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 29-MAY-2013, entry version 58.
DE RecName: Full=Phosphoglucosamine mutase;
DE EC=5.4.2.10;
GN Name=glmM; 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 (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; 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; TLMSNMS; -.
DR ProtClustDB; PRK10887; -.
DR BioCyc; BQUI283165:GHZA-1172-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 1 459 Phosphoglucosamine mutase.
FT /FTId=PRO_0000147849.
FT ACT_SITE 102 102 Phosphoserine intermediate (By
FT similarity).
FT METAL 102 102 Magnesium; via phosphate group (By
FT similarity).
FT METAL 243 243 Magnesium (By similarity).
FT METAL 245 245 Magnesium (By similarity).
FT METAL 247 247 Magnesium (By similarity).
FT MOD_RES 102 102 Phosphoserine (By similarity).
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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