Reviewed, UniProtKB/Swiss-Prot Q4WY53 (PGM_ASPFU)

Names and origin

Protein names

Recommended name:
    Phosphoglucomutase
      Short name=PGM
    EC=5.4.2.2
Alternative name(s):
    Glucose phosphomutase

Gene names

Name:	pgmA
ORF Names:	AFUA_3G11830

Organism

Aspergillus fumigatus (Sartorya fumigata) [Complete proteome]

Taxonomic identifier

5085 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus

Protein attributes

Sequence length	555 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	This enzyme participates in both the breakdown and synthesis of glucose By similarity.
Catalytic activity	Alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate.
Cofactor	Binds 1 magnesium ion per subunit By similarity.
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the phosphohexose mutase family.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Glucose metabolism
Cellular component	Cytoplasm
Ligand	Magnesium Metal-binding
Molecular function	Isomerase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	glucose metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW phosphoglucomutase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 555	555	Phosphoglucomutase		PRO_0000228674
Sites
	Active site	114	1	Phosphoserine intermediate By similarity
	Metal binding	114	1	Magnesium; via phosphate group By similarity
	Metal binding	279	1	Magnesium By similarity
	Metal binding	281	1	Magnesium By similarity
	Metal binding	283	1	Magnesium By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q4WY53-1 [UniParc]. Last modified July 5, 2005. Version 1. Checksum: F4A9589EEACFCF4F	FASTA	555	60,501
	10 20 30 40 50 60 MSVQTVSIQP FTDQKPGTSG LRKKVKVFQQ PHYSEAFVTS ILLSIPEGAE GAFLVIGGDG 70 80 90 100 110 120 RYYNPEVIQK IAKISAAYGV KKLLIGQNGI LSTPAASNLI RVRKATGGIL LTASHNPGGP 130 140 150 160 170 180 NADFGIKYNL CNGAPAPESV TNKIYETSKS LTSYKIAEIP DVDTSTIGTK TYGPLEVEIV 190 200 210 220 230 240 HSTSDYLKML KEIFDFDLIK EFLSTHKDFK VLFDGMHGVT GPYGVDIFVK ELGLPQDSTM 250 260 270 280 290 300 NCVPSPDFNG GHPDPNLVYA HELVEAVDKK GIHFGAASDG DGDRNMIYGA NTFVSPGDSL 310 320 330 340 350 360 AIIAHHAKLI PWFQKQGVYG LARSMPTSGA VDLVAKAQGL QSYEVPTGWK FFCNLFDNKK 370 380 390 400 410 420 ISICGEESFG TGSNHIREKD GVWAIVAWLN IIAGVAKQKP NETPSIASIQ NEFWQTYGRT 430 440 450 460 470 480 FFTRYDYENV DSDAANKLIA NLSEKINNKD SFVGSTVSGR KVADAGNFAY TDLDGSVTKN 490 500 510 520 530 540 QGLYVKFDDG SRLVVRLSGT GSSGATIRLY IEKYESDKSK FGMNTQDYLK DNVALAMSLL 550 KFKEYIGRED PDVKT

References

[1]

"Genomic sequence of the pathogenic and allergenic filamentous fungus Aspergillus fumigatus." Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L. , Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N., Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K., Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E., Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A., Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D., O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R., Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.G., Denning D.W. Nature 438:1151-1156(2005) [PubMed: 16372009] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Af293 / CBS 101355 / FGSC A1100.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AAHF01000002 Genomic DNA. Translation: EAL92400.1.
RefSeq	XP_754438.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q4WY53.
Genome annotation databases
GeneID	3511873.
GenomeReviews	Gene locus pgmA in contig CM000171_GR.
KEGG	afm:AFUA_3G11830.
Phylogenomic databases
HOGENOM	Q4WY53.
OMA	YMKEAIQ.
Enzyme and pathway databases
BRENDA	5.4.2.2. 18841.
Family and domain databases
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. A-D-PHexomutase_N. [Graphical view]
Gene3D	G3DSA:3.40.120.10. A-D-PHexomutase_a/b/a-I/II/III. 3 hits.
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.
PROSITE	PS00710. PGM_PMM. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PGM_ASPFU

Accession

Primary (citable) accession number: Q4WY53

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 21, 2006
Last sequence update:	July 5, 2005
Last modified:	November 3, 2009
This is version 31 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)