ID A0A316Z7S9_9BASI Unreviewed; 690 AA.
AC A0A316Z7S9;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=Phosphomannomutase {ECO:0008006|Google:ProtNLM};
GN ORFNames=FA09DRAFT_330688 {ECO:0000313|EMBL:PWN97038.1};
OS Tilletiopsis washingtonensis.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Exobasidiomycetes; Entylomatales; Entylomatales incertae sedis;
OC Tilletiopsis.
OX NCBI_TaxID=58919 {ECO:0000313|EMBL:PWN97038.1, ECO:0000313|Proteomes:UP000245946};
RN [1] {ECO:0000313|EMBL:PWN97038.1, ECO:0000313|Proteomes:UP000245946}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 4186 {ECO:0000313|EMBL:PWN97038.1,
RC ECO:0000313|Proteomes:UP000245946};
RX PubMed=29771364; DOI=10.1093/molbev/msy072;
RA Kijpornyongpan T., Mondo S.J., Barry K., Sandor L., Lee J., Lipzen A.,
RA Pangilinan J., LaButti K., Hainaut M., Henrissat B., Grigoriev I.V.,
RA Spatafora J.W., Aime M.C.;
RT "Broad genomic sampling reveals a smut pathogenic ancestry of the fungal
RT clade Ustilaginomycotina.";
RL Mol. Biol. Evol. 0:0-0(2018).
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}.
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DR EMBL; KZ819296; PWN97038.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A316Z7S9; -.
DR STRING; 58919.A0A316Z7S9; -.
DR OrthoDB; 1482at2759; -.
DR Proteomes; UP000245946; 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; IPR005843; A-D-PHexomutase_C.
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 Pfam; PF00408; PGM_PMM_IV; 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 Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000245946}.
FT DOMAIN 144..281
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 312..411
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 423..538
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 620..658
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 690 AA; 73436 MW; FBE63B942AB81A94 CRC64;
MSGEAMEACP PLPRRGLQGS LDVRPLARPR SDARGAPDTN SLPVWGALSP SRLHLRPSHA
PVPTPPSLPS VLHRALPAHT LLPLCRTMAS STSDGHAALA STARAWLALD PDAKSRAALE
QLLADAEAEP AAAAELHAAF ASRLEFGTAG LRGVVGPGPA RMNRLVVMQT TAGLARYVRE
QRREQAGVVV AYDGRLDSEA FAHAAAGVLA AAGVRVHLFT VPAPTPMCGF MVRRLSAAAG
IVVTASHNPP EYNGYKVYCA AGTQINDPVD GEIAAHIDAV AQEGRTPPAC TLVEARAKDM
LSDLGEEDFE TYIGEVLRVT PAPSAPAAAF KVAYTPLHGV GAHIAERLLK RRGYQGFTVA
EQREPDGHFP TVKFPNPEEP GAMDLVMALA DEKQCAVAIA NDPDADRLCA AARDSTGKLR
QLTGDELGTL LGDAMLRQLS ADSAASPPWV LSTIVSSRLL ARLAGAYGAR HRETLTGFKW
LGPAASALTS KGERFAFAYE EALGYMACSL VWDKDGLSAL LALADLACAL DAEGKTLLGR
LEEIQRRVGV AITTQRTIRL QPGTSGSSIM KRVRAQKPDR IGDFELALVE DLLDGRPPAD
TPEGEIPKND VLRYFFATAD ISKESARKEI MLGAPRIQVR PSGTEPKVKI YCEALGEVRA
GESFEAAQQR IRAELDAIVD VVYAWLVADA
//
