ID W0TFF9_KLUMD Unreviewed; 613 AA.
AC W0TFF9;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=Phosphoglucomutase YMR278W {ECO:0000313|EMBL:BAO42362.1};
GN Name=PGM3 {ECO:0000313|EMBL:BAO42362.1};
GN ORFNames=KLMA_80051 {ECO:0000313|EMBL:BAO42362.1};
OS Kluyveromyces marxianus (strain DMKU3-1042 / BCC 29191 / NBRC 104275)
OS (Yeast) (Candida kefyr).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=1003335 {ECO:0000313|EMBL:BAO42362.1, ECO:0000313|Proteomes:UP000065495};
RN [1] {ECO:0000313|EMBL:BAO42362.1, ECO:0000313|Proteomes:UP000065495}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DMKU3-1042 / BCC 29191 / NBRC 104275
RC {ECO:0000313|Proteomes:UP000065495};
RX PubMed=25834639; DOI=10.1186/s13068-015-0227-x;
RA Lertwattanasakul N., Kosaka T., Hosoyama A., Suzuki Y., Rodrussamee N.,
RA Matsutani M., Murata M., Fujimoto N., Suprayogi, Tsuchikane K., Limtong S.,
RA Fujita N., Yamada M.;
RT "Genetic basis of the highly efficient yeast Kluyveromyces marxianus:
RT complete genome sequence and transcriptome analyses.";
RL Biotechnol. Biofuels 8:47-47(2015).
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; AP012220; BAO42362.1; -; Genomic_DNA.
DR AlphaFoldDB; W0TFF9; -.
DR VEuPathDB; FungiDB:KLMA_80051; -.
DR OrthoDB; 1482at2759; -.
DR Proteomes; UP000065495; Chromosome 8.
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:UniProtKB-KW.
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 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 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 Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
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}.
FT DOMAIN 57..201
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 223..335
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 349..459
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 560..585
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 613 AA; 68983 MW; CCB04044AB380017 CRC64;
MSMTDLTGIV SGLPADLQDK VRDWLRFDDV KETRDEIIGL CVQGNVEELH KRLDTRIAFG
TAGLRGRMEA GFSRMNALTV KQASQGLAKY IKAQFPENLT CVVGHDHRFN SKLFARTTID
VFLQLGFKVY DLNVVVGKEE DSYVHTPLVP FTVNAKGASV GIMITASHNP KMDNGYKVYY
ANGCQIIPPH DSLIAQSIAE NLEPFQSPKT GTVVDCKKEM TAAYIKAIRE KLVHDDLQNT
AAAGGPWFIY TPMHGVGFEI FEQIAKQAMS LEENRDYVVV QEQKYPDPAF PTVPFPNPEE
RGALDLAIEY GKAESHSGAD LIIANDPDAD RFSVAVRDKA SSTWRQLTGN EIGFLFAFYE
FEKYKASNIQ EPLAMINSTV SSQMIKRMAE IEGFHYEDTL TGFKWLGNRA LQLENENYYV
PFAYEEAIGY MFSSVVHDKD GIAAAVVFLQ AYSKWRQSGI EPLQILKQAS EKYGHFKEFN
GYYTVPDTSL TKKVFDTIRS IESPFPTKLG TKFKIEKFRD LTTGYQSDTP DHVPLLATDP
NSQMITCEMV LVEQPTSRVR FTIRGSGTEP KLKVYIEART TTEQASIALA KFTWDVLKQE
WFKPEFTGLV TPF
//
