ID D4DDF6_TRIVH Unreviewed; 345 AA.
AC D4DDF6;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE RecName: Full=Phosphoglucomutase {ECO:0008006|Google:ProtNLM};
GN ORFNames=TRV_05167 {ECO:0000313|EMBL:EFE40098.1};
OS Trichophyton verrucosum (strain HKI 0517).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=663202 {ECO:0000313|EMBL:EFE40098.1, ECO:0000313|Proteomes:UP000008383};
RN [1] {ECO:0000313|Proteomes:UP000008383}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HKI 0517 {ECO:0000313|Proteomes:UP000008383};
RX PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT "Comparative and functional genomics provide insights into the
RT pathogenicity of dermatophytic fungi.";
RL Genome Biol. 12:R7.1-R7.16(2011).
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:EFE40098.1}.
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DR EMBL; ACYE01000265; EFE40098.1; -; Genomic_DNA.
DR RefSeq; XP_003020716.1; XM_003020670.1.
DR AlphaFoldDB; D4DDF6; -.
DR GeneID; 9577415; -.
DR KEGG; tve:TRV_05167; -.
DR HOGENOM; CLU_016950_0_1_1; -.
DR OrthoDB; 1482at2759; -.
DR Proteomes; UP000008383; Unassembled WGS sequence.
DR GO; GO:0016868; F:intramolecular phosphotransferase 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; 2.
DR Gene3D; 3.30.310.50; Alpha-D-phosphohexomutase, C-terminal domain; 1.
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; IPR005843; A-D-PHexomutase_C.
DR InterPro; IPR036900; A-D-PHexomutase_C_sf.
DR PANTHER; PTHR45745:SF1; PHOSPHOGLUCOMUTASE 2A-RELATED; 1.
DR PANTHER; PTHR45745; PHOSPHOMANNOMUTASE 45A; 1.
DR Pfam; PF02879; PGM_PMM_II; 1.
DR Pfam; PF02880; PGM_PMM_III; 1.
DR Pfam; PF00408; PGM_PMM_IV; 1.
DR SUPFAM; SSF55957; Phosphoglucomutase, C-terminal domain; 1.
DR SUPFAM; SSF53738; Phosphoglucomutase, first 3 domains; 2.
PE 4: Predicted;
FT DOMAIN 3..70
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 74..180
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 268..306
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 345 AA; 38364 MW; 63B5AE2E69B2B36B CRC64;
MSKLCASLGI EGIITVPEQE QPDPDFSTVK FPNPEENGAL DLAMKTADNS GVTLIVANDP
DADRFAAAEK VKFTGDHIGV LLASHLLDLW KNKKSEKPMA MLNSAVSSNM LSKMAEKEGF
HFEETLTGFK WMGNVARQLE TRGYEVPFAF EEALGYMFTK VCYDKDGLTA AMVFLAAEAK
WKEQGLTPFG KLEQLYEMYG YHENLNTYFV SPDTKSTTSL FESIRKNTLD AQGTIGSFPI
HRWRDMTRGY DSDTADKRPV LPVDPASQML TIWSHRGIRF TIRGSGTEPK VKIYIESCGA
SRNDAVEAVC DLLTAVVENW IKPYAPAMTY FNSMTTSSGH ILKLA
//
