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Reviewed, UniProtKB/Swiss-Prot A9KZX6 (GLMM1_SHEB9)

Last modified November 3, 2009. Version 14. 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 1
    EC=5.4.2.10
Gene names
Name: glmM1
Ordered Locus Names: Sbal195_3422
OrganismShewanella baltica (strain OS195) [Complete proteome] [HAMAP]
Taxonomic identifier399599 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella

Protein attributes

Sequence length445 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 – 445445Phosphoglucosamine mutase 1 HAMAP MF_01554
PRO_0000343599

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
A9KZX6-1 [UniParc].

Last modified February 5, 2008. Version 1.
Checksum: 6CD2C305F4A7A7BE

FASTA44547,643
        10         20         30         40         50         60 
MKERKFFGTD GIRGKVGSGQ MTPELALKLG WAAGRVLSRS GTKKVIIGKD TRISGYMFES 

        70         80         90        100        110        120 
ALEAGLSAAG LNVMLMGPMP TPAVAYLTRT FRAEAGVVIS ASHNPYYDNG IKFFSTDGSK 

       130        140        150        160        170        180 
LDDNLELEIE AELEKPLVCV ESHLLGKVSR IEDARGRYIE YCKGNFPAEH TLTGLKIVVD 

       190        200        210        220        230        240 
CAHGATYHIA PAVFRELGAE VIAIGDKPNG MNINDKVGAT SMGKICETVI AESADLGIAL 

       250        260        270        280        290        300 
DGDGDRIMMV NSKGEVIDGD QILYILACDA KSRGVLRGGV VGTLMSNLGL DLALQALDIP 

       310        320        330        340        350        360 
FARSKVGDRY VMELLKELDW RIGGENSGHI LNLDHGTTGD GIVAGILVLA AMRRQNATLE 

       370        380        390        400        410        420 
ELTSAMEMLP QVLVNVRFEG EHDPLKSDKV KAAQAQVESE LGVRGRVLLR KSGTEPLIRV 

       430        440 
MVEGDDHSAV LAHANLIADA VKSAS 

« Hide

References

[1]"Complete sequence of chromosome of Shewanella baltica OS195."
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E. expand/collapse author list , Brettar I., Rodrigues J., Konstantinidis K., Klappenbach J., Hofle M., Tiedje J., Richardson P.
Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000891 Genomic DNA. Translation: ABX50584.1.
RefSeqYP_001555844.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID5755228.
GenomeReviewsGene locus Sbal195_3422 in contig CP000891_GR.
KEGGsbn:Sbal195_3422.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAEPMKMLP.

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. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGLMM1_SHEB9
AccessionPrimary (citable) accession number: A9KZX6
Entry history
Integrated into UniProtKB/Swiss-Prot: July 22, 2008
Last sequence update: February 5, 2008
Last modified: November 3, 2009
This is version 14 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