ID M7WTV5_RHOT1 Unreviewed; 604 AA.
AC M7WTV5;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=Phosphoglucomutase {ECO:0000313|EMBL:EMS21300.1};
GN ORFNames=RHTO_01766 {ECO:0000313|EMBL:EMS21300.1};
OS Rhodotorula toruloides (strain NP11) (Yeast) (Rhodosporidium toruloides).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX NCBI_TaxID=1130832 {ECO:0000313|EMBL:EMS21300.1, ECO:0000313|Proteomes:UP000016926};
RN [1] {ECO:0000313|EMBL:EMS21300.1, ECO:0000313|Proteomes:UP000016926}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NP11 {ECO:0000313|EMBL:EMS21300.1,
RC ECO:0000313|Proteomes:UP000016926};
RX PubMed=23047670; DOI=10.1038/ncomms2112;
RA Zhu Z., Zhang S., Liu H., Shen H., Lin X., Yang F., Zhou Y.J., Jin G.,
RA Ye M., Zou H., Zou H., Zhao Z.K.;
RT "A multi-omic map of the lipid-producing yeast Rhodosporidium toruloides.";
RL Nat. Commun. 3:1112-1112(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}.
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DR EMBL; KB722656; EMS21300.1; -; Genomic_DNA.
DR RefSeq; XP_016272419.1; XM_016415445.1.
DR AlphaFoldDB; M7WTV5; -.
DR SMR; M7WTV5; -.
DR GeneID; 27365779; -.
DR eggNOG; KOG1220; Eukaryota.
DR HOGENOM; CLU_016950_0_0_1; -.
DR OrthoDB; 1482at2759; -.
DR Proteomes; UP000016926; 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 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;
FT DOMAIN 46..182
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 210..315
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 325..450
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
SQ SEQUENCE 604 AA; 66143 MW; CD19D294076E5C54 CRC64;
MDRTKLNEAV TDWLRLDRNP ETRAEVENLV NAGDFAELEK RFARRIAFGT AGLRGPMQTG
PSAINDLVIL QASQGLAKYA EQSIEGAKEK GIVVGHDHRH NSVQFARLTA GVFRRRGWRV
YELDGLVHTP MVPFSVKQLG AAVGVMITAS HNPARDNGYK VYWSNAIQII PPHDSGIAAA
ILESLDVDEG AWDPPKDATG WDGTHELVKQ YMDMVKQLST NASTNASSSL LFTYTAMHGV
GLPFALDALS AFGFSRDRVS IVKEQAQPDP DFPTVKFPNP EEKGALDLAI AHADNVGSTL
VLANDPDADR FCAAEKVQGK WTIFTGDQIG ALLGSYALER YRQTGAPIEK LAMCASTVSS
KMLRSMARKE GFRFEETLTG FKWIGNELQA LEDQGFAPWF AYEEAIGFAN GTSIKDKDGV
TALALFAEMA ATLARFGKPL TVHLDSLYYE YGFHATLNSY FICRDSAKTN RIFSTLRFGN
PSIDSSTASP ASLSLPTHLG GFRLTSLRDL TVGYDSTNPP TYEPKLPVDR SAHMISFSLG
ETESGDGVEV VGTVRTSGTE PKIKYYLEAR GGNRQAVRAK LEHVRMALGS EWLRAEENGL
EKPE
//
