QUEFL_PYRCJ
ID QUEFL_PYRCJ Reviewed; 109 AA.
AC A3MSP1;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Archaeosine synthase {ECO:0000303|PubMed:28383498};
DE EC=2.6.1.- {ECO:0000269|PubMed:28383498};
DE AltName: Full=Ammonium:preQ0-tRNA aminotransferase {ECO:0000305|PubMed:28383498};
DE AltName: Full=QueF-like amidinotransferase {ECO:0000303|PubMed:28383498};
DE Short=QueF-L {ECO:0000303|PubMed:28383498};
GN Name=queF-L {ECO:0000303|PubMed:28383498};
GN OrderedLocusNames=Pcal_0221 {ECO:0000312|EMBL:ABO07658.1};
OS Pyrobaculum calidifontis (strain DSM 21063 / JCM 11548 / VA1).
OC Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Pyrobaculum.
OX NCBI_TaxID=410359;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21063 / JCM 11548 / VA1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Cozen A.E.,
RA Fitz-Gibbon S.T., House C.H., Saltikov C., Lowe T.M., Richardson P.;
RT "Complete sequence of Pyrobaculum calidifontis JCM 11548.";
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, AND PATHWAY.
RX PubMed=22032275; DOI=10.1021/cb200361w;
RA Phillips G., Swairjo M.A., Gaston K.W., Bailly M., Limbach P.A.,
RA Iwata-Reuyl D., de Crecy-Lagard V.;
RT "Diversity of archaeosine synthesis in Crenarchaeota.";
RL ACS Chem. Biol. 7:300-305(2012).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, REACTION MECHANISM,
RP AND ACTIVE SITE.
RX PubMed=28383498; DOI=10.3390/biom7020036;
RA Bon Ramos A., Bao L., Turner B., de Crecy-Lagard V., Iwata-Reuyl D.;
RT "QueF-like, a non-homologous archaeosine synthase from the Crenarchaeota.";
RL Biomolecules 7:0-0(2017).
RN [4] {ECO:0007744|PDB:5JYX, ECO:0007744|PDB:5K0P}
RP X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS) OF APOENZYME AND IN COMPLEX WITH
RP PREQ0 VIA A COVALENT THIOIMIDE LINKAGE, REACTION MECHANISM, ACTIVE SITE,
RP AND SUBUNIT.
RX PubMed=27802572; DOI=10.1002/prot.25202;
RA Mei X., Alvarez J., Bon Ramos A., Samanta U., Iwata-Reuyl D., Swairjo M.A.;
RT "Crystal structure of the archaeosine synthase QueF-like-Insights into
RT amidino transfer and tRNA recognition by the tunnel fold.";
RL Proteins 85:103-116(2017).
CC -!- FUNCTION: Is responsible for the final step in the biosynthesis of
CC archaeosine, a modified nucleoside present in the dihydrouridine loop
CC (D-loop) of archaeal tRNA (PubMed:28383498, PubMed:22032275). Catalyzes
CC the conversion of 7-cyano-7-deazaguanine (preQ0)-modified tRNA to
CC archaeosine-tRNA, transforming a nitrile group to a formamidine group.
CC Can use neither glutamine nor asparagine as amino donor in vitro, is
CC only able to utilize free ammonium (PubMed:28383498). However, the
CC enzyme might function in vivo with a partner that serves to generate
CC ammonium. {ECO:0000269|PubMed:22032275, ECO:0000269|PubMed:28383498}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=7-cyano-7-carbaguanosine(15) in tRNA + NH4(+) =
CC archaeosine(15) in tRNA; Xref=Rhea:RHEA:55400, Rhea:RHEA-COMP:10371,
CC Rhea:RHEA-COMP:14170, ChEBI:CHEBI:28938, ChEBI:CHEBI:82850,
CC ChEBI:CHEBI:138803; Evidence={ECO:0000269|PubMed:28383498};
CC -!- PATHWAY: tRNA modification; archaeosine-tRNA biosynthesis.
CC {ECO:0000269|PubMed:22032275}.
CC -!- SUBUNIT: Forms a symmetric tunnel-fold (T-fold) homodecamer of two
CC head-to-head facing pentameric subunits, with 10 active sites at the
CC intermonomer interfaces. {ECO:0000269|PubMed:27802572}.
CC -!- SIMILARITY: Belongs to the archaeosine synthase type 2 family.
CC {ECO:0000305}.
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DR EMBL; CP000561; ABO07658.1; -; Genomic_DNA.
DR PDB; 5JYX; X-ray; 2.74 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O=1-109.
DR PDB; 5K0P; X-ray; 1.94 A; A/B/C/D/E/F/G/H/I/J=1-109.
DR PDBsum; 5JYX; -.
DR PDBsum; 5K0P; -.
DR AlphaFoldDB; A3MSP1; -.
DR SMR; A3MSP1; -.
DR STRING; 410359.Pcal_0221; -.
DR EnsemblBacteria; ABO07658; ABO07658; Pcal_0221.
DR KEGG; pcl:Pcal_0221; -.
DR eggNOG; arCOG04210; Archaea.
DR HOGENOM; CLU_173771_0_0_2; -.
DR OMA; ESVCPIS; -.
DR BioCyc; MetaCyc:MON-20299; -.
DR BRENDA; 2.6.1.B18; 7282.
DR UniPathway; UPA00393; -.
DR Proteomes; UP000001431; Chromosome.
DR GO; GO:0033739; F:preQ1 synthase activity; IEA:InterPro.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008616; P:queuosine biosynthetic process; IEA:InterPro.
DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR Gene3D; 3.30.1130.10; -; 1.
DR InterPro; IPR043133; GTP-CH-I_C/QueF.
DR InterPro; IPR029500; QueF.
DR Pfam; PF14489; QueF; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Transferase; tRNA processing.
FT CHAIN 1..109
FT /note="Archaeosine synthase"
FT /id="PRO_0000442193"
FT ACT_SITE 21
FT /note="Thioimide intermediate"
FT /evidence="ECO:0000269|PubMed:27802572,
FT ECO:0000269|PubMed:28383498"
FT ACT_SITE 28
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000305|PubMed:27802572"
FT BINDING 28
FT /ligand="substrate"
FT /ligand_note="ligand shared between two adjacent subunits"
FT /note="in other chain"
FT /evidence="ECO:0000269|PubMed:27802572"
FT BINDING 43..46
FT /ligand="substrate"
FT /ligand_note="ligand shared between two adjacent subunits"
FT /evidence="ECO:0000269|PubMed:27802572"
FT BINDING 62..63
FT /ligand="substrate"
FT /ligand_note="ligand shared between two adjacent subunits"
FT /note="in other chain"
FT /evidence="ECO:0000269|PubMed:27802572"
FT STRAND 9..20
FT /evidence="ECO:0007829|PDB:5K0P"
FT TURN 22..24
FT /evidence="ECO:0007829|PDB:5K0P"
FT STRAND 26..37
FT /evidence="ECO:0007829|PDB:5K0P"
FT STRAND 39..42
FT /evidence="ECO:0007829|PDB:5JYX"
FT HELIX 45..53
FT /evidence="ECO:0007829|PDB:5K0P"
FT TURN 54..57
FT /evidence="ECO:0007829|PDB:5K0P"
FT HELIX 62..77
FT /evidence="ECO:0007829|PDB:5K0P"
FT STRAND 80..90
FT /evidence="ECO:0007829|PDB:5K0P"
FT STRAND 93..102
FT /evidence="ECO:0007829|PDB:5K0P"
SQ SEQUENCE 109 AA; 12055 MW; 7918C03F02536C60 CRC64;
MLKVSKSPSL VRLKTRGESV CPISKTVDSF EVSVEYIPRG AVLAIEEFKK MVDSYRGREI
LHEELAVDLL EKVKAAVNPP YVKVTVKSYY IGVEVEVVAE SGGVPPVYI
