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Reviewed, UniProtKB/Swiss-Prot A1TQF3 (GLMM_ACIAC)

Last modified November 3, 2009. Version 26. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Phosphoglucosamine mutase
    EC=5.4.2.10
Gene names
Name: glmM
Ordered Locus Names: Aave_2619
OrganismAcidovorax avenae subsp. citrulli (strain AAC00-1) [Complete proteome] [HAMAP]
Taxonomic identifier397945 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesComamonadaceaeAcidovorax

Protein attributes

Sequence length444 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Function

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

Catalytic activity

Alpha-D-glucosamine 1-phosphate = D-glucosamine 6-phosphate. HAMAP MF_01554

Cofactor

Binds 1 magnesium ion per subunit By similarity.

Post-translational modification

Activated by phosphorylation By similarity.

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: UniProtKB-KW

phosphoglucosamine mutase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 444444Phosphoglucosamine mutase HAMAP MF_01554
PRO_0000301269

Sites

Active site1021Phosphoserine intermediate By similarity
Metal binding1021Magnesium; via phosphate group By similarity
Metal binding2411Magnesium By similarity
Metal binding2431Magnesium By similarity
Metal binding2451Magnesium By similarity

Amino acid modifications

Modified residue1021Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
A1TQF3-1 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: 044A7934D870D436

FASTA44447,539
        10         20         30         40         50         60 
MARKYFGTDG IRGTVGQAPI TPDFVLRLAH AVGRVLRRTE ERPTVLIGKD TRISGYMLES 

        70         80         90        100        110        120 
ALESGFNSAG VDVVLLGPLP TPGVAYLTRA QRASLGVVIS ASHNAYPDNG IKFFSAQGTK 

       130        140        150        160        170        180 
LPDEWELAVE AALDEAPAWA DSASLGKARR LEDAAGRYIE FCKSTFSQDL TLKGTKIVVD 

       190        200        210        220        230        240 
AAHGAAYHIA PKVFHELGAE VLAIGCSPDG LNINHQVGAT HPDALVRAVR ANRADYGVAL 

       250        260        270        280        290        300 
DGDADRLQMV DAAGRLYNGD ELLYLLAADR LSRGENVPGV VGTLMTNMAV ELALKADGVE 

       310        320        330        340        350        360 
LVRAKVGDRY VLEELARRRW LLGGESSGHL LALDRHTTGD GLISALQVLQ ACVRGGRSLA 

       370        380        390        400        410        420 
RTLEHVRLFP QVLVNVRLLP GQDWKANTVL QDALKSVEAE LGTQGRVLVR ASGTEPLLRV 

       430        440 
MVETSDADRA SHFAHQLADA ARAG 

« Hide

References

[1]"Complete sequence of Acidovorax avenae subsp. citrulli AAC00-1."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Kim E., Stahl D., Richardson P.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000512 Genomic DNA. Translation: ABM33191.1.
RefSeqYP_970965.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGA1TQF3.

Genome annotation databases

GeneID4666593.
GenomeReviewsGene locus Aave_2619 in contig CP000512_GR.
KEGGaav:Aave_2619.
NMPDRfig|397945.5.peg.2246.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAAHAVGRV.

Family and domain databases

HAMAPMF_01554.
[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. A-D-PHexomutase_N.
IPR006352. GlmM.
[Graphical view]
Gene3DG3DSA:3.40.120.10. A-D-PHexomutase_a/b/a-I/II/III. 3 hits.
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.
TIGRFAMsTIGR01455. glmM. 1 hit.
PROSITEPS00710. PGM_PMM. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGLMM_ACIAC
AccessionPrimary (citable) accession number: A1TQF3
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: February 6, 2007
Last modified: November 3, 2009
This is version 26 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents