Reviewed, UniProtKB/Swiss-Prot Q09687 (AGM1_SCHPO)

Names and origin

Protein names

Recommended name:
    Probable phosphoacetylglucosamine mutase 1
      Short name=PAGM
    EC=5.4.2.3
Alternative name(s):
    Acetylglucosamine phosphomutase
    N-acetylglucosamine-phosphate mutase

Gene names

ORF Names:

SPAC13C5.05c

Organism

Schizosaccharomyces pombe (Fission yeast) [Complete proteome]

Taxonomic identifier

4896 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	518 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.

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
Cellular component	cytosol Inferred from direct assay. Source: GeneDB_SPombe nucleus Inferred from direct assay. Source: GeneDB_SPombe
Molecular function	magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW phosphoacetylglucosamine mutase 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 – 518	518	Probable phosphoacetylglucosamine mutase 1		PRO_0000148017
Sites
	Active site	51	1	Phosphoserine intermediate By similarity
	Metal binding	51	1	Magnesium; via phosphate group By similarity
	Metal binding	267	1	Magnesium By similarity
	Metal binding	269	1	Magnesium By similarity
	Metal binding	271	1	Magnesium By similarity
Amino acid modifications
	Modified residue	49	1	Phosphothreonine Ref.2
	Modified residue	51	1	Phosphoserine Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q09687-1 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: DA8ACB0008C29594	FASTA	518	56,347
	10 20 30 40 50 60 MTKNKKYSYG TAGFRTKASD LEAAVYSSGV AAALRSMELK GKTIGVMITA SHNPVEDNGV 70 80 90 100 110 120 KIIDADGGML AMEWEDKCTQ LANAPSKAEF DFLIKQFLTP TTCQPKVIIG YDTRPSSPRL 130 140 150 160 170 180 AELLKVCLDE MSASYIDYGY ITTPQLHWLV RLINKSTAAS FLEEGPPITE YYDTLTSAFS 190 200 210 220 230 240 KIDPSMQDSP TVSRVVVDCA NGVGSQPLKT VAGLVKDSLS IELVNTDVRA SELLNNGCGA 250 260 270 280 290 300 DFVKTKQSPP LALEGKIKPN QLYASIDGDA DRLIFYYINQ NRKFHLLDGD KISTALVGYL 310 320 330 340 350 360 NILVKKSGMP FSLGVVQTAY ANGASTEYLQ DLGITTVFTP TGVKHLHKAA KEFDIGVYFE 370 380 390 400 410 420 ANGHGTVLFS DKALANLAHP FFTPSPVQAA AIEQLQSYSV LINQAIGDAI SDLLATISVL 430 440 450 460 470 480 NALHWDASAW SNTYKDLPNK LAKVKVSDRT IYKSTDAERR LVSPDGLQEK IDALVAKYEK 490 500 510 GRSFVRASGT EDVVRVYAEA STKQAADELC EKVCQLVL

References

[1]

"The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P. Nature 415:871-880(2002) [PubMed: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 38366 / 972.

[2]

"Phosphoproteome analysis of fission yeast." Wilson-Grady J.T., Villen J., Gygi S.P. J. Proteome Res. 7:1088-1097(2008) [PubMed: 18257517] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-49 AND SER-51, MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBLGenBankDDBJ	CU329670 Genomic DNA. Translation: CAA90456.1.
PIR	S59642.
RefSeq	NP_592933.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q09687.
Genome annotation databases
GeneID	2542320.
KEGG	spo:SPAC13C5.05c.
NMPDR	fig|4896.1.peg.2903.
Organism-specific databases
GeneDB_Spombe	SPAC13C5.05c.
Phylogenomic databases
OMA	NLHPIAH.
Enzyme and pathway databases
BioCyc	SPOM-XXX-01:SPOM-XXX-01-000663-MON.
BRENDA	5.4.2.3. 653.
Gene expression databases
ArrayExpress	Q09687.
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. IPR005843. A-D-PHexomutase_C. IPR016066. A-D-PHexomutase_CS. IPR016657. PAGM. [Graphical view]
Gene3D	G3DSA:3.40.120.10. A-D-PHexomutase_a/b/a-I/II/III. 1 hit.
Pfam	PF02878. PGM_PMM_I. 1 hit. PF02879. PGM_PMM_II. 1 hit. PF00408. PGM_PMM_IV. 1 hit. [Graphical view]
PIRSF	PIRSF016408. PAGM. 1 hit.
PROSITE	PS00710. PGM_PMM. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

AGM1_SCHPO

Accession

Primary (citable) accession number: Q09687

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	November 3, 2009
This is version 68 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)