P37689 (GPMI_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
2,3-bisphosphoglycerate-independent phosphoglycerate mutase
Short name=BPG-independent PGAM
Short name=Phosphoglyceromutase
Short name=iPGM
EC=5.4.2.1

Gene names

Name:	gpmI
Synonyms:	pgmI, yibO
Ordered Locus Names:	b3612, JW3587

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	514 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate. HAMAP-Rule MF_01038
Catalytic activity	2-phospho-D-glycerate = 3-phospho-D-glycerate. HAMAP-Rule MF_01038
Cofactor	Binds 2 manganese ions per subunit.
Enzyme regulation	Insensitive to vanadate. HAMAP-Rule MF_01038
Pathway	Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5. HAMAP-Rule MF_01038
Subunit structure	Monomer.
Developmental stage	Expressed most strongly in early exponential growth, with levels falling off as cells reached late log phase and stationary phase. HAMAP-Rule MF_01038
Sequence similarities	Belongs to the BPG-independent phosphoglycerate mutase family.

Ontologies

Keywords
Biological process	Glycolysis
Ligand	Manganese Metal-binding
Molecular function	Isomerase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	glycolysis Inferred from electronic annotation. Source: HAMAP
Cellular_component	cytoplasm Inferred from direct assay PubMed 16858726. Source: UniProtKB
Molecular_function	2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity Inferred from direct assay Ref.5PubMed 4932978. Source: EcoCyc manganese ion binding Inferred from direct assay Ref.5. Source: EcoCyc
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 514	514	2,3-bisphosphoglycerate-independent phosphoglycerate mutase HAMAP-Rule MF_01038		PRO_0000212145
Sites
	Active site	64	1	Phosphoserine intermediate By similarity
	Metal binding	14	1	Manganese 2 By similarity
	Metal binding	64	1	Manganese 2 By similarity
	Metal binding	403	1	Manganese 1 By similarity
	Metal binding	407	1	Manganese 1 By similarity
	Metal binding	444	1	Manganese 2 By similarity
	Metal binding	445	1	Manganese 2 By similarity
	Metal binding	463	1	Manganese 1 By similarity

Sequences

	Sequence		Length	Mass (Da)
	P37689 [UniParc]. Last modified October 1, 1994. Version 1. Checksum: BD4173C2BA2CEDD8	FASTA	514	56,194
	10 20 30 40 50 60 MLVSKKPMVL VILDGYGYRE EQQDNAIFSA KTPVMDALWA NRPHTLIDAS GLEVGLPDRQ 70 80 90 100 110 120 MGNSEVGHVN LGAGRIVYQD LTRLDVEIKD RAFFANPVLT GAVDKAKNAG KAVHIMGLLS 130 140 150 160 170 180 AGGVHSHEDH IMAMVELAAE RGAEKIYLHA FLDGRDTPPR SAESSLKKFE EKFAALGKGR 190 200 210 220 230 240 VASIIGRYYA MDRDNRWDRV EKAYDLLTLA QGEFQADTAV AGLQAAYARD ENDEFVKATV 250 260 270 280 290 300 IRAEGQPDAA MEDGDALIFM NFRADRAREI TRAFVNADFD GFARKKVVNV DFVMLTEYAA 310 320 330 340 350 360 DIKTAVAYPP ASLVNTFGEW MAKNDKTQLR ISETEKYAHV TFFFNGGVEE SFKGEDRILI 370 380 390 400 410 420 NSPKVATYDL QPEMSSAELT EKLVAAIKSG KYDTIICNYP NGDMVGHTGV MEAAVKAVEA 430 440 450 460 470 480 LDHCVEEVAK AVESVGGQLL ITADHGNAEQ MRDPATGQAH TAHTNLPVPL IYVGDKNVKA 490 500 510 VEGGKLSDIA PTMLSLMGME IPQEMTGKPL FIVE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] 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.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U00039 Genomic DNA. Translation: AAB18589.1. U00096 Genomic DNA. Translation: AAC76636.1. AP009048 Genomic DNA. Translation: BAE77680.1.
PIR	S47833.
RefSeq	NP_418069.1. NC_000913.2. YP_491821.1. NC_007779.1.
3D structure databases
ProteinModelPortal	P37689.
SMR	P37689. Positions 5-504.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-12425N.
IntAct	P37689. 4 interactions.
STRING	511145.b3612.
2D gel databases
SWISS-2DPAGE	P37689.
Proteomic databases
PaxDb	P37689.
PRIDE	P37689.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAC76636; AAC76636; b3612. BAE77680; BAE77680; BAE77680.
GeneID	12934300. 948130.
KEGG	ecj:Y75_p3562. eco:b3612.
PATRIC	32122711. VBIEscCol129921_3732.
Organism-specific databases
EchoBASE	EB2204.
EcoGene	EG12296. gpmI.
Phylogenomic databases
eggNOG	COG0696.
HOGENOM	HOG000223664.
KO	K15633.
OMA	MIDYSTG.
ProtClustDB	PRK05434.
Enzyme and pathway databases
BioCyc	EcoCyc:PGMI-MONOMER. ECOL316407:JW3587-MONOMER. MetaCyc:PGMI-MONOMER.
SABIO-RK	P37689.
UniPathway	UPA00109; UER00186.
Gene expression databases
Genevestigator	P37689.
Family and domain databases
Gene3D	3.40.1450.10. 1 hit. 3.40.720.10. 2 hits.
HAMAP	MF_01038. GpmI.
InterPro	IPR017849. Alkaline_Pase-like_a/b/a. IPR017850. Alkaline_phosphatase_core. IPR011258. BPG-indep_PGM_N. IPR006124. Metalloenzyme. IPR005995. Pgm_bpd_ind. [Graphical view]
Pfam	PF06415. iPGM_N. 1 hit. PF01676. Metalloenzyme. 1 hit. [Graphical view]
PIRSF	PIRSF001492. IPGAM. 1 hit.
SUPFAM	SSF53649. Alkaline_phosphatase_core. 1 hit. SSF64158. BPG-indep_PGM_N. 1 hit.
TIGRFAMs	TIGR01307. pgm_bpd_ind. 1 hit.
ProtoNet	Search...

Entry information

Entry name

GPMI_ECOLI

Accession

Primary (citable) accession number: P37689
Secondary accession number(s): Q2M7S6

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	October 1, 1994
Last modified:	May 1, 2013
This is version 111 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program