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Protein

Phosphoacetylglucosamine mutase

Gene

AGM1

Organism
Candida albicans (Yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the conversion of GlcNAc-6-P into GlcNAc-1-P during the synthesis of uridine diphosphate/UDP-GlcNAc, which is a biosynthetic precursor of chitin and also supplies the amino sugars for N-linked oligosaccharides of glycoproteins.1 Publication

Catalytic activityi

N-acetyl-alpha-D-glucosamine 1-phosphate = N-acetyl-D-glucosamine 6-phosphate.1 Publication

Cofactori

Mg2+1 PublicationNote: Binds 1 Mg2+ ion per subunit.1 Publication

Pathwayi: UDP-N-acetyl-alpha-D-glucosamine biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route I).1 Publication
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Glucosamine 6-phosphate N-acetyltransferase (GNA1)
  2. Phosphoacetylglucosamine mutase (AGM1)
This subpathway is part of the pathway UDP-N-acetyl-alpha-D-glucosamine biosynthesis, which is itself part of Nucleotide-sugar biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route I), the pathway UDP-N-acetyl-alpha-D-glucosamine biosynthesis and in Nucleotide-sugar biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei66Phosphoserine intermediate1 Publication1
Metal bindingi66Magnesium; via phosphate group1 Publication1
Metal bindingi290Magnesium1 Publication1
Metal bindingi292Magnesium1 Publication1
Metal bindingi294Magnesium1 Publication1
Binding sitei521Substrate1 Publication1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Carbohydrate metabolism, Cell wall biogenesis/degradation

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BRENDAi5.4.2.3. 1096.
UniPathwayiUPA00113; UER00530.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphoacetylglucosamine mutase1 Publication (EC:5.4.2.31 Publication)
Short name:
PAGM
Alternative name(s):
Acetylglucosamine phosphomutase
N-acetylglucosamine-phosphate mutase1 Publication
Gene namesi
Name:AGM11 Publication
OrganismiCandida albicans (Yeast)
Taxonomic identifieri5476 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeCandida/Lodderomyces cladeCandida

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001480161 – 544Phosphoacetylglucosamine mutaseAdd BLAST544

Keywords - PTMi

Phosphoprotein

Structurei

Secondary structure

1544
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi3 – 8Combined sources6
Helixi11 – 13Combined sources3
Beta strandi28 – 32Combined sources5
Helixi33 – 35Combined sources3
Helixi37 – 53Combined sources17
Turni54 – 56Combined sources3
Beta strandi58 – 63Combined sources6
Beta strandi72 – 78Combined sources7
Beta strandi82 – 84Combined sources3
Helixi87 – 89Combined sources3
Helixi90 – 98Combined sources9
Beta strandi99 – 101Combined sources3
Helixi114 – 124Combined sources11
Beta strandi133 – 139Combined sources7
Helixi145 – 157Combined sources13
Beta strandi159 – 169Combined sources11
Helixi172 – 183Combined sources12
Helixi185 – 187Combined sources3
Helixi192 – 207Combined sources16
Beta strandi217 – 222Combined sources6
Helixi228 – 239Combined sources12
Turni241 – 243Combined sources3
Beta strandi244 – 250Combined sources7
Helixi256 – 258Combined sources3
Turni259 – 262Combined sources4
Helixi265 – 271Combined sources7
Beta strandi286 – 289Combined sources4
Beta strandi296 – 301Combined sources6
Beta strandi307 – 310Combined sources4
Helixi312 – 327Combined sources16
Turni332 – 334Combined sources3
Beta strandi339 – 343Combined sources5
Helixi349 – 357Combined sources9
Beta strandi363 – 365Combined sources3
Helixi370 – 377Combined sources8
Beta strandi380 – 386Combined sources7
Beta strandi392 – 396Combined sources5
Helixi398 – 406Combined sources9
Helixi412 – 427Combined sources16
Beta strandi430 – 432Combined sources3
Helixi435 – 448Combined sources14
Helixi453 – 457Combined sources5
Beta strandi465 – 470Combined sources6
Helixi475 – 477Combined sources3
Beta strandi479 – 481Combined sources3
Turni482 – 484Combined sources3
Beta strandi486 – 490Combined sources5
Helixi493 – 501Combined sources9
Beta strandi508 – 513Combined sources6
Beta strandi520 – 525Combined sources6
Helixi529 – 543Combined sources15

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2DKAX-ray1.93A/B1-544[»]
2DKCX-ray2.20A/B1-544[»]
2DKDX-ray2.10A/B1-544[»]
ProteinModelPortaliQ9P4V2.
SMRiQ9P4V2.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9P4V2.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni387 – 389Substrate binding1 Publication3
Regioni512 – 516Substrate binding1 Publication5

Sequence similaritiesi

Belongs to the phosphohexose mutase family.Curated

Family and domain databases

CDDicd03086. PGM3. 1 hit.
Gene3Di3.30.310.50. 1 hit.
3.40.120.10. 4 hits.
InterProiIPR005844. A-D-PHexomutase_a/b/a-I.
IPR016055. A-D-PHexomutase_a/b/a-I/II/III.
IPR005843. A-D-PHexomutase_C.
IPR016066. A-D-PHexomutase_CS.
IPR016657. PAGM.
[Graphical view]
PfamiPF02878. PGM_PMM_I. 2 hits.
PF00408. PGM_PMM_IV. 1 hit.
[Graphical view]
PIRSFiPIRSF016408. PAGM. 1 hit.
SUPFAMiSSF53738. SSF53738. 3 hits.
SSF55957. SSF55957. 1 hit.
PROSITEiPS00710. PGM_PMM. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9P4V2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSIEQTLSQY LPSHPKPQGV TFTYGTAGFR MKADKLDYVT FTVGIIASLR
60 70 80 90 100
SKYLQGKTVG VMITASHNPP EDNGVKVVDP LGSMLESSWE KYATDLANAS
110 120 130 140 150
PSPSNDSEGE KNSLVEVIKN LVSDLKIDLS IPANVVIARD SRESSPALSM
160 170 180 190 200
ATIDGFQSVP NTKYQDFGLF TTPELHYVTR TLNDPDFGKP TEDGYYSKLA
210 220 230 240 250
KSFQEIYTIC ESNNEKIDIT IDAANGVGAP KIQELLEKYL HKEISFTVVN
260 270 280 290 300
GDYKQPNLLN FDCGADYVKT NQKLPKNVKP VNNKLYASFD GDADRLICYY
310 320 330 340 350
QNNDNKFKLL DGDKLSTLFA LFLQQLFKQI DPTKISLNIG VVQTAYANGS
360 370 380 390 400
STKYVEDVLK IPVRCTPTGV KHLHHEAENF DIGVYFEANG HGTVIFNPEA
410 420 430 440 450
EKKIFDYKPN NDNEAKAIKV LQNFSQLINQ TVGDAISDLL AVLIVVHYLK
460 470 480 490 500
LSPSDWDNEY TDLPNKLVKV IVPDRSIFKT TNAERTLVEP KGMQDEIDKL
510 520 530 540
VAQYPNGRSF VRASGTEDAV RVYAEADTQN NVEELSKAVS ELVK
Length:544
Mass (Da):60,478
Last modified:October 1, 2000 - v1
Checksum:iB022662342FA6D58
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti238K → R in AAF64520 (Ref. 2) Curated1
Sequence conflicti308K → N in AAF64520 (Ref. 2) Curated1
Sequence conflicti350S → Y in AAF64520 (Ref. 2) Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB032082 Genomic DNA. Translation: BAB00614.1.
AF253056 Genomic DNA. Translation: AAF64520.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB032082 Genomic DNA. Translation: BAB00614.1.
AF253056 Genomic DNA. Translation: AAF64520.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2DKAX-ray1.93A/B1-544[»]
2DKCX-ray2.20A/B1-544[»]
2DKDX-ray2.10A/B1-544[»]
ProteinModelPortaliQ9P4V2.
SMRiQ9P4V2.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00113; UER00530.
BRENDAi5.4.2.3. 1096.

Miscellaneous databases

EvolutionaryTraceiQ9P4V2.

Family and domain databases

CDDicd03086. PGM3. 1 hit.
Gene3Di3.30.310.50. 1 hit.
3.40.120.10. 4 hits.
InterProiIPR005844. A-D-PHexomutase_a/b/a-I.
IPR016055. A-D-PHexomutase_a/b/a-I/II/III.
IPR005843. A-D-PHexomutase_C.
IPR016066. A-D-PHexomutase_CS.
IPR016657. PAGM.
[Graphical view]
PfamiPF02878. PGM_PMM_I. 2 hits.
PF00408. PGM_PMM_IV. 1 hit.
[Graphical view]
PIRSFiPIRSF016408. PAGM. 1 hit.
SUPFAMiSSF53738. SSF53738. 3 hits.
SSF55957. SSF55957. 1 hit.
PROSITEiPS00710. PGM_PMM. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiAGM1_CANAX
AccessioniPrimary (citable) accession number: Q9P4V2
Secondary accession number(s): Q9P8H8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: October 1, 2000
Last modified: November 30, 2016
This is version 82 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.