(data stored in SCRATCH zone)

SWISSPROT: B6H1E1_PENRW

ID   B6H1E1_PENRW            Unreviewed;       539 AA.
AC   B6H1E1;
DT   16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT   16-DEC-2008, sequence version 1.
DT   05-JUL-2017, entry version 54.
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=Pc13g02740 {ECO:0000313|EMBL:CAP91343.1}, PCH_Pc13g02740
GN   {ECO:0000313|EMBL:CAP91343.1};
OS   Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 /
OS   Wisconsin 54-1255) (Penicillium chrysogenum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC   Penicillium chrysogenum species complex.
OX   NCBI_TaxID=500485 {ECO:0000313|EMBL:CAP91343.1, ECO:0000313|Proteomes:UP000000724};
RN   [1] {ECO:0000313|EMBL:CAP91343.1, ECO:0000313|Proteomes:UP000000724}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255
RC   {ECO:0000313|Proteomes:UP000000724};
RX   PubMed=18820685; DOI=10.1038/nbt.1498;
RA   van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA   Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA   Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA   Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A.,
RA   van der Klei I.J., van Peij N.N.M.E., Veenhuis M., von Doehren H.,
RA   Wagner C., Wortman J.R., Bovenberg R.A.L.;
RT   "Genome sequencing and analysis of the filamentous fungus Penicillium
RT   chrysogenum.";
RL   Nat. Biotechnol. 26:1161-1168(2008).
CC   -!- FUNCTION: Catalyzes the conversion of GlcNAc-6-P into GlcNAc-1-P
CC       during the synthesis of uridine diphosphate/UDP-GlcNAc, which is a
CC       biosynthetic precursor of chitin and also supplies the amino
CC       sugars for N-linked oligosaccharides of glycoproteins.
CC       {ECO:0000256|PIRNR:PIRNR016408}.
CC   -!- CATALYTIC ACTIVITY: N-acetyl-alpha-D-glucosamine 1-phosphate = N-
CC       acetyl-D-glucosamine 6-phosphate. {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.
CC       {ECO:0000256|PIRNR:PIRNR016408, 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
CC       from 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; AM920428; CAP91343.1; -; Genomic_DNA.
DR   RefSeq; XP_002558713.1; XM_002558667.1.
DR   STRING; 500485.XP_002558713.1; -.
DR   EnsemblFungi; CAP91343; CAP91343; PCH_Pc13g02740.
DR   GeneID; 8314729; -.
DR   KEGG; pcs:Pc13g02740; -.
DR   eggNOG; KOG2537; Eukaryota.
DR   eggNOG; COG1109; LUCA.
DR   HOGENOM; HOG000210027; -.
DR   KO; K01836; -.
DR   OMA; LHYMVCC; -.
DR   OrthoDB; EOG092C236M; -.
DR   BioCyc; PCHR:PC13G02740-MONOMER; -.
DR   UniPathway; UPA00113; UER00530.
DR   Proteomes; UP000000724; Contig Pc00c13.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0004610; F:phosphoacetylglucosamine mutase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0006048; P:UDP-N-acetylglucosamine biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd03086; PGM3; 1.
DR   Gene3D; 3.30.310.50; -; 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; 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; B6H1E1.
DR   SWISS-2DPAGE; B6H1E1.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000724};
KW   Isomerase {ECO:0000256|PIRNR:PIRNR016408};
KW   Magnesium {ECO:0000256|PIRNR:PIRNR016408,
KW   ECO:0000256|PIRSR:PIRSR016408-3};
KW   Metal-binding {ECO:0000256|PIRNR:PIRNR016408,
KW   ECO:0000256|PIRSR:PIRSR016408-3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000724}.
FT   DOMAIN       63     94       PGM_PMM_I. {ECO:0000259|Pfam:PF02878}.
FT   DOMAIN      123    175       PGM_PMM_I. {ECO:0000259|Pfam:PF02878}.
FT   DOMAIN      458    533       PGM_PMM_IV. {ECO:0000259|Pfam:PF00408}.
FT   REGION      377    379       Substrate binding. {ECO:0000256|PIRSR:
FT                                PIRSR016408-2}.
FT   REGION      502    506       Substrate binding. {ECO:0000256|PIRSR:
FT                                PIRSR016408-2}.
FT   ACT_SITE     69     69       Phosphoserine intermediate.
FT                                {ECO:0000256|PIRSR:PIRSR016408-1}.
FT   METAL        69     69       Magnesium; via phosphate group.
FT                                {ECO:0000256|PIRSR:PIRSR016408-3}.
FT   METAL       281    281       Magnesium. {ECO:0000256|PIRSR:
FT                                PIRSR016408-3}.
FT   METAL       283    283       Magnesium. {ECO:0000256|PIRSR:
FT                                PIRSR016408-3}.
FT   METAL       285    285       Magnesium. {ECO:0000256|PIRSR:
FT                                PIRSR016408-3}.
FT   BINDING     511    511       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR016408-2}.
SQ   SEQUENCE   539 AA;  58515 MW;  3341BE2225F79C30 CRC64;
     MASPAVKKAI TEAALQYAKP EGKVFEYGTA GFRMKADLLN TVVFAVGLLA SLRSKKLSGQ
     WIGVMVTASH NPAEDNGVKL VDPMGEMLEA EWEAYATRLA NAPLDKIADV YDELIKEIDV
     KMTNPARVVF ARDTRASGSR LVGVLNAALT ATEVEFVDLK YMTTPQLHYV VRCKNTLGTQ
     YEYGEPTEQG YYEKLANSFK KVMRGVKVQG SLTVDCANGV GGPKLRELMK YLTGIDIKVV
     NDDVINPDAL NFDCGADYVK TKQRAPPSSK AAVLDRCASL DGDADRLVYY FLDESNVFRL
     LDGDRIATLA ASFIGDLARN AGIASKLKIG VVQTAYANGA STDYIEKVLK LPIICTNTGV
     KHLHHAALRF DVGVYFEANG HGTVTFSENA LKVIKNTEPQ SPAQQHALES LQALTDLINQ
     AVGDALSDAL LVEAILAHKG WSPKEWLGTY TDLPSRLVRV EVNDRSIFKA YDAERKLESP
     PGLQGTIESL QSRYNKGRSF ARASGTEDAV RVYAEAASRS EADDLATRVA NAVSEAGSA
//

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