C1DFL3 (GLMM_AZOVD) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Phosphoglucosamine mutase
EC=5.4.2.10

Gene names

Name:	glmM
Ordered Locus Names:	Avin_42860

Organism

Azotobacter vinelandii (strain DJ / ATCC BAA-1303) [Complete proteome] [HAMAP]

Taxonomic identifier

322710 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Azotobacter group › Azotobacter › Azotobacter vinelandii

Protein attributes

Sequence length	445 AA.
Sequence status	Complete.
Protein existence	Inferred 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
Ligand	Magnesium Metal-binding
Molecular function	Isomerase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro
Molecular_function	magnesium ion binding Inferred from electronic annotation. Source: HAMAP phosphoglucosamine mutase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 445	445	Phosphoglucosamine mutase HAMAP-Rule MF_01554		PRO_1000215482
Sites
	Active site	101	1	Phosphoserine intermediate By similarity
	Metal binding	101	1	Magnesium; via phosphate group By similarity
	Metal binding	240	1	Magnesium By similarity
	Metal binding	242	1	Magnesium By similarity
	Metal binding	244	1	Magnesium By similarity
Amino acid modifications
	Modified residue	101	1	Phosphoserine By similarity

Sequences

	Sequence		Length	Mass (Da)
	C1DFL3 [UniParc]. Last modified May 26, 2009. Version 1. Checksum: 62B91A833CF5A690	FASTA	445	47,899
	10 20 30 40 50 60 MSKKYFGTDG IRGRVGEYPI TPDFMLKLGW AAGKAFRRQG ICRVLVGKDT RISGYMFESV 70 80 90 100 110 120 LEAGLSAAGA DVLLLGPMPT PAIAYLTRTF HAEAGIVISA SHNPHYDNGI KFFSGQGTKL 130 140 150 160 170 180 PDELELVIEE LLDNPMTVVD SAQLGKVSRI NDAAGRYIEF CKSSVPTGTS FAGLKMVVDC 190 200 210 220 230 240 AHGATYKVAP NVFRELGAEV AVLAAQPNGL NINDRCGSTD IVALQAEVLM QRADLGVAFD 250 260 270 280 290 300 GDGDRVLMVD HTGAVVDGDE LLFLIARDMH EHGKLQGGVV GTLMSNLGLE LALQDMGIPF 310 320 330 340 350 360 VRAKVGDRYV MAELLARNWQ LGGEGSGHIV CCHHSTTGDG IIAALQVLRA LKHRGQRLAE 370 380 390 400 410 420 ARQGMRKFPQ VLVNVRYAGD KDPVGHPVVQ EACERVTEQM AGRGRVLLRK SGTEPLVRVM 430 440 VEGDDESQVR LHADNLAKIV SDVCA

References

[1]

"Genome sequence of Azotobacter vinelandii, an obligate aerobe specialized to support diverse anaerobic metabolic processes." Setubal J.C., Dos Santos P., Goldman B.S., Ertesvaag H., Espin G., Rubio L.M., Valla S., Almeida N.F., Balasubramanian D., Cromes L., Curatti L., Du Z., Godsy E., Goodner B., Hellner-Burris K., Hernandez J.A., Houmiel K., Imperial J. , Kennedy C., Larson T.J., Latreille P., Ligon L.S., Lu J., Maerk M., Miller N.M., Norton S., O'Carroll I.P., Paulsen I., Raulfs E.C., Roemer R., Rosser J., Segura D., Slater S., Stricklin S.L., Studholme D.J., Sun J., Viana C.J., Wallin E., Wang B., Wheeler C., Zhu H., Dean D.R., Dixon R., Wood D. J. Bacteriol. 191:4534-4545(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: DJ / ATCC BAA-1303.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP001157 Genomic DNA. Translation: ACO80409.1.
RefSeq	YP_002801384.1. NC_012560.1.
3D structure databases
ProteinModelPortal	C1DFL3.
ModBase	Search...
Protein-protein interaction databases
STRING	322710.Avin_42860.
Proteomic databases
PRIDE	C1DFL3.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ACO80409; ACO80409; Avin_42860.
GeneID	7763161.
KEGG	avn:Avin_42860.
PATRIC	21034606. VBIAzoVin72790_4034.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1109.
HOGENOM	HOG000268678.
KO	K03431.
OMA	TLMSNMS.
ProtClustDB	PRK10887.
Enzyme and pathway databases
BioCyc	AVIN322710:GJ0M-4290-MONOMER.
Family and domain databases
Gene3D	3.40.120.10. 3 hits.
HAMAP	MF_01554_B. GlmM_B.
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. IPR016066. A-D-PHexomutase_CS. IPR005841. Alpha-D-phosphohexomutase_SF. IPR006352. GlmM. [Graphical view]
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]
PRINTS	PR00509. PGMPMM.
SUPFAM	SSF53738. A-D-PHexomutase_a/b/a-I/II/III. 3 hits.
TIGRFAMs	TIGR01455. glmM. 1 hit.
PROSITE	PS00710. PGM_PMM. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GLMM_AZOVD

Accession

Primary (citable) accession number: C1DFL3

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 22, 2009
Last sequence update:	May 26, 2009
Last modified:	May 1, 2013
This is version 31 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program