| Tag | Content |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Phosphoglucosamine mutase |
Protein Synonyms/Alias | |
Gene Name | glmM |
Gene Synonyms/Alias | ureC; OrderedLocusNames=HP_0075 |
Created Date | 3-June-2014 |
Organism | Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori) |
NCBI Taxa ID | 85962 |
Phosphorylation | Position | Peptide | Code | Type | References | | 279 | KSKNALSSQAVVATN | S | HTP | [1] | | 288 | AVVATNMSNLALKEY | S | HTP | [1] | | 278 | QKSKNALSSQAVVAT | S | HTP | [1] | |
Reference | [1]Phosphoproteome analysis of the pathogenic bacterium Helicobacter pylori reveals over-representation of tyrosine phosphorylation and multiply phosphorylated proteins. Ge R,Sun X,Xiao C,Yin X,Shan W,Chen Z,He QY Proteomics 2011, Apr;11(8):1449-61. [ PMID:21360674] |
Functional Description From UniProt | FUNCTION: Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate |
| MOD_RES 99 99 Phosphoserine; by autocatalysis |
| Completeproteome; Isomerase; Magnesium; Metal-binding; Phosphoprotein; Referenceproteome |
Protein Sequence | MKIFGTDGVR GKAGVKLTPM FVMRLGIAAG LYFKKHSQTN KILIGKDTRK SGYMVENALV 60
SALTSIGYNV IQIGPMPTPA IAFLTEDMRC DAGIMISASH NPFEDNGIKF FNSYGYKLKE 120
EEEKAIEEIF HDEELLHSSY KVGESVGSAK RIDDVIGRYI AHLKHSFPKH LNLQSLRIVL 180
DTANGAAYKV APVVFSELGA DVLVINDEPN GCNINDQCGA LHPNQLSQEV KKYRADLGFA 240
FDGDADRLVV VDNLGNIVHG DKLLGVLGVY QKSKNALSSQ AVVATNMSNL ALKEYLKSQD 300
LELKHCAIGD KFVSECMQLN KANFGGEQSG HIIFSDYAKT GDGLVCALQV SALVLESKQV 360
SSVALNPFEL YPQSLVNLNV QKKPPLESLK GYSALLKELD KLEIRHLIRY SGTENKLRIL 420
LEAKDEKLLE SKMQELKEFF EGHLC 445 |
| GO:0000287 F:magnesium ion binding IEA:UniProtKB-HAMAP GO:0008966 F:phosphoglucosamine mutase activity IEA:UniProtKB-HAMAP GO:0005975 P:carbohydrate metabolic process IEA:InterPro |
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