ID A0A0R3RZ86_9BILA Unreviewed; 569 AA.
AC A0A0R3RZ86;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
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};
OS Elaeophora elaphi.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Elaeophora.
OX NCBI_TaxID=1147741 {ECO:0000313|Proteomes:UP000050640, ECO:0000313|WBParaSite:EEL_0000763001-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:EEL_0000763001-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
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}.
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DR AlphaFoldDB; A0A0R3RZ86; -.
DR STRING; 1147741.A0A0R3RZ86; -.
DR WBParaSite; EEL_0000763001-mRNA-1; EEL_0000763001-mRNA-1; EEL_0000763001.
DR Proteomes; UP000050640; Unplaced.
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}.
FT DOMAIN 16..163
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 199..308
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 315..427
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
SQ SEQUENCE 569 AA; 62591 MW; 653191475DEFD471 CRC64;
MSIKVVTVNT KPYEGQKPGT SGLRKRVPEF QQENYTENFI QCTLDAGLGD KKRGATLVVG
GDGRYLCPET VNIIIQMAAA NGLRKLIVGQ NGFLSTPAVS CLIRKCEIND GILINGGIIL
TASHNPGGPK ADFGIKFNCE NGGPAPEKLT EAIYALSRNI SKYYICHDLH ADFTKIGKTD
YDIDGYGIFT VHVIDSVEDY VQLMEEIFDF SKIKELLSGQ TMGQFNVLID SLYGATGPYV
NTILIDKLGV DPKFTSHTTP KPDFGGGHPD PNLTYAKQLV DTLKKGEHDF GAAFDGDGDR
NMILGKNGFF VTPSDSLAVI AANMKCIPYF QQHGIKGYAR SMPTAGAIDR VAKETGVPMY
ETPTGWKFFG NLMDADKLSL CGEESFGTGS DHIREKDGIW AALAWLQILQ DKKQSVESVI
KEHWSKYGRN VFTRYDYENC DASGANLMMT FIESQMQAFI GQKFTANEKS FVIKQADNFT
YTDPVDGSVS QKQGLRILFE DGSRTVFRLS GTGSLGATIR LYVDSFIDAS DKQRLFQSSE
ELLKPLVLVA LQISKLEHFT GRDAPTVIT
//
