ARCS_METJA
ID ARCS_METJA Reviewed; 569 AA.
AC Q58428;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Archaeosine synthase {ECO:0000303|PubMed:20129918};
DE EC=2.6.1.97 {ECO:0000269|PubMed:20129918};
DE AltName: Full=Glutamine:preQ0-tRNA amidinotransferase {ECO:0000303|PubMed:20129918};
GN Name=arcS {ECO:0000303|PubMed:20129918}; OrderedLocusNames=MJ1022;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT,
RP SUBSTRATE SPECIFICITY, AND PATHWAY.
RX PubMed=20129918; DOI=10.1074/jbc.m110.102236;
RA Phillips G., Chikwana V.M., Maxwell A., El-Yacoubi B., Swairjo M.A.,
RA Iwata-Reuyl D., de Crecy-Lagard V.;
RT "Discovery and characterization of an amidinotransferase involved in the
RT modification of archaeal tRNA.";
RL J. Biol. Chem. 285:12706-12713(2010).
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. Catalyzes the conversion of 7-cyano-7-
CC deazaguanine (preQ0)-modified tRNA to archaeosine-tRNA, transforming a
CC nitrile group to a formamidine group. Can use either glutamine,
CC asparagine or ammonium as amino donor. {ECO:0000269|PubMed:20129918}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=7-cyano-7-carbaguanosine(15) in tRNA + H2O + L-glutamine =
CC archaeosine(15) in tRNA + L-glutamate; Xref=Rhea:RHEA:54084,
CC Rhea:RHEA-COMP:10371, Rhea:RHEA-COMP:14170, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:82850,
CC ChEBI:CHEBI:138803; EC=2.6.1.97;
CC Evidence={ECO:0000269|PubMed:20129918};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Optimum temperature is around 40 degrees Celsius. Activity decreases
CC significantly at temperatures above 45 degrees Celsius.
CC {ECO:0000269|PubMed:20129918};
CC -!- PATHWAY: tRNA modification; archaeosine-tRNA biosynthesis.
CC {ECO:0000305|PubMed:20129918}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:20129918}.
CC -!- SIMILARITY: Belongs to the archaeosine synthase type 1 family.
CC {ECO:0000305}.
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DR EMBL; L77117; AAB99026.1; -; Genomic_DNA.
DR PIR; E64427; E64427.
DR AlphaFoldDB; Q58428; -.
DR SMR; Q58428; -.
DR STRING; 243232.MJ_1022; -.
DR PRIDE; Q58428; -.
DR EnsemblBacteria; AAB99026; AAB99026; MJ_1022.
DR KEGG; mja:MJ_1022; -.
DR eggNOG; arCOG00990; Archaea.
DR HOGENOM; CLU_029831_0_0_2; -.
DR InParanoid; Q58428; -.
DR OMA; YPAAHYD; -.
DR PhylomeDB; Q58428; -.
DR BioCyc; MetaCyc:MON-16209; -.
DR BRENDA; 2.6.1.97; 3260.
DR UniPathway; UPA00393; -.
DR Proteomes; UP000000805; Chromosome.
DR GO; GO:0002948; F:archaeosine synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0016763; F:pentosyltransferase activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0002927; P:archaeosine-tRNA biosynthetic process; IDA:UniProtKB.
DR GO; GO:0006400; P:tRNA modification; IDA:UniProtKB.
DR Gene3D; 2.30.130.10; -; 1.
DR InterPro; IPR040777; DUF5591.
DR InterPro; IPR002478; PUA.
DR InterPro; IPR015947; PUA-like_sf.
DR InterPro; IPR036974; PUA_sf.
DR InterPro; IPR036511; TGT-like_sf.
DR InterPro; IPR004521; Uncharacterised_CHP00451.
DR InterPro; IPR036895; Uracil-DNA_glycosylase-like_sf.
DR Pfam; PF17884; DUF5591; 1.
DR Pfam; PF01472; PUA; 1.
DR SMART; SM00359; PUA; 1.
DR SUPFAM; SSF51713; SSF51713; 1.
DR SUPFAM; SSF52141; SSF52141; 1.
DR SUPFAM; SSF88697; SSF88697; 1.
DR TIGRFAMs; TIGR00451; unchar_dom_2; 1.
DR PROSITE; PS50890; PUA; 1.
PE 1: Evidence at protein level;
KW Reference proteome; Transferase; tRNA processing.
FT CHAIN 1..569
FT /note="Archaeosine synthase"
FT /id="PRO_0000107146"
FT DOMAIN 495..569
FT /note="PUA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00161"
SQ SEQUENCE 569 AA; 65582 MW; E29EC27908E366ED CRC64;
MLEPIAYDIG RLCKEEDKEL TPKLIDIDVI GLSQEKIFYG IMTPFRCPNS KSIYELRKSY
VKADGIKMPF DTFRELTSIF KKSFIGTVKY KGNVFKYQIL NFGKHVDLIE LEDADLYIIA
DGRRLIERKE LQIIPKIREK ISPNSAIYSP AVFPWEIPLL AYIGVDYFDD SLAKLYASMG
YKFTKNRAVK VDSFSFEELY NNNKKVYEEI LEEVRIAIKN GFLRNVVEET AVSHPYLWAN
YRRYEPDLRN IPLSKENKII VTTNINIPEV KKYLERLDNY EPYSNIIVLL PCSSKKPYSI
SQSHQKFIKA IKSAKVVVEE VILTSPYGLV PRALERLVNY DIPVTGEWSF EEIELINNCL
KNFLKKVKEK FDDYIVIAHL PEHYLEILEL DDIVITSKGN PTSEEALKNL TDTLKKYKEL
TKSKDINKKG QRIHNIQQLA EFQFGINFIP NEIFINHKGQ IFTKINNKNQ QIASINPKNG
LLILTLSGGE LLWNSGGKDI NYIEVNYEIK KGSLFPPGFV DCNENISYND EVVLIKDDTF
LGIGRALMSG FEMKKAKHGA LVNIRNVKS
