ID   A0A0D7BPV7_9AGAR        Unreviewed;       586 AA.
AC   A0A0D7BPV7;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=Phosphoglucomutase 1 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=CYLTODRAFT_345563 {ECO:0000313|EMBL:KIY71646.1};
OS   Cylindrobasidium torrendii FP15055 ss-10.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Marasmiineae; Physalacriaceae;
OC   Cylindrobasidium.
OX   NCBI_TaxID=1314674 {ECO:0000313|EMBL:KIY71646.1, ECO:0000313|Proteomes:UP000054007};
RN   [1] {ECO:0000313|EMBL:KIY71646.1, ECO:0000313|Proteomes:UP000054007}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FP15055 ss-10 {ECO:0000313|EMBL:KIY71646.1,
RC   ECO:0000313|Proteomes:UP000054007};
RX   PubMed=25683379; DOI=10.1016/j.fgb.2015.02.002;
RA   Floudas D., Held B.W., Riley R., Nagy L.G., Koehler G., Ransdell A.S.,
RA   Younus H., Chow J., Chiniquy J., Lipzen A., Tritt A., Sun H., Haridas S.,
RA   LaButti K., Ohm R.A., Kues U., Blanchette R.A., Grigoriev I.V., Minto R.E.,
RA   Hibbett D.S.;
RT   "Evolution of novel wood decay mechanisms in Agaricales revealed by the
RT   genome sequences of Fistulina hepatica and Cylindrobasidium torrendii.";
RL   Fungal Genet. Biol. 76:78-92(2015).
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; KN880452; KIY71646.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0D7BPV7; -.
DR   STRING; 1314674.A0A0D7BPV7; -.
DR   OrthoDB; 1482at2759; -.
DR   Proteomes; UP000054007; 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   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   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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054007}.
FT   DOMAIN          44..182
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          212..308
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          319..445
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
SQ   SEQUENCE   586 AA;  64491 MW;  C9D1BAF3626EED8A CRC64;
     MTSLDTLVDN WLRLDKNEAT RNEVLALRQA GNTDELERRM RKRIEFGTAG LRGRMEAGWA
     RMNDLIIIQA SQGLCKYVLE HVDNAATRGV VVGHDHRYNS ERWAQLTAAS LIANGVKVYL
     HRGLVHTPLV PFSVKELNAA AGIMVTASHN PKQDNGYKVY WENAVQIISP HDAGIAASIL
     ANLEPQETDL AGVTSSSLCL DVTEKMKNAY FENLLKSNTG SDYKIKFVNT SMHGVGAPFV
     SRAFELFGFQ PPVHVAAQQE PDPEFPTVAF PNPEEHGALN LALETANAEN ATYVLAQDPD
     ADRFAAAEHL PDGTWHAFTG DQLGTLFAAH VFSKYRSSGK PLSKLAMVAS TVSSKMVEAI
     ALAEGFTFVE CLTGFKYIGN TAMDLQAQGF EVPFGYEEAI GFMFGDTIRD KDGVSASVTF
     VQLVEELAKE GRTAKTFLTD LYRKYGYFET RNNYFICTEA ATIDAIFTRI RSYDGTNARS
     YPTSIAGLTV TRVVDLTTGY DSANAPSYKP ALPISSGHMI QFRAENKDEG VKIVLTVRTS
     GTEPKIKYYL EGSCKDASKV RPTLVQVVDE LSDMWVQAKK NNLARP
//