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Protein

2,3-bisphosphoglycerate-independent phosphoglycerate mutase

Gene

gpmI

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.

Catalytic activityi

2-phospho-D-glycerate = 3-phospho-D-glycerate.

Cofactori

Mn2+Note: Binds 2 manganese ions per subunit.

Enzyme regulationi

Insensitive to vanadate.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi14 – 141Manganese 2By similarity
Active sitei64 – 641Phosphoserine intermediateBy similarity
Metal bindingi64 – 641Manganese 2By similarity
Metal bindingi403 – 4031Manganese 1By similarity
Metal bindingi407 – 4071Manganese 1By similarity
Metal bindingi444 – 4441Manganese 2By similarity
Metal bindingi445 – 4451Manganese 2By similarity
Metal bindingi463 – 4631Manganese 1By similarity

GO - Molecular functioni

  1. 2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity Source: EcoCyc
  2. manganese ion binding Source: EcoCyc

GO - Biological processi

  1. glucose catabolic process Source: InterPro
  2. glycolytic process Source: UniProtKB-HAMAP
  3. response to oxidative stress Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

BioCyciEcoCyc:PGMI-MONOMER.
ECOL316407:JW3587-MONOMER.
MetaCyc:PGMI-MONOMER.
SABIO-RKP37689.
UniPathwayiUPA00109; UER00186.

Names & Taxonomyi

Protein namesi
Recommended name:
2,3-bisphosphoglycerate-independent phosphoglycerate mutase (EC:5.4.2.12)
Short name:
BPG-independent PGAM
Short name:
Phosphoglyceromutase
Short name:
iPGM
Gene namesi
Name:gpmI
Synonyms:pgmI, yibO
Ordered Locus Names:b3612, JW3587
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG12296. gpmI.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 5145142,3-bisphosphoglycerate-independent phosphoglycerate mutasePRO_0000212145Add
BLAST

Proteomic databases

PaxDbiP37689.
PRIDEiP37689.

2D gel databases

SWISS-2DPAGEP37689.

Expressioni

Developmental stagei

Expressed most strongly in early exponential growth, with levels falling off as cells reached late log phase and stationary phase.

Gene expression databases

GenevestigatoriP37689.

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

DIPiDIP-12425N.
IntActiP37689. 4 interactions.
STRINGi511145.b3612.

Structurei

3D structure databases

ProteinModelPortaliP37689.
SMRiP37689. Positions 5-504.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0696.
HOGENOMiHOG000223664.
InParanoidiP37689.
KOiK15633.
OMAiDEFIMPA.
OrthoDBiEOG6HJ22X.
PhylomeDBiP37689.

Family and domain databases

Gene3Di3.40.1450.10. 1 hit.
3.40.720.10. 2 hits.
HAMAPiMF_01038. GpmI.
InterProiIPR017849. Alkaline_Pase-like_a/b/a.
IPR017850. Alkaline_phosphatase_core.
IPR011258. BPG-indep_PGM_N.
IPR006124. Metalloenzyme.
IPR005995. Pgm_bpd_ind.
[Graphical view]
PfamiPF06415. iPGM_N. 1 hit.
PF01676. Metalloenzyme. 1 hit.
[Graphical view]
PIRSFiPIRSF001492. IPGAM. 1 hit.
SUPFAMiSSF53649. SSF53649. 2 hits.
SSF64158. SSF64158. 1 hit.
TIGRFAMsiTIGR01307. pgm_bpd_ind. 1 hit.

Sequencei

Sequence statusi: Complete.

P37689-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLVSKKPMVL VILDGYGYRE EQQDNAIFSA KTPVMDALWA NRPHTLIDAS
60 70 80 90 100
GLEVGLPDRQ MGNSEVGHVN LGAGRIVYQD LTRLDVEIKD RAFFANPVLT
110 120 130 140 150
GAVDKAKNAG KAVHIMGLLS AGGVHSHEDH IMAMVELAAE RGAEKIYLHA
160 170 180 190 200
FLDGRDTPPR SAESSLKKFE EKFAALGKGR VASIIGRYYA MDRDNRWDRV
210 220 230 240 250
EKAYDLLTLA QGEFQADTAV AGLQAAYARD ENDEFVKATV IRAEGQPDAA
260 270 280 290 300
MEDGDALIFM NFRADRAREI TRAFVNADFD GFARKKVVNV DFVMLTEYAA
310 320 330 340 350
DIKTAVAYPP ASLVNTFGEW MAKNDKTQLR ISETEKYAHV TFFFNGGVEE
360 370 380 390 400
SFKGEDRILI NSPKVATYDL QPEMSSAELT EKLVAAIKSG KYDTIICNYP
410 420 430 440 450
NGDMVGHTGV MEAAVKAVEA LDHCVEEVAK AVESVGGQLL ITADHGNAEQ
460 470 480 490 500
MRDPATGQAH TAHTNLPVPL IYVGDKNVKA VEGGKLSDIA PTMLSLMGME
510
IPQEMTGKPL FIVE
Length:514
Mass (Da):56,194
Last modified:October 1, 1994 - v1
Checksum:iBD4173C2BA2CEDD8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00039 Genomic DNA. Translation: AAB18589.1.
U00096 Genomic DNA. Translation: AAC76636.1.
AP009048 Genomic DNA. Translation: BAE77680.1.
PIRiS47833.
RefSeqiNP_418069.1. NC_000913.3.
YP_491821.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC76636; AAC76636; b3612.
BAE77680; BAE77680; BAE77680.
GeneIDi12934300.
948130.
KEGGiecj:Y75_p3562.
eco:b3612.
PATRICi32122711. VBIEscCol129921_3732.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00039 Genomic DNA. Translation: AAB18589.1.
U00096 Genomic DNA. Translation: AAC76636.1.
AP009048 Genomic DNA. Translation: BAE77680.1.
PIRiS47833.
RefSeqiNP_418069.1. NC_000913.3.
YP_491821.1. NC_007779.1.

3D structure databases

ProteinModelPortaliP37689.
SMRiP37689. Positions 5-504.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-12425N.
IntActiP37689. 4 interactions.
STRINGi511145.b3612.

2D gel databases

SWISS-2DPAGEP37689.

Proteomic databases

PaxDbiP37689.
PRIDEiP37689.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76636; AAC76636; b3612.
BAE77680; BAE77680; BAE77680.
GeneIDi12934300.
948130.
KEGGiecj:Y75_p3562.
eco:b3612.
PATRICi32122711. VBIEscCol129921_3732.

Organism-specific databases

EchoBASEiEB2204.
EcoGeneiEG12296. gpmI.

Phylogenomic databases

eggNOGiCOG0696.
HOGENOMiHOG000223664.
InParanoidiP37689.
KOiK15633.
OMAiDEFIMPA.
OrthoDBiEOG6HJ22X.
PhylomeDBiP37689.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00186.
BioCyciEcoCyc:PGMI-MONOMER.
ECOL316407:JW3587-MONOMER.
MetaCyc:PGMI-MONOMER.
SABIO-RKP37689.

Miscellaneous databases

PROiP37689.

Gene expression databases

GenevestigatoriP37689.

Family and domain databases

Gene3Di3.40.1450.10. 1 hit.
3.40.720.10. 2 hits.
HAMAPiMF_01038. GpmI.
InterProiIPR017849. Alkaline_Pase-like_a/b/a.
IPR017850. Alkaline_phosphatase_core.
IPR011258. BPG-indep_PGM_N.
IPR006124. Metalloenzyme.
IPR005995. Pgm_bpd_ind.
[Graphical view]
PfamiPF06415. iPGM_N. 1 hit.
PF01676. Metalloenzyme. 1 hit.
[Graphical view]
PIRSFiPIRSF001492. IPGAM. 1 hit.
SUPFAMiSSF53649. SSF53649. 2 hits.
SSF64158. SSF64158. 1 hit.
TIGRFAMsiTIGR01307. pgm_bpd_ind. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Analysis of the Escherichia coli genome. V. DNA sequence of the region from 76.0 to 81.5 minutes."
    Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.
    Nucleic Acids Res. 22:2576-2586(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. "Enrichment of low abundance proteins of Escherichia coli by hydroxyapatite chromatography."
    Fountoulakis M., Takacs M.-F., Berndt P., Langen H., Takacs B.
    Electrophoresis 20:2181-2195(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: B / BL21.
  5. "The two analogous phosphoglycerate mutases of Escherichia coli."
    Fraser H.I., Kvaratskhelia M., White M.F.
    FEBS Lett. 455:344-348(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.

Entry informationi

Entry nameiGPMI_ECOLI
AccessioniPrimary (citable) accession number: P37689
Secondary accession number(s): Q2M7S6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: January 7, 2015
This is version 123 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.