ID A0A0L1J367_ASPNO Unreviewed; 596 AA.
AC A0A0L1J367;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=Phosphoglucomutase {ECO:0000313|EMBL:KNG86251.1};
GN ORFNames=ANOM_004504 {ECO:0000313|EMBL:KNG86251.1};
OS Aspergillus nomiae NRRL 13137.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1509407 {ECO:0000313|EMBL:KNG86251.1, ECO:0000313|Proteomes:UP000037505};
RN [1] {ECO:0000313|EMBL:KNG86251.1, ECO:0000313|Proteomes:UP000037505}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 13137 {ECO:0000313|EMBL:KNG86251.1,
RC ECO:0000313|Proteomes:UP000037505};
RA Moore M.G., Shannon B.M., Brian M.M.;
RT "The Genome of the Aflatoxigenic Filamentous Fungus Aspergillus nomius.";
RL Submitted (JUN-2014) 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}.
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:KNG86251.1}.
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DR EMBL; JNOM01000122; KNG86251.1; -; Genomic_DNA.
DR RefSeq; XP_015407174.1; XM_015549761.1.
DR AlphaFoldDB; A0A0L1J367; -.
DR STRING; 1509407.A0A0L1J367; -.
DR GeneID; 26806308; -.
DR OrthoDB; 1482at2759; -.
DR Proteomes; UP000037505; 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; 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 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:UP000037505}.
FT DOMAIN 45..183
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 212..314
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 324..430
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
SQ SEQUENCE 596 AA; 66026 MW; 347002ACC5A3EB93 CRC64;
MVDSLSPLIQ KWLEWDQDPT TRAEIQQLRD SGAIADLEQR LQKRIQFGTA GLRGRMAAGF
SCMNSLTVIQ ASQGLAKYLK EKHTDIASGG VVIGHDARHN SAKFAALAAN AFISQQIPVW
FYSEPSVTPS VPFGVTHLKA AAGIMITASH NPAQDNGYKV YFKNGAQINT PVDVEIAQSI
EENLAPWPGA WKDLQACEYL HADAYKTILP HYTKTVWDYA NSTVSDWKQP RPFVYTPLHG
VGGLVFPDLC RSVGVTEFTP VPEQVEPNPD FPTVSFPNPE EAGALDLAMQ TADKEGKTLI
IAHDPDADRF AAAEKVDGSW FSFTGNHIGV LLASHLFDSL ENKKDDTRIA VLNSTVSTGM
VEKMATARGI QFEEALTGFK WMGNIARRLE GEGYTVPYAF EEALGYMFPA VCHDKDGITA
AMVFLAAQAK WQSQGLTPYM KLQQLFKEFG HYETLNNYFR SPNPETTMAL FGAIRNGPYR
TEKTLGPFKI LRWRDMTEGY DSGTADNKPT LPVDKSSQML TLWLDQDVRF TFRASGTEPK
VKLYVESCGA SREQAVDAVC NAFLAVLKEW VLPFAPSMTY SRQMPTSSGH VFQIPE
//
