| Tag | Content |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | 2,3-bisphosphoglycerate-independent phosphoglycerate mutase |
Protein Synonyms/Alias | BPG-independent PGAM; Phosphoglyceromutase; iPGM |
Gene Name | gpmI |
Gene Synonyms/Alias | pgm; OrderedLocusNames=lmo2456 |
Created Date | 3-June-2014 |
Organism | Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e) |
NCBI Taxa ID | 169963 |
Phosphorylation | Position | Peptide | Code | Type | References | | 62 | PEGQMGNSEVGHTNI | S | HTP | [1] | |
Reference | [1]Analysis of the serine/threonine/tyrosine phosphoproteome of the pathogenic bacterium Listeria monocytogenes reveals phosphorylated proteins related to virulence. Misra SK,Milohanic E,Aké F,Mijakovic I,Deutscher J,Monnet V,Henry C Proteomics 2011, Nov;11(21):4155-65. [ PMID:21956863] |
Functional Description From UniProt | FUNCTION: Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate (By similarity) |
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| Completeproteome; Glycolysis; Isomerase; Manganese; Metal-binding; Referenceproteome |
Protein Sequence | MSKSPVAIII LDGFGKRAET VGNAVAQANK PNFDRYWADF PHGELKAAGL DVGLPEGQMG 60
NSEVGHTNIG AGRIVYQSLT RIDKAIEEGE FQENKALNNA FTHTKENNSD LHLFGLLSDG 120
GVHSHINHLV ALLETAKDKG VKNVYIHAFL DGRDVAPQSS LEYLETLQKA ISDLNYGAIA 180
TVSGRFYAMD RDKRWERVEK AYKAIVSAEG EKFEDPIELV KASYANDKND EFVVPAIITK 240
DGKPVATVKD NDAVIFFNFR PDRAIQLSNA FTDKEWDHFD RGADHPKNIK FVTMTLYNPS 300
IDAEVAFEPI EMKNVIGEVL SNEGLSQLRI AETEKYPHVT FFMNGGRNEE FPGENRILIN 360
SPKVETYDLQ PEMSAYEVTD ALVEDIKNDK HDAIILNFAN PDMVGHSGML EPTIKAIEAV 420
DENLGRVVDL ILEKGGSAII FADHGNSETM STPEGKPHTA HTTVPVPVIV TKKGVTLREG 480
GRLADVAPTM LDLLGVKKPA EMTGESLIQK 510 |
| GO:0005737 C:cytoplasm IEA:InterPro GO:0046537 F:2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity IEA:UniProtKB-HAMAP GO:0030145 F:manganese ion binding IEA:UniProtKB-HAMAP GO:0006096 P:glycolytic process IEA:UniProtKB-HAMAP |
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