ID Q6C7B1_YARLI Unreviewed; 595 AA.
AC Q6C7B1;
DT 16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT 16-AUG-2004, sequence version 1.
DT 27-MAR-2024, entry version 104.
DE SubName: Full=YALI0E02244p {ECO:0000313|EMBL:CAG79030.1};
GN ORFNames=YALI0_E02244g {ECO:0000313|EMBL:CAG79030.1};
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591 {ECO:0000313|EMBL:CAG79030.1, ECO:0000313|Proteomes:UP000001300};
RN [1] {ECO:0000313|EMBL:CAG79030.1, ECO:0000313|Proteomes:UP000001300}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150 {ECO:0000313|Proteomes:UP000001300};
RX PubMed=15229592; DOI=10.1038/nature02579;
RG Genolevures;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.F., Straub M.L.,
RA Suleau A., Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E.,
RA Wirth B., Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA Wincker P., Souciet J.L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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; CR382131; CAG79030.1; -; Genomic_DNA.
DR RefSeq; XP_503451.1; XM_503451.1.
DR AlphaFoldDB; Q6C7B1; -.
DR STRING; 284591.Q6C7B1; -.
DR EnsemblFungi; CAG79030; CAG79030; YALI0_E02244g.
DR GeneID; 2912087; -.
DR KEGG; yli:YALI0E02244g; -.
DR VEuPathDB; FungiDB:YALI0_E02244g; -.
DR HOGENOM; CLU_016950_0_1_1; -.
DR InParanoid; Q6C7B1; -.
DR OMA; GYCVDPE; -.
DR OrthoDB; 1482at2759; -.
DR Proteomes; UP000001300; Chromosome E.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0008973; F:phosphopentomutase activity; IBA:GO_Central.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0046115; P:guanosine catabolic process; IEA:EnsemblFungi.
DR GO; GO:0006148; P:inosine catabolic process; IEA:EnsemblFungi.
DR GO; GO:0006166; P:purine ribonucleoside salvage; IBA:GO_Central.
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 Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Magnesium {ECO:0000256|RuleBase:RU004326};
KW Metal-binding {ECO:0000256|RuleBase:RU004326};
KW Reference proteome {ECO:0000313|Proteomes:UP000001300}.
FT DOMAIN 42..180
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 212..322
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 329..450
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
SQ SEQUENCE 595 AA; 66151 MW; AA5631B0FBC62D43 CRC64;
MTTTLVKQWL DLDQNPVTRK QIEDLQTAND TKQLETLLSK RISFGTAGLR ARMEAGFARM
NDVTVLQASI GLASYVDREV PDATSKGVVI GHDHRHNSEQ FAKLTALAFV NKGFKVYLFK
GLVHTPIVPF AIDALGASCG VMVTASHNPA ADNGYKVYWG NGCQIIPPHD TGIAAEIDAL
ADKTTKFEWD LSKLDKLIEG ETIDNRTEMQ QKYNDNLKNL VHHKFEPSGP LASGVVYTAM
HGVGYLPSIE AFKLFGIPLE DVFSVRKQQE PNPDFPTVAF PNPEEHGALD LAMKLGDAQG
ADLIVANDPD ADRFAVAVKE NGDKWVQLTG NQIGILFSAY QWDQYKNSGK KIAMLNSTVS
SQMLKFMAEK EGFLYEDTLT GFKWIGNRAI DLEKEGYTVP FAYEEAIGYM FPGVHDKDGV
SASLVFLQLA QAYGGGAKLI EKLNSLYDKY GHFAEKNGYY IAKTPELTTE AFKHVRSYFK
GRFQKGDYPK TIGPFDVTSW RDLTTGYDST TPDHKPTLPV SPSTEMITAT LATHDNPDEF
IRFTARGSGT EPKLKIYIDA KAASTERAQE LAQETWDALD EEWWRPEESG LQRVH
//
