ID A0A1Y1VYZ1_9FUNG Unreviewed; 616 AA.
AC A0A1Y1VYZ1;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=Phosphoglucomutase, first 3 domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=DL89DRAFT_279131 {ECO:0000313|EMBL:ORX66479.1};
OS Linderina pennispora.
OC Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota; Kickxellomycotina;
OC Kickxellomycetes; Kickxellales; Kickxellaceae; Linderina.
OX NCBI_TaxID=61395 {ECO:0000313|EMBL:ORX66479.1, ECO:0000313|Proteomes:UP000193922};
RN [1] {ECO:0000313|EMBL:ORX66479.1, ECO:0000313|Proteomes:UP000193922}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12442 {ECO:0000313|EMBL:ORX66479.1,
RC ECO:0000313|Proteomes:UP000193922};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (JUL-2016) 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}.
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:ORX66479.1}.
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DR EMBL; MCFD01000015; ORX66479.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y1VYZ1; -.
DR STRING; 61395.A0A1Y1VYZ1; -.
DR OrthoDB; 1482at2759; -.
DR Proteomes; UP000193922; 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 Reference proteome {ECO:0000313|Proteomes:UP000193922}.
FT DOMAIN 49..188
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 213..317
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 328..453
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
SQ SEQUENCE 616 AA; 67796 MW; 8B568328715D3E21 CRC64;
MSSAAEPIST LVERWLSQDK DPKTRAQIQA LADANDTEAL EALLRHPIEF GTAGLRARME
AGYSRLNQLT VITASQGLAA YVAENVTGAC ERGVVVGHDH RYNSDVFAQL TVRAFLDAGY
RVYFYPGIGL TPEVPFAVKF LKAACGVMVT ASHNPKDDNG YKVYWENGAQ IKPPLDVGIA
RSIQQHSEPR NWSVEGVEND PKVDDVTERM MNEYFKAAEH LVADRAANAA TELRYVYTAM
HGVGAPFAAR ILDTFGLPPY VAVPEQIAAD PDFPTVSFPN PEEKGALDMA KALADTQGIE
LVVANDPDAD RFAAAEKQAD GTWHSFTGDQ LGSIFAAAVL EMARTDQVPT EKLAMVNSTV
SSRMLEAMAA KEGFKYADTL TGFKWMANEL AALQKDGYFV GFGYEEAIGY MIHDQVLDKD
GVTAMGVFVQ LAARLHKQGR RVHDYLEDQY AKYGFFVSSN SYVISNDPKK TTEIFSRIRF
GPTQPESGDV ERTELARATD VLRYPKSIGG FPVSYIRDLT VGFEMRDVDI QDVKISVAED
QFVPTFPVDH GAHMITFETR NGGRLTMRTS GTEPKLKYYL EVRSPSNDRA AAARDLDVMS
TAVLEELIQA SKNGLL
//