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A0LRQ7 (GLMM_ACIC1) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 37. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Phosphoglucosamine mutase

EC=5.4.2.10
Gene names
Name:glmM
Ordered Locus Names:Acel_0343
OrganismAcidothermus cellulolyticus (strain ATCC 43068 / 11B) [Complete proteome] [HAMAP]
Taxonomic identifier351607 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesFrankineaeAcidothermaceaeAcidothermus

Protein attributes

Sequence length461 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate By similarity. HAMAP MF_01554_B

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

Post-translational modification

Activated by phosphorylation By similarity. HAMAP MF_01554_B

Sequence similarities

Belongs to the phosphohexose mutase family.

Ontologies

Keywords
   LigandMagnesium
Metal-binding
   Molecular functionIsomerase
   PTMPhosphoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processcarbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

   Molecular functionmagnesium ion binding

Inferred from electronic annotation. Source: InterPro

phosphoglucosamine mutase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 461461Phosphoglucosamine mutase HAMAP MF_01554_B
PRO_0000305630

Sites

Active site1181Phosphoserine intermediate By similarity
Metal binding1181Magnesium; via phosphate group By similarity
Metal binding2551Magnesium By similarity
Metal binding2571Magnesium By similarity
Metal binding2591Magnesium By similarity

Amino acid modifications

Modified residue1181Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
A0LRQ7 [UniParc].

Last modified December 12, 2006. Version 1.
Checksum: 8F5F0889D96BB30B

FASTA46147,715
        10         20         30         40         50         60 
MAVSGTAAGT GLASTPRLFG TDGVRGIANR DLTAELALDL AVAAAHVLAQ AGAFEGHRPL 

        70         80         90        100        110        120 
AVVGRDPRAS GEFLEAAVVA GLASAGVDVL RLGVLPTPAV AYLTAALDAD LGVVLSASHN 

       130        140        150        160        170        180 
PMPDNGIKFL ARGGHKLPDD IEDAVAARLG EPWTRPVGRF VGRVRDYPEG LDQYVEHVLA 

       190        200        210        220        230        240 
TSDQRLDGLR VVVDCAHGAA SVVSPAVLRR AGATVVPIGC EPDGYNINDG HGSTNIETLQ 

       250        260        270        280        290        300 
AAVRREGADA GIAHDGDADR CLAVDAAGDV VDGDQILAIL ALAWQEAGRL AHDTVVATVM 

       310        320        330        340        350        360 
SNLGLKLGLA AHGISVVETA VGDRYVLEAM RAGGYVLGGE QSGHIIMLDY ATTGDGVLTG 

       370        380        390        400        410        420 
LQLLGRMAAT GRPLADLARV VRRLPQVLRN VTGVDKTRVD TDPVINKELA AARGELGDGG 

       430        440        450        460 
RVLLRASGTE PVVRVMVEAE TEADAERVAE RLARVVRERL G 

« Hide

References

[1]"Complete sequence of Acidothermus cellulolyticus 11B."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Zharchuk I., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N. expand/collapse author list , Berry A.M., Adney W.S., Normand P., Leu D., Pujic P., Richardson P.
Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43068 / 11B.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000481 Genomic DNA. Translation: ABK52117.1.
RefSeqYP_872103.1. NC_008578.1.

3D structure databases

ProteinModelPortalA0LRQ7.
ModBaseSearch...

Protein-protein interaction databases

STRINGA0LRQ7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4486411.
GenomeReviewsGene locus Acel_0343 in contig CP000481_GR.
KEGGace:Acel_0343.
PATRIC20671048. VBIAciCel132453_0371.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1109.
HOGENOMHBG644964.
OMAGVGSTHL.
ProtClustDBPRK14318.

Enzyme and pathway databases

BioCycACEL351607:ACEL_0343-MONOMER.

Family and domain databases

HAMAPMF_01554_B. GlmM_B.
[Tree]
InterProIPR005844. 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]
Gene3DG3DSA:3.40.120.10. A-D-PHexomutase_a/b/a-I/II/III. 3 hits.
KOK03431.
PfamPF02878. 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]
PRINTSPR00509. PGMPMM.
SUPFAMSSF53738. A-D-PHexomutase_a/b/a-I/II/III. 3 hits.
TIGRFAMsTIGR01455. GlmM. 1 hit.
PROSITEPS00710. PGM_PMM. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGLMM_ACIC1
AccessionPrimary (citable) accession number: A0LRQ7
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: December 12, 2006
Last modified: December 14, 2011
This is version 37 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families