Q9P4V2 (AGM1_CANAX) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Alternative name(s):
Acetylglucosamine phosphomutase
N-acetylglucosamine-phosphate mutase

Gene names

Name:

AGM1

Organism

Candida albicans (Yeast)

Taxonomic identifier

5476 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › mitosporic Saccharomycetales › Candida

Protein attributes

Sequence length	544 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Interconverts GlcNAc-6-P and GlcNAc-1-P.
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	3D-structure
Gene Ontology (GO)
Biological_process	UDP-N-acetylglucosamine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro
Molecular_function	magnesium ion binding Inferred from electronic annotation. Source: InterPro 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 – 544

544

Phosphoacetylglucosamine mutase

PRO_0000148016

Sites

Active site

66

1

Phosphoserine intermediate By similarity

Metal binding

66

1

Magnesium; via phosphate group By similarity

Metal binding

290

1

Magnesium By similarity

Metal binding

292

1

Magnesium By similarity

Metal binding

294

1

Magnesium By similarity

Experimental info

Sequence conflict

238

1

K → R in AAF64520. Ref.2

Sequence conflict

308

1

K → N in AAF64520. Ref.2

Sequence conflict

350

1

S → Y in AAF64520. Ref.2

Secondary structure

1

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544

Helix Strand Turn

Details...

Helix

3 – 8

6

Helix

11 – 13

3

Beta strand

28 – 32

5

Helix

33 – 35

3

Helix

37 – 53

17

Turn

54 – 56

3

Beta strand

58 – 63

6

Beta strand

72 – 78

7

Beta strand

82 – 84

3

Helix

87 – 89

3

Helix

90 – 98

9

Beta strand

99 – 101

3

Helix

114 – 124

11

Beta strand

133 – 139

7

Helix

145 – 157

13

Beta strand

159 – 169

11

Helix

172 – 183

12

Helix

185 – 187

3

Helix

192 – 207

16

Beta strand

217 – 222

6

Helix

228 – 239

12

Turn

241 – 243

3

Beta strand

244 – 250

7

Helix

256 – 258

3

Turn

259 – 262

4

Helix

265 – 271

7

Beta strand

286 – 289

4

Beta strand

296 – 301

6

Beta strand

307 – 310

4

Helix

312 – 327

16

Turn

332 – 334

3

Beta strand

339 – 343

5

Helix

349 – 357

9

Beta strand

363 – 365

3

Helix

370 – 377

8

Beta strand

380 – 386

7

Beta strand

392 – 396

5

Helix

398 – 406

9

Helix

412 – 427

16

Beta strand

430 – 432

3

Helix

435 – 448

14

Helix

453 – 457

5

Beta strand

465 – 470

6

Helix

475 – 477

3

Beta strand

479 – 481

3

Turn

482 – 484

3

Beta strand

486 – 490

5

Helix

493 – 501

9

Beta strand

508 – 513

6

Beta strand

520 – 525

6

Helix

529 – 543

15

Sequences

	Sequence		Length	Mass (Da)
	Q9P4V2 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: B022662342FA6D58	FASTA	544	60,478
	10 20 30 40 50 60 MSIEQTLSQY LPSHPKPQGV TFTYGTAGFR MKADKLDYVT FTVGIIASLR SKYLQGKTVG 70 80 90 100 110 120 VMITASHNPP EDNGVKVVDP LGSMLESSWE KYATDLANAS PSPSNDSEGE KNSLVEVIKN 130 140 150 160 170 180 LVSDLKIDLS IPANVVIARD SRESSPALSM ATIDGFQSVP NTKYQDFGLF TTPELHYVTR 190 200 210 220 230 240 TLNDPDFGKP TEDGYYSKLA KSFQEIYTIC ESNNEKIDIT IDAANGVGAP KIQELLEKYL 250 260 270 280 290 300 HKEISFTVVN GDYKQPNLLN FDCGADYVKT NQKLPKNVKP VNNKLYASFD GDADRLICYY 310 320 330 340 350 360 QNNDNKFKLL DGDKLSTLFA LFLQQLFKQI DPTKISLNIG VVQTAYANGS STKYVEDVLK 370 380 390 400 410 420 IPVRCTPTGV KHLHHEAENF DIGVYFEANG HGTVIFNPEA EKKIFDYKPN NDNEAKAIKV 430 440 450 460 470 480 LQNFSQLINQ TVGDAISDLL AVLIVVHYLK LSPSDWDNEY TDLPNKLVKV IVPDRSIFKT 490 500 510 520 530 540 TNAERTLVEP KGMQDEIDKL VAQYPNGRSF VRASGTEDAV RVYAEADTQN NVEELSKAVS ELVK

References

[1]	"Functional cloning and mutational analysis of the human cDNA for phosphoacetylglucosamine mutase: identification of the amino acid residues essential for the catalysis." Mio T., Yamada-Okabe T., Arisawa M., Yamada-Okabe H. Biochim. Biophys. Acta 1492:369-376(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Identification and isolation of Candida albicans AGM1." Spettel C., Eschrich D., Koetter P., Entian K. Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AB032082 Genomic DNA. Translation: BAB00614.1.
AF253056 Genomic DNA. Translation: AAF64520.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2DKA	X-ray	1.93	A/B	1-544	[»]
2DKC	X-ray	2.20	A/B	1-544	[»]
2DKD	X-ray	2.10	A/B	1-544	[»]

ProteinModelPortal

Q9P4V2.

SMR

Q9P4V2. Positions 1-544.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Phylogenomic databases

eggNOG

COG1109.

Enzyme and pathway databases

BRENDA

5.4.2.3. 1096.

UniPathway

UPA00113; UER00530.

Family and domain databases

Gene3D

3.40.120.10. 3 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.
IPR005843. A-D-PHexomutase_C.
IPR016066. A-D-PHexomutase_CS.
IPR016657. PAGM.
[Graphical view]

PANTHER

PTHR22573:SF3. PTHR22573:SF3. 1 hit.

Pfam

PF02878. PGM_PMM_I. 2 hits.
PF02879. PGM_PMM_II. 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. 4 hits.

PROSITE

PS00710. PGM_PMM. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q9P4V2.

Entry information

Entry name

AGM1_CANAX

Accession

Primary (citable) accession number: Q9P4V2
Secondary accession number(s): Q9P8H8

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 24, 2001
Last sequence update:	October 1, 2000
Last modified:	April 3, 2013
This is version 68 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program