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Database: UniProt
Entry: A0A098VT85_9MICR
LinkDB: A0A098VT85_9MICR
Original site: A0A098VT85_9MICR 
ID   A0A098VT85_9MICR        Unreviewed;       429 AA.
AC   A0A098VT85;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=Phosphoglucomutase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=DI09_1p570 {ECO:0000313|EMBL:KGG52207.1};
OS   Mitosporidium daphniae.
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Mitosporidium.
OX   NCBI_TaxID=1485682 {ECO:0000313|EMBL:KGG52207.1, ECO:0000313|Proteomes:UP000029725};
RN   [1] {ECO:0000313|EMBL:KGG52207.1, ECO:0000313|Proteomes:UP000029725}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UGP3 {ECO:0000313|EMBL:KGG52207.1,
RC   ECO:0000313|Proteomes:UP000029725};
RC   TISSUE=Spores {ECO:0000313|EMBL:KGG52207.1};
RA   Haag K.L., James T.Y., Larsson R., Schaer T.M., Refardt D., Pombert J.-F.,
RA   Ebert D.;
RT   "A new species of microsporidia sheds light on the evolution of extreme
RT   parasitism.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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:KGG52207.1}.
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DR   EMBL; JMKJ01000111; KGG52207.1; -; Genomic_DNA.
DR   RefSeq; XP_013238634.1; XM_013383180.1.
DR   AlphaFoldDB; A0A098VT85; -.
DR   GeneID; 25258948; -.
DR   VEuPathDB; MicrosporidiaDB:DI09_1p570; -.
DR   HOGENOM; CLU_016950_0_1_1; -.
DR   OrthoDB; 1482at2759; -.
DR   Proteomes; UP000029725; Unassembled WGS sequence.
DR   GO; GO:0016868; F:intramolecular phosphotransferase activity; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd05799; PGM2; 1.
DR   Gene3D; 3.40.120.10; Alpha-D-Glucose-1,6-Bisphosphate, subunit A, domain 3; 3.
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; IPR016066; A-D-PHexomutase_CS.
DR   PANTHER; PTHR45745:SF1; PHOSPHOGLUCOMUTASE 2A-RELATED; 1.
DR   PANTHER; PTHR45745; PHOSPHOMANNOMUTASE 45A; 1.
DR   Pfam; PF02878; PGM_PMM_I; 1.
DR   Pfam; PF02879; PGM_PMM_II; 1.
DR   Pfam; PF02880; PGM_PMM_III; 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:UP000029725}.
FT   DOMAIN          50..186
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          209..312
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          322..428
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
SQ   SEQUENCE   429 AA;  47033 MW;  859D5D736B836D24 CRC64;
     MTLCIPDKEL AILIDRWIEY DSNTNTRAFI AGLKEKNSWD VLESLMRPRI SFGTAGLRAE
     MGAGFARMND LTVMQTSQGL ASYVKKHTAK EEPVAVIGYD HRANSKTFSR ITTEAFLKKG
     FKVFLFPDII PTPLLAFSVL QLKADIGVMI TASHNPKSDN GYKVYWSNGA QILAPHDANI
     LCSIQANLEP WSALPSALDK TFVPDTLCAY LSSITSILSV KTAPKSVPRV VYTAMHGVGY
     QTVKASVKAC GFPELFPVKS QVDPDPEFPT APKPNPEEAG AFDEAFKTAK DVGATVIFSN
     DPDADRFSLA EELSDGKWRI FTGDEVGIIL ASYLVEEGLF RETPNIAVLN TVVSSSLLGK
     MASNWSAEYA HRKFKYAQCL TGFKNIVHSA QRLMNQGYNV ALAYEEALGY MCTTNVMDKD
     GISALMNAC
//
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