ID A0A158PGR3_ANGCS Unreviewed; 527 AA.
AC A0A158PGR3;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
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};
GN ORFNames=ACOC_LOCUS5508 {ECO:0000313|EMBL:VDM57093.1};
OS Angiostrongylus costaricensis (Nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Metastrongylidae;
OC Angiostrongylus.
OX NCBI_TaxID=334426 {ECO:0000313|Proteomes:UP000050601, ECO:0000313|WBParaSite:ACOC_0000550701-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:ACOC_0000550701-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (APR-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDM57093.1, ECO:0000313|Proteomes:UP000267027}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Costa Rica {ECO:0000313|EMBL:VDM57093.1,
RC ECO:0000313|Proteomes:UP000267027};
RG Pathogen Informatics;
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; UYYA01003875; VDM57093.1; -; Genomic_DNA.
DR STRING; 334426.A0A158PGR3; -.
DR WBParaSite; ACOC_0000550701-mRNA-1; ACOC_0000550701-mRNA-1; ACOC_0000550701.
DR OMA; WIQDRAN; -.
DR Proteomes; UP000050601; Unplaced.
DR Proteomes; UP000267027; Unassembled WGS sequence.
DR GO; GO:0004614; F:phosphoglucomutase activity; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 3.40.120.10; Alpha-D-Glucose-1,6-Bisphosphate, subunit A, domain 3; 4.
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; 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.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000267027}.
FT DOMAIN 16..87
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 171..263
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 292..385
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
SQ SEQUENCE 527 AA; 57955 MW; FCC046C772A3C84D CRC64;
MVFKVETVPT KPFEGQKPGT SGLRKRVPEF QQKHYTENFV QAVLDGGLGS KKKGSVLVVG
GDGRFLCSEA VNVIIQIAAA NGVSLYLEKA SKDARLMEVF TALFLDITNA IHDVTTKISH
YSICPDLKCD FTRIGRNEYD IDGVGHFMVD IIDPVKDYVE LMQSIFDFSK IKSLISGQLT
GKRFEVLVDS MHGATGPYVS TILCDYLGVE SHGLLRTVPK PDFGGGHPDP NLTYAKTLVE
QLNKGKHDFG AAFDGDGDRN MILGKGFFVT PSDSLAVIAD NINCIPYFKS RKISGFARSM
PTAGAIDLVA KARGLEVFET PTGWKYFGNL MDAGRICLCG EESFGTGSIH IREKDGVWAM
LAWLQILAEK KMSVEDIVKE QWKRYGRNVF TRYDYENVDA SGANLLMTFL ESQMPSFVGK
ELSANNVSYK VKLADNFLYT DPIDGSVAAK QGLRIIFEDS SRLVFRLSGT GSAGATIRLY
VDSYVPSSAS DKLFAPAHDI LKPLVLIALD LCKMEHFTGR KSPTVIT
//
