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
//