P31120 (GLMM_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Phosphoglucosamine mutase
EC=5.4.2.10

Gene names

Name:	glmM
Synonyms:	mrsA, yhbF
Ordered Locus Names:	b3176, JW3143

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	445 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate. Can also catalyze the formation of glucose-6-P from glucose-1-P, although at a 1400-fold lower rate. Ref.6
Catalytic activity	Alpha-D-glucosamine 1-phosphate = D-glucosamine 6-phosphate. HAMAP MF_01554_B
Cofactor	Binds 1 magnesium ion per subunit By similarity. HAMAP MF_01554_B
Enzyme regulation	Autophosphorylation is inhibited by inorganic phosphate or EDTA. Ref.7
Post-translational modification	Activated by phosphorylation. Can autophosphorylate in vitro using ATP, alpha-D-glucosamine 1,6-bisphosphate or alpha-D-glucose 1,6-bisphosphate. HAMAP MF_01554_B
Miscellaneous	Catalysis proceeds by a classical ping-pong bi-bi reaction mechanism, with alpha-D-glucosamine 1,6-bisphosphate as an intermediate. HAMAP MF_01554_B
Sequence similarities	Belongs to the phosphohexose mutase family.
Biophysicochemical properties	Kinetic parameters: KM=0.05 mM for glucosamine-6-P Ref.6 Ref.7 KM=0.08 mM for glucosamine-1,6-diP KM=0.5 mM for glucose-1,6-diP KM=0.65 mM for glucose-1-P KM=0.06 mM for ATP

Ontologies

Keywords
Ligand	Magnesium Metal-binding
Molecular function	Isomerase
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	UDP-N-acetylglucosamine biosynthetic process Inferred from mutant phenotype Ref.5. Source: EcoCyc glucose 1-phosphate metabolic process Inferred from Biological aspect of Ancestor. Source: RefGenome protein autophosphorylation Inferred from direct assay Ref.7. Source: EcoCyc
Cellular component	cytosol Inferred from Biological aspect of Ancestor. Source: RefGenome
Molecular function	magnesium ion binding Inferred from electronic annotation. Source: InterPro phosphoglucomutase activity Inferred from Biological aspect of Ancestor. Source: RefGenome phosphoglucosamine mutase activity Inferred from direct assay Ref.6. Source: EcoCyc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
yjhG	P39358	1	EBI-370683,EBI-1127001

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.5
	Chain	2 – 445	444	Phosphoglucosamine mutase HAMAP MF_01554_B		PRO_0000147887
Sites
	Active site	102	1	Phosphoserine intermediate Ref.7
	Metal binding	102	1	Magnesium; via phosphate group By similarity
	Metal binding	241	1	Magnesium By similarity
	Metal binding	243	1	Magnesium By similarity
	Metal binding	245	1	Magnesium By similarity
Amino acid modifications
	Modified residue	102	1	Phosphoserine; by autocatalysis Ref.6 Ref.7
Experimental info
	Mutagenesis	100	1	S → A: 2% of wild-type activity. Ref.6
	Mutagenesis	100	1	S → T: 20-fold increase in the non-specific phosphoglucomutase activity towards glucose-phosphate substrates (non aminated). Ref.6
	Mutagenesis	102	1	S → A: Loss of activity in the absence or presence of glucosamine-1,6-diP. Ref.6
	Sequence conflict	69	1	A → R in AAA97510. Ref.2
	Sequence conflict	162	1	C → S in AAA97510. Ref.2
	Sequence conflict	167	1	P → R in AAA97510. Ref.2
	Sequence conflict	178 – 181	4	VVDC → LVIG in AAA97510. Ref.2
	Sequence conflict	411	1	R → C in AAA97510. Ref.2
	Sequence conflict	417	1	P → R in AAA97510. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P31120 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: ECDF9A0378A980EC	FASTA	445	47,544
	10 20 30 40 50 60 MSNRKYFGTD GIRGRVGDAP ITPDFVLKLG WAAGKVLARH GSRKIIIGKD TRISGYMLES 70 80 90 100 110 120 ALEAGLAAAG LSALFTGPMP TPAVAYLTRT FRAEAGIVIS ASHNPFYDNG IKFFSIDGTK 130 140 150 160 170 180 LPDAVEEAIE AEMEKEISCV DSAELGKASR IVDAAGRYIE FCKATFPNEL SLSELKIVVD 190 200 210 220 230 240 CANGATYHIA PNVLRELGAN VIAIGCEPNG VNINAEVGAT DVRALQARVL AEKADLGIAF 250 260 270 280 290 300 DGDGDRVIMV DHEGNKVDGD QIMYIIAREG LRQGQLRGGA VGTLMSNMGL ELALKQLGIP 310 320 330 340 350 360 FARAKVGDRY VLEKMQEKGW RIGAENSGHV ILLDKTTTGD GIVAGLQVLA AMARNHMSLH 370 380 390 400 410 420 DLCSGMKMFP QILVNVRYTA GSGDPLEHES VKAVTAEVEA ALGNRGRVLL RKSGTEPLIR 430 440 VMVEGEDEAQ VTEFAHRIAD AVKAV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The dihydropteroate synthase gene, folP, is near the leucine tRNA gene, leuU, on the Escherichia coli chromosome." Dallas W.S., Dev I.K., Ray P.H. J. Bacteriol. 175:7743-7744(1993) [PubMed: 8244950] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[2]	Wang R., Kushner S.R. Submitted (SEP-1993) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[3]	"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: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"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: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"Characterization of the essential gene glmM encoding phosphoglucosamine mutase in Escherichia coli." Mengin-Lecreulx D., van Heijenoort J. J. Biol. Chem. 271:32-39(1996) [PubMed: 8550580] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-12, CHARACTERIZATION.
[6]	"Reaction mechanism of phosphoglucosamine mutase from Escherichia coli." Jolly L., Ferrari P., Blanot D., Van Heijenoort J., Fassy F., Mengin-Lecreulx D. Eur. J. Biochem. 262:202-210(1999) [PubMed: 10231382] [Abstract] Cited for: PHOSPHORYLATION AT SER-102, FUNCTION, SUBSTRATE SPECIFICITY, KINETIC PARAMETERS, REACTION MECHANISM, MASS SPECTROMETRY, MUTAGENESIS OF SER-100 AND SER-102.
[7]	"Autophosphorylation of phosphoglucosamine mutase from Escherichia coli." Jolly L., Pompeo F., van Heijenoort J., Fassy F., Mengin-Lecreulx D. J. Bacteriol. 182:1280-1285(2000) [PubMed: 10671448] [Abstract] Cited for: AUTOPHOSPHORYLATION AT SER-102, KINETIC PARAMETERS, ENZYME REGULATION, ACTIVE SITE.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L12968 Unassigned DNA. Translation: AAA16122.1. U01376 Genomic DNA. Translation: AAA97510.1. U18997 Genomic DNA. Translation: AAA57977.1. U00096 Genomic DNA. Translation: AAC76208.1. AP009048 Genomic DNA. Translation: BAE77220.1.
PIR	I41215.
RefSeq	NP_417643.1. NC_000913.2.
3D structure databases
ProteinModelPortal	P31120.
SMR	P31120. Positions 5-445.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-10260N.
IntAct	P31120. 15 interactions.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBESCT00000003138; EBESCP00000003138; EBESCG00000002574. EBESCT00000014407; EBESCP00000013698; EBESCG00000013468.
GeneID	947692.
GenomeReviews	Gene locus JW3143 in contig AP009048_GR. Gene locus b3176 in contig U00096_GR.
KEGG	ecj:JW3143. eco:b3176.
PATRIC	32121770. VBIEscCol129921_3269.
Organism-specific databases
EchoBASE	EB1514.
EcoGene	EG11553. glmM.
Phylogenomic databases
eggNOG	COG1109.
GeneTree	EBGT00050000008225.
HOGENOM	HBG644964.
OMA	GVGSTHL.
PhylomeDB	P31120.
ProtClustDB	PRK10887.
Enzyme and pathway databases
BioCyc	EcoCyc:PHOSGLUCOSAMINEMUT-MONOMER. MetaCyc:PHOSGLUCOSAMINEMUT-MONOMER.
Gene expression databases
Genevestigator	P31120.
Family and domain databases
HAMAP	MF_01554_B. GlmM_B. [Tree]
InterPro	IPR005844. A-D-PHexomutase_a/b/a-I. IPR016055. A-D-PHexomutase_a/b/a-I/II/III. IPR005845. A-D-PHexomutase_a/b/a-II. IPR005846. A-D-PHexomutase_a/b/a-III. IPR005843. A-D-PHexomutase_C. IPR016066. A-D-PHexomutase_CS. IPR005841. Alpha-D-phosphohexomutase_SF. IPR006352. GlmM. [Graphical view]
Gene3D	G3DSA:3.40.120.10. A-D-PHexomutase_a/b/a-I/II/III. 3 hits.
KO	K03431.
Pfam	PF02878. PGM_PMM_I. 1 hit. PF02879. PGM_PMM_II. 1 hit. PF02880. PGM_PMM_III. 1 hit. PF00408. PGM_PMM_IV. 1 hit. [Graphical view]
PRINTS	PR00509. PGMPMM.
SUPFAM	SSF53738. A-D-PHexomutase_a/b/a-I/II/III. 3 hits.
TIGRFAMs	TIGR01455. GlmM. 1 hit.
PROSITE	PS00710. PGM_PMM. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GLMM_ECOLI

Accession

Primary (citable) accession number: P31120
Secondary accession number(s): Q2M936

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 104 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program