ID   F2SI61_TRIRC            Unreviewed;       594 AA.
AC   F2SI61;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   RecName: Full=Phosphoglucomutase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=TERG_02601 {ECO:0000313|EMBL:EGD86344.1};
OS   Trichophyton rubrum (strain ATCC MYA-4607 / CBS 118892) (Athlete's foot
OS   fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=559305 {ECO:0000313|EMBL:EGD86344.1, ECO:0000313|Proteomes:UP000008864};
RN   [1] {ECO:0000313|Proteomes:UP000008864}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4607 / CBS 118892 {ECO:0000313|Proteomes:UP000008864};
RX   PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA   Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA   Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA   Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA   Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA   Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT   "Comparative genome analysis of Trichophyton rubrum and related
RT   dermatophytes reveals candidate genes involved in infection.";
RL   MBio 3:E259-E259(2012).
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; GG700649; EGD86344.1; -; Genomic_DNA.
DR   RefSeq; XP_003237893.1; XM_003237845.1.
DR   AlphaFoldDB; F2SI61; -.
DR   STRING; 559305.F2SI61; -.
DR   GeneID; 10376783; -.
DR   VEuPathDB; FungiDB:TERG_02601; -.
DR   eggNOG; KOG1220; Eukaryota.
DR   HOGENOM; CLU_016950_0_1_1; -.
DR   InParanoid; F2SI61; -.
DR   OMA; GYCVDPE; -.
DR   OrthoDB; 1482at2759; -.
DR   Proteomes; UP000008864; 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:UP000008864}.
FT   DOMAIN          44..181
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          211..313
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          323..429
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
SQ   SEQUENCE   594 AA;  66273 MW;  CC511664729AC027 CRC64;
     MEPLDTLIQR WLEWDQDPST RREIEKLQAD KDDAGLEKRL RERIQFGTAG LRGRMQAGFS
     CMNSLTVIQA SQGLAKFIKA THRGTEQPSV VIGRDARHNS EKFAFLAANS FEAEGIHVWW
     YDDVNPTPFV PFAVLLKKAD AGVMVTASHN PAQDNGYKVY FANGAQINSP IDGQIAESIR
     TNLVPWPNAW RGIDGPQTRE SDLHDEVSAL YCETVNRFAK STVDNWRQPS KFVYTPMHGV
     GHATMSKLCA SLGIDGIITV LEQEQPDPDF STVKFPNPEE NGALDLAMKT ADNSGVTLIV
     ANDPDADRFA AAEKVNGSWF RFTGDHIGVL LASHLLDLWK NKKSEKPMAM LNSAVSSNML
     SKMAEKEGFH FEETLTGFKW MGNVARQLEA RGYEVPFAFE EALGYMFTKV CYDKDGLTAA
     MVFLAAEAKW KEQGLTPLGK LEQLYETYGY HENLNTYFIS PDTKSTTSLF ESIRKNTLDA
     QGTIGSFPIH RWRDMTRGYD SDTADKRPVL PVDPASQMLT IWSHRGIRFT IRGSGTEPKV
     KIYIESCGAS RNDAVEAVCD LLTAVVENWI KPYAPAMTYF NSMTTSSGHI LKLA
//