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Q9P4V2

- AGM1_CANAX

UniProt

Q9P4V2 - AGM1_CANAX

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Protein

Phosphoacetylglucosamine mutase

Gene

AGM1

Organism
Candida albicans (Yeast)
Status
Reviewed - Annotation score: 3 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 Mg(2+) ion per subunit.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei66 – 661Phosphoserine intermediate1 Publication
Metal bindingi66 – 661Magnesium; via phosphate group1 Publication
Metal bindingi290 – 2901Magnesium1 Publication
Metal bindingi292 – 2921Magnesium1 Publication
Metal bindingi294 – 2941Magnesium1 Publication
Binding sitei521 – 5211Substrate1 Publication

GO - Molecular functioni

  1. magnesium ion binding Source: InterPro
  2. phosphoacetylglucosamine mutase activity Source: UniProtKB-EC

GO - Biological processi

  1. carbohydrate metabolic process Source: InterPro
  2. UDP-N-acetylglucosamine biosynthetic process Source: UniProtKB-UniPathway
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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 544544Phosphoacetylglucosamine mutasePRO_0000148016Add
BLAST

Keywords - PTMi

Phosphoprotein

Structurei

Secondary structure

1
544
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 86Combined sources
Helixi11 – 133Combined sources
Beta strandi28 – 325Combined sources
Helixi33 – 353Combined sources
Helixi37 – 5317Combined sources
Turni54 – 563Combined sources
Beta strandi58 – 636Combined sources
Beta strandi72 – 787Combined sources
Beta strandi82 – 843Combined sources
Helixi87 – 893Combined sources
Helixi90 – 989Combined sources
Beta strandi99 – 1013Combined sources
Helixi114 – 12411Combined sources
Beta strandi133 – 1397Combined sources
Helixi145 – 15713Combined sources
Beta strandi159 – 16911Combined sources
Helixi172 – 18312Combined sources
Helixi185 – 1873Combined sources
Helixi192 – 20716Combined sources
Beta strandi217 – 2226Combined sources
Helixi228 – 23912Combined sources
Turni241 – 2433Combined sources
Beta strandi244 – 2507Combined sources
Helixi256 – 2583Combined sources
Turni259 – 2624Combined sources
Helixi265 – 2717Combined sources
Beta strandi286 – 2894Combined sources
Beta strandi296 – 3016Combined sources
Beta strandi307 – 3104Combined sources
Helixi312 – 32716Combined sources
Turni332 – 3343Combined sources
Beta strandi339 – 3435Combined sources
Helixi349 – 3579Combined sources
Beta strandi363 – 3653Combined sources
Helixi370 – 3778Combined sources
Beta strandi380 – 3867Combined sources
Beta strandi392 – 3965Combined sources
Helixi398 – 4069Combined sources
Helixi412 – 42716Combined sources
Beta strandi430 – 4323Combined sources
Helixi435 – 44814Combined sources
Helixi453 – 4575Combined sources
Beta strandi465 – 4706Combined sources
Helixi475 – 4773Combined sources
Beta strandi479 – 4813Combined sources
Turni482 – 4843Combined sources
Beta strandi486 – 4905Combined sources
Helixi493 – 5019Combined sources
Beta strandi508 – 5136Combined sources
Beta strandi520 – 5256Combined sources
Helixi529 – 54315Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DKAX-ray1.93A/B1-544[»]
2DKCX-ray2.20A/B1-544[»]
2DKDX-ray2.10A/B1-544[»]
ProteinModelPortaliQ9P4V2.
SMRiQ9P4V2. Positions 1-544.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9P4V2.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni387 – 3893Substrate binding1 Publication
Regioni512 – 5165Substrate binding1 Publication

Sequence similaritiesi

Belongs to the phosphohexose mutase family.Curated

Phylogenomic databases

eggNOGiCOG1109.

Family and domain databases

Gene3Di3.30.310.50. 1 hit.
3.40.120.10. 3 hits.
InterProiIPR005844. 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]
PfamiPF02878. PGM_PMM_I. 2 hits.
PF02879. PGM_PMM_II. 1 hit.
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti238 – 2381K → R in AAF64520. 1 PublicationCurated
Sequence conflicti308 – 3081K → N in AAF64520. 1 PublicationCurated
Sequence conflicti350 – 3501S → Y in AAF64520. 1 PublicationCurated

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
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 [» ]
ProteinModelPortali Q9P4V2.
SMRi Q9P4V2. Positions 1-544.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

eggNOGi COG1109.

Enzyme and pathway databases

UniPathwayi UPA00113 ; UER00530 .
BRENDAi 5.4.2.3. 1096.

Miscellaneous databases

EvolutionaryTracei Q9P4V2.

Family and domain databases

Gene3Di 3.30.310.50. 1 hit.
3.40.120.10. 3 hits.
InterProi 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 ]
Pfami PF02878. PGM_PMM_I. 2 hits.
PF02879. PGM_PMM_II. 1 hit.
PF00408. PGM_PMM_IV. 1 hit.
[Graphical view ]
PIRSFi PIRSF016408. PAGM. 1 hit.
SUPFAMi SSF53738. SSF53738. 3 hits.
SSF55957. SSF55957. 1 hit.
PROSITEi PS00710. PGM_PMM. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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], FUNCTION, CATALYTIC ACTIVITY.
    Strain: ATCC 10259 / CBS 5796 / DSM 5817 / JCM 2078 / NBRC 1060.
  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].
  3. "Crystal structures of N-acetylglucosamine-phosphate mutase, a member of the alpha-D-phosphohexomutase superfamily, and its substrate and product complexes."
    Nishitani Y., Maruyama D., Nonaka T., Kita A., Fukami T.A., Mio T., Yamada-Okabe H., Yamada-Okabe T., Miki K.
    J. Biol. Chem. 281:19740-19747(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) IN COMPLEX WITH SUBSTRATE AND ZINC.

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 26, 2014
This is version 74 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

External Data

Dasty 3