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B8GXK7 (GLMM_CAUCN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 34. 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:CCNA_00116
OrganismCaulobacter crescentus (strain NA1000 / CB15N) [Complete proteome] [HAMAP]
Taxonomic identifier565050 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Caulobacterales › Caulobacteraceae › Caulobacter ›

Protein attributes

Sequence length448 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-Rule MF_01554

Catalytic activity

Alpha-D-glucosamine 1-phosphate = D-glucosamine 6-phosphate. HAMAP-Rule 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: HAMAP

phosphoglucosamine mutase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 448448Phosphoglucosamine mutase HAMAP-Rule MF_01554
PRO_1000185358

Sites

Active site1041Phosphoserine intermediate By similarity
Metal binding1041Magnesium; via phosphate group By similarity
Metal binding2451Magnesium By similarity
Metal binding2471Magnesium By similarity
Metal binding2491Magnesium By similarity

Amino acid modifications

Modified residue1041Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
B8GXK7 [UniParc].

Last modified March 3, 2009. Version 1.
Checksum: C1757B069A9DDF3D

FASTA44847,384
        10         20         30         40         50         60 
MSKRAYFGTD GIRGQANKHP MTAEVALRVG LAAGKLFRSQ DERRHLVVIG KDTRLSGYMI 

        70         80         90        100        110        120 
EPALVAGLTS VGLDVRLFGP LPTPAVAMMT RSMRADLGIM ISASHNSFAD NGIKLFGPDG 

       130        140        150        160        170        180 
YKLSDAQELG IEALMDQGLQ EGLAAPRELG RVKRIDDAQA RYVEIVKATF PRHLNLSGLR 

       190        200        210        220        230        240 
IVIDCANGAA YKVAPTALYE LGAEVITLGV SPDGTNINEE CGSTHPEAMA KMVREYRADI 

       250        260        270        280        290        300 
GIALDGDADR LVICDEKGVV VDGDQIMAII AAASHKAGTL KGGGVVATVM SNLGLERQLN 

       310        320        330        340        350        360 
TMGLSLERTA VGDRYVMQRM REGGFNVGGE QSGHLILSDF STTGDGLIAA LQVLAVMVET 

       370        380        390        400        410        420 
DKPMSALGRQ FEPVPQLLEN VRFVGGKPLE AAAVKEAIAD GEAQLNGAGR IVVRASGTEP 

       430        440 
LIRIMAEGDD PALVKKVVKS IASAVKAA

« Hide

References

[1]"The genetic basis of laboratory adaptation in Caulobacter crescentus."
Marks M.E., Castro-Rojas C.M., Teiling C., Du L., Kapatral V., Walunas T.L., Crosson S.
J. Bacteriol. 192:3678-3688(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NA1000 / CB15N.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP001340 Genomic DNA. Translation: ACL93583.1.
RefSeqYP_002515491.1. NC_011916.1.

3D structure databases

ProteinModelPortalB8GXK7.
SMRB8GXK7. Positions 6-447.
ModBaseSearch...

Protein-protein interaction databases

STRING190650.CC_0117.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACL93583; ACL93583; CCNA_00116.
GeneID7332370.
KEGGccs:CCNA_00116.
PATRIC21304797. VBICauCre52860_0115.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1109.
HOGENOMHOG000268678.
KOK03431.
OMASGHIILF.
ProtClustDBPRK14315.

Family and domain databases

Gene3D3.40.120.10. 3 hits.
HAMAPMF_01554_B. GlmM_B.
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.
IPR005841. Alpha-D-phosphohexomutase_SF.
IPR006352. GlmM.
[Graphical view]
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. 2 hits.
TIGRFAMsTIGR01455. glmM. 1 hit.
PROSITEPS00710. PGM_PMM. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGLMM_CAUCN
AccessionPrimary (citable) accession number: B8GXK7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 3, 2009
Last modified: May 1, 2013
This is version 34 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

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