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A4Y9C5 (GLMM_SHEPC) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 44. 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:Sputcn32_2839
OrganismShewanella putrefaciens (strain CN-32 / ATCC BAA-453) [Complete proteome] [HAMAP]
Taxonomic identifier319224 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella

Protein attributes

Sequence length445 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 – 445445Phosphoglucosamine mutase HAMAP-Rule MF_01554
PRO_1000068916

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
A4Y9C5 [UniParc].

Last modified May 29, 2007. Version 1.
Checksum: F52A14AF9738F8B5

FASTA44547,684
        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 SMGKICETVL AESADLGIAL 

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

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

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

       430        440 
MVEGDDHSAV LAHANLIADA VKSAS 

« Hide

References

[1]"Complete sequence of Shewanella putrefaciens CN-32."
US DOE Joint Genome Institute
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., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Mikhailova N., Romine M.F., Fredrickson J., Tiedje J., Richardson P.
Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CN-32 / ATCC BAA-453.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000681 Genomic DNA. Translation: ABP76558.1.
RefSeqYP_001184357.1. NC_009438.1.

3D structure databases

ProteinModelPortalA4Y9C5.
ModBaseSearch...

Protein-protein interaction databases

STRING319224.Sputcn32_2839.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABP76558; ABP76558; Sputcn32_2839.
GeneID5078673.
KEGGspc:Sputcn32_2839.
PATRIC23554650. VBIShePut135485_2967.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1109.
HOGENOMHOG000268678.
KOK03431.
OMATRINDAT.
ProtClustDBPRK10887.

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.
IPR016066. A-D-PHexomutase_CS.
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. 3 hits.
TIGRFAMsTIGR01455. glmM. 1 hit.
PROSITEPS00710. PGM_PMM. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGLMM_SHEPC
AccessionPrimary (citable) accession number: A4Y9C5
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: May 29, 2007
Last modified: May 1, 2013
This is version 44 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