ID A0A0D2AFE1_9EURO Unreviewed; 555 AA.
AC A0A0D2AFE1;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 24.
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=PV07_11774 {ECO:0000313|EMBL:KIW23587.1};
OS Cladophialophora immunda.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC Cladophialophora.
OX NCBI_TaxID=569365 {ECO:0000313|EMBL:KIW23587.1, ECO:0000313|Proteomes:UP000054466};
RN [1] {ECO:0000313|EMBL:KIW23587.1, ECO:0000313|Proteomes:UP000054466}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 83496 {ECO:0000313|EMBL:KIW23587.1,
RC ECO:0000313|Proteomes:UP000054466};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Cladophialophora immunda CBS83496.";
RL Submitted (JAN-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}.
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DR EMBL; KN847046; KIW23587.1; -; Genomic_DNA.
DR RefSeq; XP_016243803.1; XM_016399241.1.
DR AlphaFoldDB; A0A0D2AFE1; -.
DR STRING; 569365.A0A0D2AFE1; -.
DR GeneID; 27350968; -.
DR VEuPathDB; FungiDB:PV07_11774; -.
DR HOGENOM; CLU_009330_0_1_1; -.
DR OrthoDB; 5476118at2759; -.
DR Proteomes; UP000054466; 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 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:UP000054466}.
FT DOMAIN 15..155
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 186..289
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 300..417
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
SQ SEQUENCE 555 AA; 60742 MW; 1DDAD14702F4DF22 CRC64;
MASVKEVQFK SFTDQKPGTS GLRKKVTVFQ QPHYSESFIT SILLSIPEGA EGAFLVIGGD
GRYWNPEVVQ LIAKIGAAYG VKKLLIGQNG ILSTPAASHV IRIRKATGGI LLTASHNPGG
PKADFGMKYN LSNGAPAPES VTNKIFEKSK SLTSYKIADI PELDLSTIGT KKYGDLEVEI
VDSVADYMAM LKDIFDFDLI RSFFKSQPDF KVLFDGLSGV TGPYGVAIFQ GELGLGPEST
QNCQPSPDFN GGHPDPNLTY AHSLVERVDR EGIHFGAASD GDGDRNMIYG KNAFVSPGDS
LAIIAHYAQK YIPYFKKQGV YGLARSFPTS AALDLVAKKQ KLSIYVVPTG WKFFCALFDT
NKMSICGEES FGTGSNHIRE KDGLWAITAW LNIIAGVGKE TGKFPSIAEI QKEFWHEYGR
VYFTRYDYEN VSSDGANDMV KYLKEKIAKS DTVGSELQGR KILEADDFSY TDLDGSVSKN
QGIYFIFNDG TRVVVRLSGT GSSGATIRLY VEKLEEDKSK LGEDTQTYLK GSVGLAIELL
QLQKFIGRTE PDVKT
//
