ID A0A0M9VNE6_9BASI Unreviewed; 551 AA.
AC A0A0M9VNE6;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 19.
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=Malapachy_1543 {ECO:0000313|EMBL:KOS13005.1};
OS Malassezia pachydermatis.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Malasseziomycetes; Malasseziales; Malasseziaceae; Malassezia.
OX NCBI_TaxID=77020 {ECO:0000313|EMBL:KOS13005.1, ECO:0000313|Proteomes:UP000037751};
RN [1] {ECO:0000313|EMBL:KOS13005.1, ECO:0000313|Proteomes:UP000037751}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 1879 {ECO:0000313|EMBL:KOS13005.1,
RC ECO:0000313|Proteomes:UP000037751};
RA Triana S., Ohm R., Gonzalez A., DeCock H., Restrepo S., Celis A.;
RT "Draft Genome Sequence of Malassezia furfur CBS1878 and Malassezia
RT pachydermatis CBS1879.";
RL Submitted (JUL-2015) 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, 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:KOS13005.1}.
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DR EMBL; LGAV01000007; KOS13005.1; -; Genomic_DNA.
DR RefSeq; XP_017990637.1; XM_018136047.1.
DR AlphaFoldDB; A0A0M9VNE6; -.
DR STRING; 77020.A0A0M9VNE6; -.
DR GeneID; 28727922; -.
DR VEuPathDB; FungiDB:Malapachy_1543; -.
DR OrthoDB; 5476118at2759; -.
DR Proteomes; UP000037751; Unassembled WGS sequence.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000037751}.
FT DOMAIN 13..152
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 184..286
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 297..413
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
SQ SEQUENCE 551 AA; 59309 MW; 441C99EB299A2F92 CRC64;
MAQTVATKPF EGQKPGTSGL RKRVKVFEQE NYTENFVQSI LSAIPGGAKG ATLVVGGDGR
YFSQPAVQKI VRLAAGNGVS KLIIGQNGIL STPAASHVIR LRKATGGILL TASHNPGGPN
ADFGIKYNME NGGPAPEGVT NKIYELTTKI DHYLVEQGED VDLASIGETT FGSMKVEVID
SVKDYVEYLS KIFDFDMIKS FLRSGSFKVR FDALHGVTGP YARALFVECF GLPEAAVQNC
VPSPDFGGGH PDPNLTYAKS LVDAVQQEGL DFGAASDGDG DRNMILGKNA FVNPSDSVAI
IADWAERAIP YFKSGVRGVA RSMPTSGAID LVAKERKYEC FEVPTGWKFF GNLMDAGRLS
ICGEESFGTG SDHIREKDGL WAVVAWLSIV SKANEEKPGT SVADVLQAHY EKYGRNFFSR
YDYEEVESAG ANAMMDGLRS KFADASFVGT SLGSFKVADA GDFSYTDPID GSVSKNQGLY
VRMEDGSRLV FRLSGTGSAG ATIRLYVEKY SSDPAEYKAD VQQALKPIID VALELSALQK
HTGREKPTVI T
//