PSUG_THEMA
ID PSUG_THEMA Reviewed; 285 AA.
AC Q9X1H5;
DT 19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Pseudouridine-5'-phosphate glycosidase {ECO:0000255|HAMAP-Rule:MF_01876, ECO:0000303|PubMed:18591240};
DE Short=PsiMP glycosidase {ECO:0000255|HAMAP-Rule:MF_01876, ECO:0000303|PubMed:18591240};
DE EC=4.2.1.70 {ECO:0000255|HAMAP-Rule:MF_01876, ECO:0000269|PubMed:18591240};
GN Name=psuG {ECO:0000255|HAMAP-Rule:MF_01876};
GN Synonyms=indA {ECO:0000303|PubMed:18591240}; OrderedLocusNames=TM_1464;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=18591240; DOI=10.1074/jbc.m804122200;
RA Preumont A., Snoussi K., Stroobant V., Collet J.-F., Van Schaftingen E.;
RT "Molecular identification of pseudouridine-metabolizing enzymes.";
RL J. Biol. Chem. 283:25238-25246(2008).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH MANGANESE, AND
RP SUBUNIT.
RX PubMed=15822122; DOI=10.1002/prot.20420;
RA Levin I., Miller M.D., Schwarzenbacher R., McMullan D., Abdubek P.,
RA Ambing E., Biorac T., Cambell J., Canaves J.M., Chiu H.-J., Deacon A.M.,
RA DiDonato M., Elsliger M.-A., Godzik A., Grittini C., Grzechnik S.K.,
RA Hale J., Hampton E., Han G.W., Haugen J., Hornsby M., Jaroszewski L.,
RA Karlak C., Klock H.E., Koesema E., Kreusch A., Kuhn P., Lesley S.A.,
RA Morse A., Moy K., Nigoghossian E., Ouyang J., Page R., Quijano K.,
RA Reyes R., Robb A., Sims E., Spraggon G., Stevens R.C., van den Bedem H.,
RA Velasquez J., Vincent J., Wang X., West B., Wolf G., Xu Q., Zagnitko O.,
RA Hodgson K.O., Wooley J., Wilson I.A.;
RT "Crystal structure of an indigoidine synthase A (IndA)-like protein
RT (TM1464) from Thermotoga maritima at 1.90 A resolution reveals a new
RT fold.";
RL Proteins 59:864-868(2005).
CC -!- FUNCTION: Catalyzes the hydrolysis of pseudouridine 5'-phosphate
CC (PsiMP) to ribose 5-phosphate and uracil.
CC {ECO:0000269|PubMed:18591240}.
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:0000255|HAMAP-Rule:MF_01876,
CC ECO:0000269|PubMed:18591240}.
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:0000255|HAMAP-Rule:MF_01876,
CC ECO:0000269|PubMed:18591240};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01876,
CC ECO:0000269|PubMed:15822122, ECO:0000303|PubMed:18591240};
CC Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01876,
CC ECO:0000269|PubMed:15822122, ECO:0000303|PubMed:18591240};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC No activity can be observed at or below 50 degrees Celsius.
CC {ECO:0000269|PubMed:18591240};
CC -!- SUBUNIT: Homotrimer. {ECO:0000255|HAMAP-Rule:MF_01876,
CC ECO:0000269|PubMed:15822122}.
CC -!- SIMILARITY: Belongs to the pseudouridine-5'-phosphate glycosidase
CC family. {ECO:0000255|HAMAP-Rule:MF_01876}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE000512; AAD36532.1; -; Genomic_DNA.
DR PIR; A72252; A72252.
DR RefSeq; NP_229264.1; NC_000853.1.
DR RefSeq; WP_004081760.1; NZ_CP011107.1.
DR PDB; 1VKM; X-ray; 1.90 A; A/B/C/D/E/F=1-285.
DR PDBsum; 1VKM; -.
DR AlphaFoldDB; Q9X1H5; -.
DR SMR; Q9X1H5; -.
DR STRING; 243274.THEMA_06990; -.
DR EnsemblBacteria; AAD36532; AAD36532; TM_1464.
DR KEGG; tma:TM1464; -.
DR eggNOG; COG2313; Bacteria.
DR InParanoid; Q9X1H5; -.
DR OMA; RKLGHRD; -.
DR OrthoDB; 1294333at2; -.
DR EvolutionaryTrace; Q9X1H5; -.
DR Proteomes; UP000008183; 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 1: Evidence at protein level;
KW 3D-structure; Glycosidase; Hydrolase; Lyase; Manganese; Metal-binding;
KW Reference proteome.
FT CHAIN 1..285
FT /note="Pseudouridine-5'-phosphate glycosidase"
FT /id="PRO_0000390555"
FT ACT_SITE 17
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01876"
FT ACT_SITE 147
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01876"
FT BINDING 77
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01876"
FT BINDING 97
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01876"
FT BINDING 126
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01876,
FT ECO:0000269|PubMed:15822122"
FT BINDING 128..130
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01876"
FT STRAND 3..5
FT /evidence="ECO:0007829|PDB:1VKM"
FT STRAND 13..16
FT /evidence="ECO:0007829|PDB:1VKM"
FT HELIX 19..22
FT /evidence="ECO:0007829|PDB:1VKM"
FT HELIX 27..44
FT /evidence="ECO:0007829|PDB:1VKM"
FT STRAND 47..54
FT /evidence="ECO:0007829|PDB:1VKM"
FT STRAND 57..61
FT /evidence="ECO:0007829|PDB:1VKM"
FT HELIX 64..73
FT /evidence="ECO:0007829|PDB:1VKM"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:1VKM"
FT HELIX 80..82
FT /evidence="ECO:0007829|PDB:1VKM"
FT HELIX 83..89
FT /evidence="ECO:0007829|PDB:1VKM"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:1VKM"
FT HELIX 97..106
FT /evidence="ECO:0007829|PDB:1VKM"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:1VKM"
FT HELIX 129..134
FT /evidence="ECO:0007829|PDB:1VKM"
FT STRAND 139..146
FT /evidence="ECO:0007829|PDB:1VKM"
FT HELIX 152..161
FT /evidence="ECO:0007829|PDB:1VKM"
FT STRAND 166..170
FT /evidence="ECO:0007829|PDB:1VKM"
FT HELIX 192..204
FT /evidence="ECO:0007829|PDB:1VKM"
FT STRAND 209..214
FT /evidence="ECO:0007829|PDB:1VKM"
FT HELIX 219..221
FT /evidence="ECO:0007829|PDB:1VKM"
FT HELIX 225..233
FT /evidence="ECO:0007829|PDB:1VKM"
FT HELIX 241..243
FT /evidence="ECO:0007829|PDB:1VKM"
FT HELIX 244..255
FT /evidence="ECO:0007829|PDB:1VKM"
FT TURN 256..258
FT /evidence="ECO:0007829|PDB:1VKM"
FT HELIX 259..282
FT /evidence="ECO:0007829|PDB:1VKM"
SQ SEQUENCE 285 AA; 31728 MW; 9657B169EC62DB74 CRC64;
MIIESRIEKG KPVVGMETTV FVHGLPRKEA IELFRRAKEI SREKGFQLAV IGILKGKIVA
GMSEEELEAM MREGADKVGT REIPIVVAEG KNAATTVSAT IFLSRRIGIE VVVTGGTGGV
HPGRVDVSQD LTEMSSSRAV LVSSGIKSIL DVEATFEMLE TLEIPLVGFR TNEFPLFFSR
KSGRRVPRIE NVEEVLKIYE SMKEMELEKT LMVLNPVPEE YEIPHDEIER LLEKIELEVE
GKEVTPFLLK KLVEMTNGRT LKANLALLEE NVKLAGEIAV KLKRS
