSeq; YP_032707.1; NC_005955.1.
DR   ProteinModelPortal; Q6FYQ7; -.
DR   STRING; 283165.BQ11740; -.
DR   EnsemblBacteria; CAF26633; CAF26633; BQ11740.
DR   GeneID; 2866668; -.
DR   KEGG; bqu:BQ11740; -.
DR   PATRIC; 31953763; VBIBarQui58630_1279.
DR   eggNOG; COG1109; -.
DR   HOGENOM; HOG000268678; -.
DR   KO; K03431; -.
DR   OMA; GHIIILD; -.
DR   OrthoDB; EOG6TN467; -.
DR   BioCyc; BQUI283165:GHZA-1172-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; 3.30.310.50; -; 1.
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   SUPFAM; SSF55957; SSF55957; 1.
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    459       Phosphoglucosamine mutase.
FT                                /FTId=PRO_0000147849.
FT   ACT_SITE    102    102       Phosphoserine intermediate.
FT                                {ECO:0000255|HAMAP-Rule:MF_01554}.
FT   METAL       102    102       Magnesium; via phosphate group.
FT                                {ECO:0000255|HAMAP-Rule:MF_01554}.
FT   METAL       243    243       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_01554}.
FT   METAL       245    245       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_01554}.
FT   METAL       247    247       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_01554}.
FT   MOD_RES     102    102       Phosphoserine. {ECO:0000255|HAMAP-
FT                                Rule:MF_01554}.
SQ   SEQUENCE   459 AA;  49802 MW;  F2D519773F534588 CRC64;
     MAQKYFGTDG IRGKANVFPM TPDFAMKVGM AVGVLFRSQR QSRRVVIGKD TRLSGYMLEN
     ALVSGFTAAG MEAFLLGPVP TPAVAMLCRS LRADLGVMIS ASHNPFYDNG IKLFGPDGFK
     LSDEIEKKIE QLIDTDLSKS LASCAEIGYA KRVEGDIYRY IEYAKRTLPR DVRLDALRIV
     VDCANGAAYK AAPRALWELG AEVFAINDAP NGTNINQKCG STDLASLKQK VHEVRADVGI
     ALDGDGDRVL IVDEKAQTVD GDQLIAVIAE HWHKTGRLQG NGVVTTIMSN LGLERFLNRK
     GLELVRTNVG DRYVVDAMRQ KGYNIGGEAS GHIVLSDFGT TGDGLVAALQ ILACMQESQS
     SMSHLCKRFE PVPQILKNVT IKNKNVLKKN QVKTAIDQAT QRLGNEARLV IRASGTEPVI
     RIMGEGDERE VLDAVVAEMV DVIAHHDALS KVGASLEGS
//
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