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Database: UniProt
Entry: A0A0B2USN0_TOXCA
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ID   A0A0B2USN0_TOXCA        Unreviewed;       595 AA.
AC   A0A0B2USN0;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Phosphoglucomutase (alpha-D-glucose-1,6-bisphosphate-dependent) {ECO:0000313|WBParaSite:TCNE_0001375601-mRNA-1};
DE   SubName: Full=Phosphoglucomutase-2 {ECO:0000313|EMBL:KHN72132.1};
GN   Name=PGM2 {ECO:0000313|EMBL:KHN72132.1};
GN   ORFNames=Tcan_16378 {ECO:0000313|EMBL:KHN72132.1}, TCNE_LOCUS13756
GN   {ECO:0000313|EMBL:VDM45077.1};
OS   Toxocara canis (Canine roundworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Ascaridomorpha; Ascaridoidea; Toxocaridae; Toxocara.
OX   NCBI_TaxID=6265 {ECO:0000313|EMBL:KHN72132.1, ECO:0000313|Proteomes:UP000031036};
RN   [1] {ECO:0000313|EMBL:KHN72132.1, ECO:0000313|Proteomes:UP000031036}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PN_DK_2014 {ECO:0000313|EMBL:KHN72132.1};
RA   Zhu X.-Q., Korhonen P.K., Cai H., Young N.D., Nejsum P.,
RA   von Samson-Himmelstjerna G., Boag P.R., Tan P., Li Q., Min J., Yang Y.,
RA   Wang X., Fang X., Hall R.S., Hofmann A., Sternberg P.W., Jex A.R.,
RA   Gasser R.B.;
RT   "Genetic blueprint of the zoonotic pathogen Toxocara canis.";
RL   Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|WBParaSite:TCNE_0001375601-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (JUN-2016) to UniProtKB.
RN   [3] {ECO:0000313|EMBL:VDM45077.1, ECO:0000313|Proteomes:UP000267007}
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, ECO:0000256|RuleBase:RU004326}.
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DR   EMBL; JPKZ01003299; KHN72132.1; -; Genomic_DNA.
DR   EMBL; UYWY01021881; VDM45077.1; -; Genomic_DNA.
DR   STRING; 6265.A0A0B2USN0; -.
DR   WBParaSite; TCNE_0001375601-mRNA-1; TCNE_0001375601-mRNA-1; TCNE_0001375601.
DR   OMA; HVTKASY; -.
DR   Proteomes; UP000031036; Unassembled WGS sequence.
DR   Proteomes; UP000050794; Unplaced.
DR   Proteomes; UP000267007; 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   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; IPR005843; A-D-PHexomutase_C.
DR   InterPro; IPR036900; A-D-PHexomutase_C_sf.
DR   InterPro; IPR016066; A-D-PHexomutase_CS.
DR   InterPro; IPR005841; Alpha-D-phosphohexomutase_SF.
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   Pfam; PF00408; PGM_PMM_IV; 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   Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|RuleBase:RU004326};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU004326};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031036}.
FT   DOMAIN          48..185
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          220..320
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          359..450
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          523..570
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   595 AA;  66983 MW;  F97F54EC58E61D08 CRC64;
     MGASCADLDE LVANWLKWDK NEKNRKEIEE LVSKKDVETL KARMCKKMVF GTAGIRSRME
     AGFSRLNDLT ILMVTNGFAL HLKEVYKRES NGVAIGYDGR HNSRRWAELA ANVFVRHGLK
     VYLFSEVCPT PLVSYATIRL KCDAGLMITA SHNPKHDNGY KAYWSNGAQI LAPHDAEICR
     IAYANMEPKP EFWDLSQLHS HPLLHSADPV IDDYFKDEQS LCHYKSINEK CPIKFTYSAF
     HGVGLPYATR LFTNFGFSPD NISIVEEQAK PDPDFPTVPF PNPEEGRPVL KLSIETADRN
     GATVILANDP DADRFQLAEK QPDGEWKVFA GNEMGALISW WTWKCWRKEN PEGDASNLYM
     LNSAVSSSIV KTMAAKEGFK NELTLTGFKW MGNKADELRK QGKNVVLAWE ESIGFMAGHP
     LDKDGITAAG IFAEIASYLH SENLTLAKQI FNIYKEYGFH VVRSSYWFVP NPDVTIKIFA
     KLRKDNKYPV KIGDHSVKYV RDLTIGYDNE QPGNKPVLPL STSSEMITFT LADGSWATVR
     ASGTEPKIKY YIELKTAPGK EEKDLVEVMA ELSKLEEMVV VNLLEPSVNG LIARK
//
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