(data stored in ACNUC7421 zone)

SWISSPROT: Q75CE5_ASHGO

ID   Q75CE5_ASHGO            Unreviewed;       552 AA.
AC   Q75CE5;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   11-DEC-2019, entry version 103.
DE   RecName: Full=Phosphoacetylglucosamine mutase {ECO:0000256|PIRNR:PIRNR016408};
DE            Short=PAGM {ECO:0000256|PIRNR:PIRNR016408};
DE            EC=5.4.2.3 {ECO:0000256|PIRNR:PIRNR016408};
DE   AltName: Full=Acetylglucosamine phosphomutase {ECO:0000256|PIRNR:PIRNR016408};
DE   AltName: Full=N-acetylglucosamine-phosphate mutase {ECO:0000256|PIRNR:PIRNR016408};
GN   ORFNames=AGOS_ACR015W {ECO:0000313|EMBL:AAS51242.1};
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811 {ECO:0000313|EMBL:AAS51242.1, ECO:0000313|Proteomes:UP000000591};
RN   [1] {ECO:0000313|EMBL:AAS51242.1, ECO:0000313|Proteomes:UP000000591}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Pohlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2] {ECO:0000313|Proteomes:UP000000591}
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
CC   -!- FUNCTION: Catalyzes the conversion of GlcNAc-6-P into GlcNAc-1-P during
CC       the synthesis of uridine diphosphate/UDP-GlcNAc, which is a
CC       biosynthetic precursor of chitin and also supplies the amino sugars for
CC       N-linked oligosaccharides of glycoproteins.
CC       {ECO:0000256|PIRNR:PIRNR016408}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N-acetyl-alpha-D-glucosamine 1-phosphate = N-acetyl-D-
CC         glucosamine 6-phosphate; Xref=Rhea:RHEA:23804, ChEBI:CHEBI:57513,
CC         ChEBI:CHEBI:57776; EC=5.4.2.3;
CC         Evidence={ECO:0000256|PIRNR:PIRNR016408};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|PIRNR:PIRNR016408,
CC         ECO:0000256|PIRSR:PIRSR016408-3};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|PIRNR:PIRNR016408,
CC       ECO:0000256|PIRSR:PIRSR016408-3};
CC   -!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-
CC       glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from
CC       alpha-D-glucosamine 6-phosphate (route I): step 2/2.
CC       {ECO:0000256|PIRNR:PIRNR016408}.
CC   -!- SIMILARITY: Belongs to the phosphohexose mutase family.
CC       {ECO:0000256|PIRNR:PIRNR016408}.
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DR   EMBL; AE016816; AAS51242.1; -; Genomic_DNA.
DR   RefSeq; NP_983418.1; NM_208771.1.
DR   STRING; 33169.AAS51242; -.
DR   PRIDE; Q75CE5; -.
DR   EnsemblFungi; AAS51242; AAS51242; AGOS_ACR015W.
DR   GeneID; 4619543; -.
DR   KEGG; ago:AGOS_ACR015W; -.
DR   HOGENOM; HOG000210027; -.
DR   InParanoid; Q75CE5; -.
DR   KO; K01836; -.
DR   OMA; PGDRCCS; -.
DR   UniPathway; UPA00113; UER00530.
DR   Proteomes; UP000000591; Chromosome III.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0004610; F:phosphoacetylglucosamine mutase activity; IBA:GO_Central.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0034221; P:fungal-type cell wall chitin biosynthetic process; IBA:GO_Central.
DR   GO; GO:0006048; P:UDP-N-acetylglucosamine biosynthetic process; IBA:GO_Central.
DR   CDD; cd03086; PGM3; 1.
DR   InterPro; IPR005844; A-D-PHexomutase_a/b/a-I.
DR   InterPro; IPR016055; A-D-PHexomutase_a/b/a-I/II/III.
DR   InterPro; IPR005843; A-D-PHexomutase_C.
DR   InterPro; IPR036900; A-D-PHexomutase_C_sf.
DR   InterPro; IPR016066; A-D-PHexomutase_CS.
DR   InterPro; IPR016657; PAGM.
DR   Pfam; PF02878; PGM_PMM_I; 2.
DR   Pfam; PF00408; PGM_PMM_IV; 1.
DR   PIRSF; PIRSF016408; PAGM; 1.
DR   SUPFAM; SSF53738; SSF53738; 3.
DR   SUPFAM; SSF55957; SSF55957; 1.
DR   PROSITE; PS00710; PGM_PMM; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q75CE5.
DR   SWISS-2DPAGE; Q75CE5.
KW   Isomerase {ECO:0000256|PIRNR:PIRNR016408};
KW   Magnesium {ECO:0000256|PIRNR:PIRNR016408, ECO:0000256|PIRSR:PIRSR016408-3};
KW   Metal-binding {ECO:0000256|PIRNR:PIRNR016408,
KW   ECO:0000256|PIRSR:PIRSR016408-3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000591}.
FT   DOMAIN          56..97
FT                   /note="PGM_PMM_I"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          124..175
FT                   /note="PGM_PMM_I"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          481..539
FT                   /note="PGM_PMM_IV"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
FT   REGION          382..384
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR016408-2"
FT   REGION          510..514
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR016408-2"
FT   ACT_SITE        65
FT                   /note="Phosphoserine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR016408-1"
FT   METAL           65
FT                   /note="Magnesium; via phosphate group"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR016408-3"
FT   METAL           285
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR016408-3"
FT   METAL           287
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR016408-3"
FT   METAL           289
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR016408-3"
FT   BINDING         519
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR016408-2"
SQ   SEQUENCE   552 AA;  60326 MW;  9AC727E916C9BA21 CRC64;
     MRTVQEMVKL YDRHRGCGRV YAYGTAGFRS RAEVLAPVVF ATGLLACLRS LYLGGAYVGV
     MLTASHNPPE DNGVKLVDPH GEMLAAEWEK HATALANCAS QGQQELLDAL HMLVDRLGLD
     LALRARVVVA RDSRASGPQL LDALLDGTRM LEDVEVVDCG MLTTPQLHFL TCACNERGSA
     AGVREDLYYA HFVAALEELA ALHGLETLPF PLVVDTANGV GALKARELFR RSPLFKNRVS
     IINDNWSQHE LLNSGCGADY VKTKQCLPQG ISADLLRESL FCSYDGDADR VIFYYIDGQE
     RFHLLDGDKI STLIAKFLQS ALLTAGINDD VCLGVVQTAY ANGSSTRYLS EVLEVPVSCT
     PTGVKHLHRE AVQKYDVGIY FEANGHGTVI FSEHFTLTVE RALENPALSA KARLSLQTLK
     TFANLINQTI GDAIADMLAV IAILSILHWS PEDWDKQYTD LPNNLVKVVV PDRSMFKTTN
     AEQQLTSPAG LQELIDDIVM VYDSGRSFVR ASGTEDAVRI YAEAASQQQA DELATKVSTL
     VVESTNDPGI CN
//

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