ID A0A0R3SCT0_HYMDI Unreviewed; 613 AA.
AC A0A0R3SCT0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=Phosphoglucomutase-2 {ECO:0000313|WBParaSite:HDID_0000241601-mRNA-1};
GN ORFNames=HDID_LOCUS2417 {ECO:0000313|EMBL:VDL19878.1};
OS Hymenolepis diminuta (Rat tapeworm).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC Eucestoda; Cyclophyllidea; Hymenolepididae; Hymenolepis.
OX NCBI_TaxID=6216 {ECO:0000313|Proteomes:UP000046397, ECO:0000313|WBParaSite:HDID_0000241601-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:HDID_0000241601-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDL19878.1, ECO:0000313|Proteomes:UP000274504}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (NOV-2018) 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}.
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DR EMBL; UYSG01000587; VDL19878.1; -; Genomic_DNA.
DR STRING; 6216.A0A0R3SCT0; -.
DR WBParaSite; HDID_0000241601-mRNA-1; HDID_0000241601-mRNA-1; HDID_0000241601.
DR Proteomes; UP000046397; Unplaced.
DR Proteomes; UP000274504; 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; IPR036900; A-D-PHexomutase_C_sf.
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; 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 Reference proteome {ECO:0000313|Proteomes:UP000274504}.
FT DOMAIN 46..184
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 213..318
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 330..440
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
SQ SEQUENCE 613 AA; 69846 MW; 98B5A167BD7DC09C CRC64;
MQADLKAKVD EWLKWDKNET TRKEIEAMAS SPARFEELKK LMLNRMEFGT AGLRSKMGPG
YSQMNDLTIV QTAQGLLKYM EEKHLKLKPK GIIVGYDGRY NSKTWACITA NIFVRSGWKV
YLFRDVNTTP FLAYGVRHFK TACGVMVTAS HNPKDDNGYK VYWENGAQIL SPHDKGIATA
ITESLEPRAS SWQYHDVMNH PQCLNPMPEL EDTYIKVQKE KICFTEEENK KSNVQFVYTA
MHGVGYNAAK RIFETFGFKH MIPVEEQIHP DPEFSTVKFP NPEEGRSALE LAMATANKHG
VKIICANDPD ADRMAVAEKL PDGTWKILNG NELATVLGWW MWMNWHKRNP DADLSKVYMI
SSTVSSKILR AIAQKEGFNF EETLTGFKWI ANKAYDIMQE GGEVIFCFEE AIGFMCGTTV
LDKDGIGTFG VVCEMVSHLY SKNISLVQQL HSVFEIDVFV QIANMNFFLS RYGKHVSNNS
YYFCYEPPKI VQMFERLRHM PKTGGYPQTL GRFKINGLRD LTVGYDSNYP DHKARLPVSA
SSQMITFTFD NDVVLTIRTS GTEPKIKYYS ELCGKCDDKR SMAELEAELT ELIGLMVKEF
YQPDVNGFTA RSD
//
