ID GLMM_METCA Reviewed; 447 AA.
AC Q607B4;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 01-MAY-2013, entry version 59.
DE RecName: Full=Phosphoglucosamine mutase;
DE EC=5.4.2.10;
GN Name=glmM; OrderedLocusNames=MCA1847;
OS Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Methylococcales;
OC Methylococcaceae; Methylococcus.
OX NCBI_TaxID=243233;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33009 / NCIMB 11132 / Bath;
RX PubMed=15383840; DOI=10.1371/journal.pbio.0020303;
RA Ward N.L., Larsen O., Sakwa J., Bruseth L., Khouri H.M., Durkin A.S.,
RA Dimitrov G., Jiang L., Scanlan D., Kang K.H., Lewis M.R., Nelson K.E.,
RA Methe B.A., Wu M., Heidelberg J.F., Paulsen I.T., Fouts D.E.,
RA Ravel J., Tettelin H., Ren Q., Read T.D., DeBoy R.T., Seshadri R.,
RA Salzberg S.L., Jensen H.B., Birkeland N.K., Nelson W.C., Dodson R.J.,
RA Grindhaug S.H., Holt I.E., Eidhammer I., Jonasen I., Vanaken S.,
RA Utterback T.R., Feldblyum T.V., Fraser C.M., Lillehaug J.R.,
RA Eisen J.A.;
RT "Genomic insights into methanotrophy: the complete genome sequence of
RT Methylococcus capsulatus (Bath).";
RL PLoS Biol. 2:1616-1628(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; AE017282; AAU91923.1; -; Genomic_DNA.
DR RefSeq; YP_114284.1; NC_002977.6.
DR ProteinModelPortal; Q607B4; -.
DR STRING; 243233.MCA1847; -.
DR EnsemblBacteria; AAU91923; AAU91923; MCA1847.
DR GeneID; 3104072; -.
DR KEGG; mca:MCA1847; -.
DR PATRIC; 22607540; VBIMetCap22254_1878.
DR eggNOG; COG1109; -.
DR HOGENOM; HOG000268678; -.
DR KO; K03431; -.
DR OMA; AYSIGRC; -.
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 1 447 Phosphoglucosamine mutase.
FT /FTId=PRO_0000147914.
FT ACT_SITE 102 102 Phosphoserine intermediate (By
FT similarity).
FT METAL 102 102 Magnesium; via phosphate group (By
FT similarity).
FT METAL 241 241 Magnesium (By similarity).
FT METAL 243 243 Magnesium (By similarity).
FT METAL 245 245 Magnesium (By similarity).
FT MOD_RES 102 102 Phosphoserine (By similarity).
SQ SEQUENCE 447 AA; 48325 MW; 4000CE96BD635E9B CRC64;
MKKEYFGTDG IRGRVGDYPI TPDFMLKLGW AAGCVFAREM PGRRVLIGKD TRISGYMFES
ALEAGFSAAG VDTQLLGPMP TPAVAYLTRT LRAQAGVVIS ASHNPYYDNG IKFFGPDGMK
LPDELELLIE DYLGRPMTTV ECSHIGKATR IVDAAGRYIE FCKSTIPLGM HFSGMKIVVD
CAHGSTYHVA PDVFSELRAT VSTLGVAPDG LNINDRVGAT DPENLRQTVL EENADLGIAL
DGDGDRLIMV DHRGEVVDGD ELLFVIANAR HAEGELKGSV VGTLMSNLGL EQAIRRLGLE
FRRAAVGDRY VMEMMLEHGS MLGGEGSGHI ICRDRTTTGD GIVSALQVLA EIVRSGKTLH
ELKQGMRKYP QRLVNVRLAE RVSLASVPLV QKVKAEVEAE LGDSGRVLLR PSGTEPLIRV
MVEGADEGQV RELADRLAGA VARAFSA
//
