ID F4P7V1_BATDJ Unreviewed; 594 AA.
AC F4P7V1;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=Phosphoglucomutase {ECO:0008006|Google:ProtNLM};
GN ORFNames=BATDEDRAFT_35697 {ECO:0000313|EMBL:EGF78536.1};
OS Batrachochytrium dendrobatidis (strain JAM81 / FGSC 10211) (Frog chytrid
OS fungus).
OC Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC Chytridiomycota incertae sedis; Chytridiomycetes; Rhizophydiales;
OC Rhizophydiales incertae sedis; Batrachochytrium.
OX NCBI_TaxID=684364 {ECO:0000313|EMBL:EGF78536.1, ECO:0000313|Proteomes:UP000007241};
RN [1] {ECO:0000313|EMBL:EGF78536.1, ECO:0000313|Proteomes:UP000007241}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JAM81 / FGSC 10211 {ECO:0000313|Proteomes:UP000007241};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Kuo A., Salamov A., Schmutz J., Lucas S., Pitluck S., Rosenblum E.,
RA Stajich J., Eisen M., Grigoriev I.V.;
RT "The draft genome of Batrachochytrium dendrobatidis.";
RL Submitted (DEC-2009) 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}.
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DR EMBL; GL882888; EGF78536.1; -; Genomic_DNA.
DR RefSeq; XP_006680791.1; XM_006680728.1.
DR AlphaFoldDB; F4P7V1; -.
DR STRING; 684364.F4P7V1; -.
DR GeneID; 18240846; -.
DR HOGENOM; CLU_016950_0_1_1; -.
DR InParanoid; F4P7V1; -.
DR OMA; GYCVDPE; -.
DR OrthoDB; 1482at2759; -.
DR Proteomes; UP000007241; Unassembled WGS sequence.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0008973; F:phosphopentomutase activity; IBA:GO_Central.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0006166; P:purine ribonucleoside salvage; IBA:GO_Central.
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 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:UP000007241}.
FT DOMAIN 44..179
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 209..314
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 324..450
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
SQ SEQUENCE 594 AA; 65289 MW; E4CD4568B8C40765 CRC64;
MNSTTSLAHE YLALDQNPVT HAEIKGLLDS ANHDKLQKLL STRIAFGTAG LRAEMGGGYS
RMNELTVIQA SQGVCAYYLD TVPDFKSKGV VIGHDHRHNS DAFARLTAAV FASKGIKVYY
YRDLVHTPMV PFGVTSLGAG CGIMITASHN PKQDNGYKLY AGNGCQIISP HDSLIAEQIL
LNLKPWTWDY ELINTSSLVT DPINEMYPAY FAKLKSLSVF HEKNAIQNVK FCYTAMHGVG
LTPALKVFEA FGLSPFVQTA EQVNPDPEFP TVAYPNPEEG KGALTLAMQT ADKNGATVIF
ANDPDADRLA IAEKKPNGEW HIFNGNEIGV ILATLVLESL RISGGAKRPL AMLTTTVSMH
MLKQVAKQEG FQFEETLTGF KWLGNRAIDL EKKGFQVAFA YEEAIGFMVG DAVRDKDGVS
ALGVVAEWAN HLATKGQTLH GYLLSLYEKY GYFTSNNGYF ICHEQSVINS LFDDIRYGKE
RKSAEAGSPY KYALQYPTTI GGSKVCWVRD LTIGYDTAQA DKKPTLPVSS SAQMLTLELE
NGALITLRTS GTEPKIKYYT ELRASTLAQA TKDLQIVVDS MIEICLRPKE HKLV
//