Phosphoacetylglucosamine mutase - Arabidopsis thaliana (Mouse-ear cress)

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P57750 (AGM1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 101. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Phosphoacetylglucosamine mutase
Short name=PAGM
EC=5.4.2.3

Alternative name(s):
Acetylglucosamine phosphomutase
DNA-damage-repair/toleration protein DRT101
N-acetylglucosamine-phosphate mutase

Gene names

Name:	DRT101
Ordered Locus Names:	At5g18070
ORF Names:	MRG7.2

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	556 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Interconverts GlcNAc-6-P and GlcNAc-1-P By similarity.
Catalytic activity	N-acetyl-alpha-D-glucosamine 1-phosphate = N-acetyl-D-glucosamine 6-phosphate.
Cofactor	Binds 1 magnesium ion per subunit By similarity.
Pathway	Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route I): step 2/2.
Sequence similarities	Belongs to the phosphohexose mutase family.
Sequence caution	The sequence AAA72352.1 differs from that shown. Reason: Sequencing errors.

Ontologies

Keywords
Biological process	DNA damage DNA repair
Ligand	Magnesium Metal-binding
Molecular function	Isomerase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	UDP-N-acetylglucosamine biosynthetic process Inferred from Biological aspect of Ancestor. Source: RefGenome carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro glucose 1-phosphate metabolic process Inferred from Biological aspect of Ancestor. Source: RefGenome photoreactive repair Inferred from genetic interaction Ref.4. Source: TAIR response to UV Inferred from genetic interaction Ref.4. Source: TAIR
Cellular_component	cytosol Inferred from direct assay Ref.5. Source: TAIR mitochondrion Inferred from direct assay PubMed 14671022. Source: TAIR plasmodesma Inferred from direct assay PubMed 21533090. Source: TAIR
Molecular_function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW phosphoacetylglucosamine mutase activity Inferred from Biological aspect of Ancestor. Source: RefGenome phosphoglucomutase activity Inferred from Biological aspect of Ancestor. Source: RefGenome
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 556

556

Phosphoacetylglucosamine mutase

PRO_0000148015

Sites

Active site

Phosphoserine intermediate By similarity

Metal binding

Magnesium; via phosphate group By similarity

Metal binding

286

Magnesium By similarity

Metal binding

288

Magnesium By similarity

Metal binding

290

Magnesium By similarity

Amino acid modifications

Modified residue

Phosphoserine Ref.5

Sequences

Sequence

Length

Mass (Da)

Tools

P57750 [UniParc].

Last modified January 24, 2001. Version 1.
Checksum: BCADE44F14DDC3D0
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FASTA

556

60,391

        10         20         30         40         50         60 
MDEIQIASIL KSSELFPIPQ GVKLSYGTAG FRGDAKLLES TVYRVGILSA LRSLKLGSAT 

        70         80         90        100        110        120 
VGLMITASHN KVSDNGIKVS DPSGFMLSQE WEPFADQIAN ASSPEELVSL IRKFMEKEEI 

       130        140        150        160        170        180 
AIGENNKGAE VWLGRDTRPS GESLLRAGEI GVGSILGSVA IDIGILTTPQ LHWMVRAKNK 

       190        200        210        220        230        240 
GLKATENDYF ENLSTSFRCL IDLIPSSGND KLEISKLLVD GANGVGGQKI EKLRGSLSNL 

       250        260        270        280        290        300 
DVEIRNTGRD GGVLNEGVGA DFVQKEKVLP VGFGFKDVGM RCASLDGDAD RLVYFYIPSD 

       310        320        330        340        350        360 
SSEKVELLDG DKILSLFALF IKEQLNALED DEERKQSRLG VVQTAYANGA STDYLKHLGL 

       370        380        390        400        410        420 
DVVFAKTGVK HLHEKAAEFD IGIYFEANGH GTILFSESFL SWLVSKQKDL TAKGQGGSEE 

       430        440        450        460        470        480 
HKAVSRLMAV SNLINQAVGD ALSGVLLVEV ILQHLGWSIE KWNELYKDLP SRQIKVEVPD 

       490        500        510        520        530        540 
RTAVVTTSEE TEALRPMGIQ DAINSEIKKY SRGRAFIRPS GTEDVVRVYA EASTQEDADS 

       550 
LANSVAQLVK SFLGSS

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence features of the regions of 1,367,185 bp covered by 19 physically assigned P1 and TAC clones." Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N., Tabata S. DNA Res. 5:203-216(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[2]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[3]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. Ecker J.R. Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[4]	"Selection of Arabidopsis cDNAs that partially correct phenotypes of Escherichia coli DNA-damage-sensitive mutants and analysis of two plant cDNAs that appear to express UV-specific dark repair activities." Pang Q., Hays J.B., Rajagopal I., Schaefer T.S. Plant Mol. Biol. 22:411-426(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 183-556. Strain: cv. Columbia.
[5]	"Site-specific phosphorylation profiling of Arabidopsis proteins by mass spectrometry and peptide chip analysis." de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E., Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C., Lorkovic Z.J., Barta A., Lecourieux D., Verhounig A., Jonak C., Hirt H. J. Proteome Res. 7:2458-2470(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68, MASS SPECTROMETRY. Tissue: Root.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB012246 Genomic DNA. Translation: BAB09465.1. CP002688 Genomic DNA. Translation: AED92503.1. AY075620 mRNA. Translation: AAL91631.1. L11367 mRNA. Translation: AAA72352.1. Sequence problems.
IPI	IPI00520298.
PIR	S35270.
RefSeq	NP_568359.2. NM_121812.2.
UniGene	At.466.
3D structure databases
ProteinModelPortal	P57750.
SMR	P57750. Positions 127-179, 465-554.
ModBase	Search...
Protein-protein interaction databases
STRING	3702.AT5G18070.1-P.
Proteomic databases
PaxDb	P57750.
PRIDE	P57750.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT5G18070.1; AT5G18070.1; AT5G18070.
GeneID	831926.
KEGG	ath:AT5G18070.
Organism-specific databases
TAIR	At5g18070.
Phylogenomic databases
eggNOG	COG1109.
HOGENOM	HOG000210027.
InParanoid	P57750.
KO	K01836.
OMA	DIVRVYA.
PhylomeDB	P57750.
ProtClustDB	PLN02895.
Enzyme and pathway databases
UniPathway	UPA00113; UER00530.
Gene expression databases
Genevestigator	P57750.
GermOnline	AT5G18070. Arabidopsis thaliana.
Family and domain databases
Gene3D	3.40.120.10. 2 hits.
InterPro	IPR005844. 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. IPR016657. PAGM. [Graphical view]
PANTHER	PTHR22573:SF3. PTHR22573:SF3. 1 hit.
Pfam	PF02878. 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]
PIRSF	PIRSF016408. PAGM. 1 hit.
SUPFAM	SSF53738. A-D-PHexomutase_a/b/a-I/II/III. 3 hits.
PROSITE	PS00710. PGM_PMM. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

AGM1_ARATH

Accession

Primary (citable) accession number: P57750
Secondary accession number(s): Q05211

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 24, 2001
Last sequence update:	January 24, 2001
Last modified:	May 1, 2013
This is version 101 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents