ID G1X6H1_ARTOA Unreviewed; 594 AA.
AC G1X6H1;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Phosphoglucomutase-3 {ECO:0008006|Google:ProtNLM};
GN ORFNames=AOL_s00054g465 {ECO:0000313|EMBL:EGX51395.1};
OS Arthrobotrys oligospora (strain ATCC 24927 / CBS 115.81 / DSM 1491)
OS (Nematode-trapping fungus) (Didymozoophaga oligospora).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC Orbiliales; Orbiliaceae; Orbilia; Orbilia oligospora.
OX NCBI_TaxID=756982 {ECO:0000313|EMBL:EGX51395.1, ECO:0000313|Proteomes:UP000008784};
RN [1] {ECO:0000313|EMBL:EGX51395.1, ECO:0000313|Proteomes:UP000008784}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24927 / CBS 115.81 / DSM 1491
RC {ECO:0000313|Proteomes:UP000008784};
RX PubMed=21909256; DOI=10.1371/journal.ppat.1002179;
RA Yang J., Wang L., Ji X., Feng Y., Li X., Zou C., Xu J., Ren Y., Mi Q.,
RA Wu J., Liu S., Liu Y., Huang X., Wang H., Niu X., Li J., Liang L., Luo Y.,
RA Ji K., Zhou W., Yu Z., Li G., Liu Y., Li L., Qiao M., Feng L., Zhang K.-Q.;
RT "Genomic and proteomic analyses of the fungus Arthrobotrys oligospora
RT provide insights into nematode-trap formation.";
RL PLoS Pathog. 7:E1002179-E1002179(2011).
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:EGX51395.1}.
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DR EMBL; ADOT01000085; EGX51395.1; -; Genomic_DNA.
DR RefSeq; XP_011120083.1; XM_011121781.1.
DR AlphaFoldDB; G1X6H1; -.
DR STRING; 756982.G1X6H1; -.
DR GeneID; 22891010; -.
DR eggNOG; KOG1220; Eukaryota.
DR HOGENOM; CLU_016950_0_1_1; -.
DR InParanoid; G1X6H1; -.
DR OMA; GYCVDPE; -.
DR OrthoDB; 1482at2759; -.
DR Proteomes; UP000008784; 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 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 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:UP000008784}.
FT DOMAIN 49..190
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 220..325
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 335..459
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 537..578
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 594 AA; 64374 MW; E122493243CB4147 CRC64;
MSENADKTIQ QLVKEWLELD QNEATRQEIK DLSDKKDYDE LEKRLRTRIA FGTAGLRSSM
QAGFAHLNPL TIIQASQGLA SYLLASIPQT VTPSPKLSVI IGHDHRHNSS QFAKLTATAF
ILKGIKVYFL EDLVHTPLVP FGLNLLGANA GVMITASHNP ARDNGYKVYW GNGCQIIPPV
DAGIAAAISE NLIPLEGAWD TSVLDKAVGL VENVKGRVEE AYFEKVKGLV DGMAVEGAGK
VGFVYTPMHG VGLEAAKQVV KILGVEEDFV VVEEQAKPDP DFPTVKFPNP EEKGALDLAM
AAADKHGITI VLANDPDADR FAAAEKVNGK WQILTGNQLG VLFASHMVST SSLPASKVAL
LSSAVSTQML AAMGQIDGFH HEETLTGFKW LGNVAQQITS KGTHKAIYAF EEAIGYMFSD
VVHDKDGIAA LSVFVTMLKK WLSEGTTPAG KLQELYEKYG FFESCNGYVV SPSPDVTRQV
FDGIRRLGDE SGKKFPGSLG GREINYWRDL TEGYDSATIN GIPVLPVDRS SQMITVGMDG
VRFTIRGSGT EPKIKYYVEA KASGKEEASA AAKEVADAIV REWFKPEVHG LIVS
//
