PGM_ASPFU
ID PGM_ASPFU Reviewed; 555 AA.
AC Q4WY53;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Phosphoglucomutase {ECO:0000250|UniProtKB:P37012};
DE Short=PGM {ECO:0000250|UniProtKB:P37012};
DE EC=5.4.2.2 {ECO:0000250|UniProtKB:P37012};
DE AltName: Full=Glucose phosphomutase;
GN Name=pgmA; ORFNames=AFUA_3G11830;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
CC -!- FUNCTION: Catalyzes the reversible interconversion of glucose 1-
CC phosphate and glucose 6-phosphate. Key enzyme in hexose metabolism. The
CC reverse reaction is an essential step for biosynthesis because glucose
CC 1-phosphate is the starting point for the synthesis of UDP-glucose,
CC which acts as a precursor for the synthesis of oligosaccharides and
CC trehalose. {ECO:0000250|UniProtKB:P37012}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate;
CC Xref=Rhea:RHEA:23536, ChEBI:CHEBI:58225, ChEBI:CHEBI:58601;
CC EC=5.4.2.2; Evidence={ECO:0000250|UniProtKB:P37012};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P37012};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:P37012};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P37012}.
CC -!- SIMILARITY: Belongs to the phosphohexose mutase family. {ECO:0000305}.
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DR EMBL; AAHF01000002; EAL92400.1; -; Genomic_DNA.
DR RefSeq; XP_754438.1; XM_749345.1.
DR AlphaFoldDB; Q4WY53; -.
DR SMR; Q4WY53; -.
DR STRING; 746128.CADAFUBP00003657; -.
DR SwissPalm; Q4WY53; -.
DR PRIDE; Q4WY53; -.
DR EnsemblFungi; EAL92400; EAL92400; AFUA_3G11830.
DR GeneID; 3511873; -.
DR KEGG; afm:AFUA_3G11830; -.
DR VEuPathDB; FungiDB:Afu3g11830; -.
DR eggNOG; KOG0625; Eukaryota.
DR HOGENOM; CLU_009330_0_1_1; -.
DR InParanoid; Q4WY53; -.
DR OMA; DIYKIYA; -.
DR OrthoDB; 555015at2759; -.
DR Proteomes; UP000002530; Chromosome 3.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004614; F:phosphoglucomutase activity; IBA:GO_Central.
DR GO; GO:0005975; P:carbohydrate metabolic process; IBA:GO_Central.
DR GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR005844; A-D-PHexomutase_a/b/a-I.
DR InterPro; IPR016055; A-D-PHexomutase_a/b/a-I/II/III.
DR InterPro; IPR005845; A-D-PHexomutase_a/b/a-II.
DR InterPro; IPR005846; A-D-PHexomutase_a/b/a-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; IPR005841; Alpha-D-phosphohexomutase_SF.
DR InterPro; IPR045244; PGM.
DR PANTHER; PTHR22573; PTHR22573; 1.
DR Pfam; PF02878; PGM_PMM_I; 1.
DR Pfam; PF02879; PGM_PMM_II; 1.
DR Pfam; PF02880; PGM_PMM_III; 1.
DR Pfam; PF00408; PGM_PMM_IV; 1.
DR PRINTS; PR00509; PGMPMM.
DR SUPFAM; SSF53738; SSF53738; 3.
DR SUPFAM; SSF55957; SSF55957; 1.
DR PROSITE; PS00710; PGM_PMM; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Cytoplasm; Glucose metabolism; Isomerase;
KW Magnesium; Metal-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1..555
FT /note="Phosphoglucomutase"
FT /id="PRO_0000228674"
FT ACT_SITE 114
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000250"
FT BINDING 114
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /note="via phosphate group"
FT /evidence="ECO:0000250"
FT BINDING 279
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 281
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 283
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 555 AA; 60501 MW; F4A9589EEACFCF4F CRC64;
MSVQTVSIQP FTDQKPGTSG LRKKVKVFQQ PHYSEAFVTS ILLSIPEGAE GAFLVIGGDG
RYYNPEVIQK IAKISAAYGV KKLLIGQNGI LSTPAASNLI RVRKATGGIL LTASHNPGGP
NADFGIKYNL CNGAPAPESV TNKIYETSKS LTSYKIAEIP DVDTSTIGTK TYGPLEVEIV
HSTSDYLKML KEIFDFDLIK EFLSTHKDFK VLFDGMHGVT GPYGVDIFVK ELGLPQDSTM
NCVPSPDFNG GHPDPNLVYA HELVEAVDKK GIHFGAASDG DGDRNMIYGA NTFVSPGDSL
AIIAHHAKLI PWFQKQGVYG LARSMPTSGA VDLVAKAQGL QSYEVPTGWK FFCNLFDNKK
ISICGEESFG TGSNHIREKD GVWAIVAWLN IIAGVAKQKP NETPSIASIQ NEFWQTYGRT
FFTRYDYENV DSDAANKLIA NLSEKINNKD SFVGSTVSGR KVADAGNFAY TDLDGSVTKN
QGLYVKFDDG SRLVVRLSGT GSSGATIRLY IEKYESDKSK FGMNTQDYLK DNVALAMSLL
KFKEYIGRED PDVKT
