(data stored in SCRATCH zone)

SWISSPROT: A8LDS9_FRASN

ID   A8LDS9_FRASN            Unreviewed;       306 AA.
AC   A8LDS9;
DT   04-DEC-2007, integrated into UniProtKB/TrEMBL.
DT   04-DEC-2007, sequence version 1.
DT   10-APR-2019, entry version 62.
DE   RecName: Full=Pseudouridine-5'-phosphate glycosidase {ECO:0000256|HAMAP-Rule:MF_01876};
DE            Short=PsiMP glycosidase {ECO:0000256|HAMAP-Rule:MF_01876};
DE            EC=4.2.1.70 {ECO:0000256|HAMAP-Rule:MF_01876};
GN   Name=psuG {ECO:0000256|HAMAP-Rule:MF_01876};
GN   OrderedLocusNames=Franean1_0227 {ECO:0000313|EMBL:ABW09694.1};
OS   Frankia sp. (strain EAN1pec).
OC   Bacteria; Actinobacteria; Frankiales; Frankiaceae; Frankia.
OX   NCBI_TaxID=298653 {ECO:0000313|EMBL:ABW09694.1, ECO:0000313|Proteomes:UP000001313};
RN   [1] {ECO:0000313|Proteomes:UP000001313}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EAN1pec {ECO:0000313|Proteomes:UP000001313};
RX   PubMed=17151343; DOI=10.1101/gr.5798407;
RA   Normand P., Lapierre P., Tisa L.S., Gogarten J.P., Alloisio N.,
RA   Bagnarol E., Bassi C.A., Berry A.M., Bickhart D.M., Choisne N.,
RA   Couloux A., Cournoyer B., Cruveiller S., Daubin V., Demange N.,
RA   Francino M.P., Goltsman E., Huang Y., Kopp O.R., Labarre L.,
RA   Lapidus A., Lavire C., Marechal J., Martinez M., Mastronunzio J.E.,
RA   Mullin B.C., Niemann J., Pujic P., Rawnsley T., Rouy Z.,
RA   Schenowitz C., Sellstedt A., Tavares F., Tomkins J.P., Vallenet D.,
RA   Valverde C., Wall L.G., Wang Y., Medigue C., Benson D.R.;
RT   "Genome characteristics of facultatively symbiotic Frankia sp. strains
RT   reflect host range and host plant biogeography.";
RL   Genome Res. 17:7-15(2007).
CC   -!- FUNCTION: Catalyzes the reversible cleavage of pseudouridine 5'-
CC       phosphate (PsiMP) to ribose 5-phosphate and uracil. Functions
CC       biologically in the cleavage direction, as part of a pseudouridine
CC       degradation pathway. {ECO:0000256|HAMAP-Rule:MF_01876}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-ribose 5-phosphate + uracil = H2O + psi-UMP;
CC         Xref=Rhea:RHEA:18337, ChEBI:CHEBI:15377, ChEBI:CHEBI:17568,
CC         ChEBI:CHEBI:58380, ChEBI:CHEBI:78346; EC=4.2.1.70;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01876,
CC         ECO:0000256|SAAS:SAAS01152484};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01876};
CC       Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01876};
CC   -!- SUBUNIT: Homotrimer. {ECO:0000256|HAMAP-Rule:MF_01876}.
CC   -!- SIMILARITY: Belongs to the pseudouridine-5'-phosphate glycosidase
CC       family. {ECO:0000256|HAMAP-Rule:MF_01876}.
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DR   EMBL; CP000820; ABW09694.1; -; Genomic_DNA.
DR   RefSeq; WP_012157671.1; NC_009921.1.
DR   STRING; 298653.Franean1_0227; -.
DR   EnsemblBacteria; ABW09694; ABW09694; Franean1_0227.
DR   KEGG; fre:Franean1_0227; -.
DR   eggNOG; ENOG4105D53; Bacteria.
DR   eggNOG; COG2313; LUCA.
DR   HOGENOM; HOG000064311; -.
DR   KO; K16329; -.
DR   OMA; IIAHGMP; -.
DR   OrthoDB; 1294333at2; -.
DR   BioCyc; FSP298653:G1G9X-219-MONOMER; -.
DR   Proteomes; UP000001313; Chromosome.
DR   GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004730; F:pseudouridylate synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046113; P:nucleobase catabolic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.1790.10; -; 1.
DR   HAMAP; MF_01876; PsiMP_glycosidase; 1.
DR   InterPro; IPR022830; Indigdn_synthA-like.
DR   InterPro; IPR007342; PsuG.
DR   PANTHER; PTHR42909; PTHR42909; 1.
DR   Pfam; PF04227; Indigoidine_A; 1.
DR   SUPFAM; SSF110581; SSF110581; 1.
PE   3: Inferred from homology;
DR   PRODOM; A8LDS9.
DR   SWISS-2DPAGE; A8LDS9.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001313};
KW   Glycosidase {ECO:0000256|HAMAP-Rule:MF_01876,
KW   ECO:0000256|SAAS:SAAS01089065};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01876,
KW   ECO:0000256|SAAS:SAAS01089069};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_01876,
KW   ECO:0000256|SAAS:SAAS01089072};
KW   Manganese {ECO:0000256|HAMAP-Rule:MF_01876,
KW   ECO:0000256|SAAS:SAAS01089076};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01876,
KW   ECO:0000256|SAAS:SAAS01089073};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001313}.
FT   REGION      143    145       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01876}.
FT   ACT_SITE     28     28       Proton donor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01876}.
FT   ACT_SITE    162    162       Nucleophile. {ECO:0000256|HAMAP-Rule:
FT                                MF_01876}.
FT   METAL       141    141       Manganese. {ECO:0000256|HAMAP-Rule:
FT                                MF_01876}.
FT   BINDING      89     89       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01876}.
FT   BINDING     109    109       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01876}.
SQ   SEQUENCE   306 AA;  31399 MW;  3C7EF95D52F2E4BE CRC64;
     MISPGPGLAV SAEVSAALAA GRPVVALEST LIAHGLPRPR NRAVAVELEE MLRERGVTPA
     TVAVIDGVPT IGLDDATLSR VADDPAVAKA SVRDLPAAAA LRRTCATTVA STSMLAARAG
     IRVFATGGLG GVHRGAGESF DESADLPTLG GTPITVVSAG VKSILDVGAT LERMETLGIT
     LLGWRTSEFP GFYLPGSGHR LDWRVDDARQ VAGTMAARDR LGLTSAIVVA NPVPREQALD
     PGVHDRVLAE ALRRAEAGGL RGKAVTPFLL ETFRTETAGA SLEVNVAVVR SNVAVAAEIA
     TAWAAG
//

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