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Database: UniProt
Entry: A0A3D8SK05_9EURO
LinkDB: A0A3D8SK05_9EURO
Original site: A0A3D8SK05_9EURO 
ID   A0A3D8SK05_9EURO        Unreviewed;       556 AA.
AC   A0A3D8SK05;
DT   16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT   16-JAN-2019, sequence version 1.
DT   24-JAN-2024, entry version 11.
DE   RecName: Full=phosphoglucomutase (alpha-D-glucose-1,6-bisphosphate-dependent) {ECO:0000256|ARBA:ARBA00012728};
DE            EC=5.4.2.2 {ECO:0000256|ARBA:ARBA00012728};
GN   ORFNames=DSM5745_03176 {ECO:0000313|EMBL:RDW86534.1};
OS   Aspergillus mulundensis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1810919 {ECO:0000313|EMBL:RDW86534.1, ECO:0000313|Proteomes:UP000256690};
RN   [1] {ECO:0000313|EMBL:RDW86534.1, ECO:0000313|Proteomes:UP000256690}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 5745 {ECO:0000313|EMBL:RDW86534.1,
RC   ECO:0000313|Proteomes:UP000256690};
RX   PubMed=30018880; DOI=10.5598/imafungus.2018.09.01.13;
RA   Wingfield B.D., Bills G.F., Dong Y., Huang W., Nel W.J.,
RA   Swalarsk-Parry B.S., Vaghefi N., Wilken P.M., An Z., de Beer Z.W.,
RA   De Vos L., Chen L., Duong T.A., Gao Y., Hammerbacher A., Kikkert J.R.,
RA   Li Y., Li H., Li K., Li Q., Liu X., Ma X., Naidoo K., Pethybridge S.J.,
RA   Sun J., Steenkamp E.T., van der Nest M.A., van Wyk S., Wingfield M.J.,
RA   Xiong C., Yue Q., Zhang X.;
RT   "IMA Genome-F 9: Draft genome sequence of Annulohypoxylon stygium,
RT   Aspergillus mulundensis, Berkeleyomyces basicola (syn. Thielaviopsis
RT   basicola), Ceratocystis smalleyi, two Cercospora beticola strains,
RT   Coleophoma cylindrospora, Fusarium fracticaudum, Phialophora cf. hyalina,
RT   and Morchella septimelata.";
RL   IMA Fungus 9:199-223(2018).
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:0000256|ARBA:ARBA00000443};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SIMILARITY: Belongs to the phosphohexose mutase family.
CC       {ECO:0000256|ARBA:ARBA00010231, ECO:0000256|RuleBase:RU004326}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RDW86534.1}.
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DR   EMBL; PVWQ01000003; RDW86534.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3D8SK05; -.
DR   STRING; 1810919.A0A3D8SK05; -.
DR   OrthoDB; 5476118at2759; -.
DR   Proteomes; UP000256690; Unassembled WGS sequence.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0004614; F:phosphoglucomutase activity; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd03085; PGM1; 1.
DR   Gene3D; 3.40.120.10; Alpha-D-Glucose-1,6-Bisphosphate, subunit A, domain 3; 3.
DR   Gene3D; 3.30.310.50; Alpha-D-phosphohexomutase, C-terminal domain; 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; IPR005845; A-D-PHexomutase_a/b/a-II.
DR   InterPro; IPR005846; A-D-PHexomutase_a/b/a-III.
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:SF2; PHOSPHOGLUCOMUTASE; 1.
DR   PANTHER; PTHR22573; PHOSPHOHEXOMUTASE FAMILY MEMBER; 1.
DR   Pfam; PF02878; PGM_PMM_I; 1.
DR   Pfam; PF02879; PGM_PMM_II; 1.
DR   Pfam; PF02880; PGM_PMM_III; 1.
DR   PRINTS; PR00509; PGMPMM.
DR   SUPFAM; SSF55957; Phosphoglucomutase, C-terminal domain; 1.
DR   SUPFAM; SSF53738; Phosphoglucomutase, first 3 domains; 3.
DR   PROSITE; PS00710; PGM_PMM; 1.
PE   3: Inferred from homology;
KW   Magnesium {ECO:0000256|RuleBase:RU004326};
KW   Metal-binding {ECO:0000256|RuleBase:RU004326};
KW   Reference proteome {ECO:0000313|Proteomes:UP000256690}.
FT   DOMAIN          14..153
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          184..288
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          297..401
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
SQ   SEQUENCE   556 AA;  60647 MW;  479D17B815C99554 CRC64;
     MSVQTVSIQP FGDQKPGTSG LRKKVKIFQQ ENYTESFVTS IILSIPEGAQ DAFLVIGGDG
     RYYNSDVIQK IAKIGAAYGV KKLIVGQNGI LSTPAASNLI RKRKATGGIL LTASHNPGGP
     DNDFGIKYNL TNGAPAPEQV TNKIYEVSKS LTSYNYIDLP EVDTTTIGTR SYGPLEVEVV
     HSTEDYVAMM KEIFDFDLIR SFLKKHPDFK VLFDGMHGVT GPYGVDIFVN ELGLPSDSTM
     NCIPKPDFGG GHPDPNLVYA HELVEAVDKN GIHFGAASDG DGDRNMIYGA NTFVSPGDSL
     AIIAHHAKLI PWFQKHGVDG LARSMPTSGA VDLVAKAQGL QSYEVPTGWK FFCNLFDNKK
     MSICGEESFG TGSNHIREKD GVWAIVAWLN IIAGVAEQKP NETPSIASIQ AEFWETYGRT
     FFTRYDYENV DSEGANKLIA ALSEKAVDNK DSFVGSTVSG RKVVDSGNFA YTDLDGSVAK
     NQGLYAKFDD GSRLVVRLSG TGSSGATIRL YVEKYEGDKS KYQMETQEYL KDNVGLALEL
     LKFKEFVGRE EPDVKT
//
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