| 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 | pgmI, yibO; OrderedLocusNames=b3612, JW3587 |
Created Date | 3-June-2014 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Phosphorylation | Position | Peptide | Code | Type | References | | 64 | PDRQMGNSEVGHVNL | S | HTP | [1] | |
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 interconversion of 2-phosphoglycerate and 3-phosphoglycerate |
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| Completeproteome; Glycolysis; Isomerase; Manganese; Metal-binding; Referenceproteome |
Protein Sequence | MLVSKKPMVL VILDGYGYRE EQQDNAIFSA KTPVMDALWA NRPHTLIDAS GLEVGLPDRQ 60
MGNSEVGHVN LGAGRIVYQD LTRLDVEIKD RAFFANPVLT GAVDKAKNAG KAVHIMGLLS 120
AGGVHSHEDH IMAMVELAAE RGAEKIYLHA FLDGRDTPPR SAESSLKKFE EKFAALGKGR 180
VASIIGRYYA MDRDNRWDRV EKAYDLLTLA QGEFQADTAV AGLQAAYARD ENDEFVKATV 240
IRAEGQPDAA MEDGDALIFM NFRADRAREI TRAFVNADFD GFARKKVVNV DFVMLTEYAA 300
DIKTAVAYPP ASLVNTFGEW MAKNDKTQLR ISETEKYAHV TFFFNGGVEE SFKGEDRILI 360
NSPKVATYDL QPEMSSAELT EKLVAAIKSG KYDTIICNYP NGDMVGHTGV MEAAVKAVEA 420
LDHCVEEVAK AVESVGGQLL ITADHGNAEQ MRDPATGQAH TAHTNLPVPL IYVGDKNVKA 480
VEGGKLSDIA PTMLSLMGME IPQEMTGKPL FIVE 514 |
| GO:0005737 C:cytoplasm IDA:UniProtKB GO:0046537 F:2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity IDA:EcoCyc GO:0030145 F:manganese ion binding IDA:EcoCyc GO:0006096 P:glycolytic process IEA:UniProtKB-HAMAP |
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