| Tag | Content |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Phosphoglucosamine mutase |
Protein Synonyms/Alias | |
Gene Name | glmM |
Gene Synonyms/Alias | mrsA, yhbF; OrderedLocusNames=b3176, JW3143 |
Created Date | 3-June-2014 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Phosphorylation | Position | Peptide | Code | Type | References | | 102 | AGIVISASHNPFYDN | S | HTP | [1],UniProt | |
Reference | [1]Phosphoproteome analysis of E. coli reveals evolutionary conservation of bacterial Ser/Thr/Tyr phosphorylation. Macek B,Gnad F,Soufi B,Kumar C,Olsen JV,Mijakovic I,Mann M Mol. Cell Proteomics 2008, Feb;7(2):299-307. [ PMID:17938405] |
Functional Description From UniProt | FUNCTION: Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate. Can also catalyze the formation of glucose-6-P from glucose-1-P, although at a 1400-fold lower rate |
| MOD_RES 102 102 Phosphoserine; by autocatalysis |
| Completeproteome; Directproteinsequencing; Isomerase; Magnesium; Metal-binding; Phosphoprotein; Referenceproteome |
Protein Sequence | MSNRKYFGTD GIRGRVGDAP ITPDFVLKLG WAAGKVLARH GSRKIIIGKD TRISGYMLES 60
ALEAGLAAAG LSALFTGPMP TPAVAYLTRT FRAEAGIVIS ASHNPFYDNG IKFFSIDGTK 120
LPDAVEEAIE AEMEKEISCV DSAELGKASR IVDAAGRYIE FCKATFPNEL SLSELKIVVD 180
CANGATYHIA PNVLRELGAN VIAIGCEPNG VNINAEVGAT DVRALQARVL AEKADLGIAF 240
DGDGDRVIMV DHEGNKVDGD QIMYIIAREG LRQGQLRGGA VGTLMSNMGL ELALKQLGIP 300
FARAKVGDRY VLEKMQEKGW RIGAENSGHV ILLDKTTTGD GIVAGLQVLA AMARNHMSLH 360
DLCSGMKMFP QILVNVRYTA GSGDPLEHES VKAVTAEVEA ALGNRGRVLL RKSGTEPLIR 420
VMVEGEDEAQ VTEFAHRIAD AVKAV 445 |
| GO:0005829 C:cytosol IBA:RefGenome GO:0000287 F:magnesium ion binding IEA:UniProtKB-HAMAP GO:0008966 F:phosphoglucosamine mutase activity IDA:EcoCyc GO:0005975 P:carbohydrate metabolic process IEA:InterPro GO:0046777 P:protein autophosphorylation IDA:EcoCyc GO:0006048 P:UDP-N-acetylglucosamine biosynthetic process IMP:EcoCyc |
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