Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q3J826 (GLMM_NITOC) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 42. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phosphoglucosamine mutase

EC=5.4.2.10
Gene names
Name:glmM
Ordered Locus Names:Noc_2567
OrganismNitrosococcus oceani (strain ATCC 19707 / NCIMB 11848) [Complete proteome] [HAMAP]
Taxonomic identifier323261 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaChromatialesChromatiaceaeNitrosococcus

Protein attributes

Sequence length451 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 – 451451Phosphoglucosamine mutase HAMAP MF_01554_B
PRO_0000147924

Sites

Active site1011Phosphoserine intermediate By similarity
Metal binding1011Magnesium; via phosphate group By similarity
Metal binding2401Magnesium By similarity
Metal binding2421Magnesium By similarity
Metal binding2441Magnesium By similarity

Amino acid modifications

Modified residue1011Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q3J826 [UniParc].

Last modified November 8, 2005. Version 1.
Checksum: B397B36A0A1C21CE

FASTA45148,284
        10         20         30         40         50         60 
MEKKYFGTDG IRGKVGERPI TPDFILHLGW AVGRVLAQGR QSKVLIGKDT RISGYMFESA 

        70         80         90        100        110        120 
LQAGLSAAGV DIRLLGPMPT PAIAYLTRTL HAKAGIVISA SHNPYYDNGI KFFSSAGTKL 

       130        140        150        160        170        180 
PDEIEVAIEA ELEKPMQTAT SSRLGKAERV VDAAGRYIEF CKSTGPASVD LSELRLVLDC 

       190        200        210        220        230        240 
AHGATYQVAP EVFAEMGADI TVIGASPNGL NINENCGSTA LESLQHKVLE CKADVGIALD 

       250        260        270        280        290        300 
GDGDRVIMID QRGEIVDGDD ILYIIARARQ RTSKLTGAVV GTLMSNLGLE KALATLGIPL 

       310        320        330        340        350        360 
MRSQVGDRYV LEMLQCNGYS LGGESSGHII CLDRTTTGDG IVSALQVLVE MVATGHSLYE 

       370        380        390        400        410        420 
LKSGVVKYPQ CLINVQVARS INLHDNNAII NAMQEAENQL GDEGRVLLRP SGTEPVVRVM 

       430        440        450 
VEGRDISQVN SLAQQLAQEV AFHLGNPQIC P 

« Hide

References

[1]"Complete genome sequence of the marine, chemolithoautotrophic, ammonia-oxidizing bacterium Nitrosococcus oceani ATCC 19707."
Klotz M.G., Arp D.J., Chain P.S.G., El-Sheikh A.F., Hauser L.J., Hommes N.G., Larimer F.W., Malfatti S.A., Norton J.M., Poret-Peterson A.T., Vergez L.M., Ward B.B.
Appl. Environ. Microbiol. 72:6299-6315(2006) [PubMed: 16957257] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 19707 / NCIMB 11848.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000127 Genomic DNA. Translation: ABA59020.1.
RefSeqYP_344550.1. NC_007484.1.

3D structure databases

ProteinModelPortalQ3J826.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ3J826.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3704571.
GenomeReviewsGene locus Noc_2567 in contig CP000127_GR.
KEGGnoc:Noc_2567.
NMPDRfig|323261.3.peg.2273.
PATRIC22709584. VBINitOce57959_2995.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1109.
HOGENOMHBG644964.
OMAPLEDIQV.
PhylomeDBQ3J826.
ProtClustDBCLSK741963.

Enzyme and pathway databases

BioCycNOCE323261:NOC_2567-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_NITOC
AccessionPrimary (citable) accession number: Q3J826
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: November 8, 2005
Last modified: January 25, 2012
This is version 42 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