ARCSA_METAC
ID ARCSA_METAC Reviewed; 625 AA.
AC Q8TH90;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Archaeosine synthase subunit alpha {ECO:0000303|PubMed:31740832};
DE EC=4.3.3.- {ECO:0000269|PubMed:31740832};
DE AltName: Full=Archaeosine synthase, lysine transferase subunit {ECO:0000303|PubMed:31740832};
GN Name=arcS {ECO:0000303|PubMed:31740832};
GN Synonyms=tgt {ECO:0000312|EMBL:AAM07966.1};
GN OrderedLocusNames=MA_4632 {ECO:0000312|EMBL:AAM07966.1};
OS Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 /
OS C2A).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=188937;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A;
RX PubMed=11932238; DOI=10.1101/gr.223902;
RA Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W.,
RA Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J.,
RA Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P.,
RA McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D.,
RA Cann I., Graham D.E., Grahame D.A., Guss A.M., Hedderich R.,
RA Ingram-Smith C., Kuettner H.C., Krzycki J.A., Leigh J.A., Li W., Liu J.,
RA Mukhopadhyay B., Reeve J.N., Smith K., Springer T.A., Umayam L.A.,
RA White O., White R.H., de Macario E.C., Ferry J.G., Jarrell K.F., Jing H.,
RA Macario A.J.L., Paulsen I.T., Pritchett M., Sowers K.R., Swanson R.V.,
RA Zinder S.H., Lander E., Metcalf W.W., Birren B.;
RT "The genome of Methanosarcina acetivorans reveals extensive metabolic and
RT physiological diversity.";
RL Genome Res. 12:532-542(2002).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND INTERACTION WITH RASEA.
RX PubMed=31740832; DOI=10.1038/s41589-019-0390-7;
RA Yokogawa T., Nomura Y., Yasuda A., Ogino H., Hiura K., Nakada S., Oka N.,
RA Ando K., Kawamura T., Hirata A., Hori H., Ohno S.;
RT "Identification of a radical SAM enzyme involved in the synthesis of
RT archaeosine.";
RL Nat. Chem. Biol. 15:1148-1155(2019).
CC -!- FUNCTION: Functions in the biosynthesis of archaeosine, a modified
CC nucleoside present in the dihydrouridine loop (D-loop) of archaeal
CC tRNAs. Catalyzes the addition of L-lysine to the cyano group of 7-
CC cyano-7-deazaguanine (preQ0)-modified tRNAs at position 15, to generate
CC q0kN15-tRNA, a q0N lysine adduct identified as 7-N-[(5S)-5-amino-5-
CC carboxypentyl]formamidino-7-deazaguanosine.
CC {ECO:0000269|PubMed:31740832}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=7-cyano-7-carbaguanosine(15) in tRNA + L-lysine = 7-N-[(5S)-5-
CC amino-5-carboxypentyl]formamidino-7-deazaguanosine(15) in tRNA;
CC Xref=Rhea:RHEA:63216, Rhea:RHEA-COMP:10371, Rhea:RHEA-COMP:16288,
CC ChEBI:CHEBI:32551, ChEBI:CHEBI:82850, ChEBI:CHEBI:145542;
CC Evidence={ECO:0000269|PubMed:31740832};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63217;
CC Evidence={ECO:0000269|PubMed:31740832};
CC -!- PATHWAY: tRNA modification; archaeosine-tRNA biosynthesis.
CC {ECO:0000269|PubMed:31740832}.
CC -!- SUBUNIT: Forms a robust complex with the archaeosine synthase beta
CC subunit RaSEA. Formation of this complex highly increases lysine
CC transfer activity (PubMed:31740832). The complex likely consists of an
CC alpha(2)beta(2) heterotetrameric structure (By similarity).
CC {ECO:0000250|UniProtKB:Q5JHG7, ECO:0000269|PubMed:31740832}.
CC -!- SIMILARITY: Belongs to the archaeosine synthase type 1 family.
CC {ECO:0000305}.
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DR EMBL; AE010299; AAM07966.1; -; Genomic_DNA.
DR RefSeq; WP_011024500.1; NC_003552.1.
DR AlphaFoldDB; Q8TH90; -.
DR SMR; Q8TH90; -.
DR STRING; 188937.MA_4632; -.
DR EnsemblBacteria; AAM07966; AAM07966; MA_4632.
DR GeneID; 1476526; -.
DR KEGG; mac:MA_4632; -.
DR HOGENOM; CLU_029831_0_0_2; -.
DR InParanoid; Q8TH90; -.
DR OMA; YPAAHYD; -.
DR OrthoDB; 21064at2157; -.
DR PhylomeDB; Q8TH90; -.
DR BRENDA; 2.6.1.97; 7224.
DR UniPathway; UPA00393; -.
DR Proteomes; UP000002487; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0016763; F:pentosyltransferase activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0008616; P:queuosine biosynthetic process; IBA:GO_Central.
DR GO; GO:0002099; P:tRNA wobble guanine modification; IBA:GO_Central.
DR Gene3D; 2.30.130.10; -; 1.
DR Gene3D; 3.10.450.90; -; 1.
DR Gene3D; 3.20.20.105; -; 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; IPR029402; TGT_C2.
DR InterPro; IPR038250; TGT_C2_sf.
DR InterPro; IPR002616; tRNA_ribo_trans-like.
DR InterPro; IPR004521; Uncharacterised_CHP00451.
DR InterPro; IPR036895; Uracil-DNA_glycosylase-like_sf.
DR Pfam; PF17884; DUF5591; 1.
DR Pfam; PF01472; PUA; 1.
DR Pfam; PF01702; TGT; 1.
DR Pfam; PF14810; TGT_C2; 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 Lyase; Reference proteome; tRNA processing.
FT CHAIN 1..625
FT /note="Archaeosine synthase subunit alpha"
FT /id="PRO_0000450069"
FT DOMAIN 556..624
FT /note="PUA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00161"
SQ SEQUENCE 625 AA; 69134 MW; AB8F334CE9D4F84D CRC64;
MTQYFEIENR DGAARIGKLL LFPEIRTPCA LHTAALGDLE NPGPIVDAGS LWIADQKELE
ARIKEIREKT GKGTLIILPH QTYPPAVPAE STGKVEAFTA TGDENAEAEG PTGSLLRAEG
EVRKSDLYIM EGAGTLENNA RRFLETLIDL KNRIPPDTAL YAPKLALPEN AAMLAYVGID
VMDDTRAEIA AYSDIYLTAA GSFYLDSLVE FPCRCRVCAA TTPAELRALP KADRVELLSA
HNRDALDAEL ALVREKIRTG NLREYVEGQC RVRPWLTALL RLGDFEYSYI EEKVPAFRQS
QLLADTSEAL SRIEVVRFAR RIQERYAPPD LDVLLLLPCA ARKPYSTSQS HQKFILALGK
YRKFVHEVII TSPLGIVPRE LELTYPAAHY DTAVTGHWDE EEKAWVSGCL ESYLSKHMYK
AVVAHVEGAY REICERVAEK LGIDVVYTAG ESLASYESLT NLKNTVEAIC TSKDFSRKSQ
NAEKEKKNFI KAVAGYQFGE GAGHLFSEEV GDPLVKGRFP KYQLFAGKKQ LATLIPQYGM
LALSPEGAEL VLKSEKYVVK IDDFVPRGSI LAPGVLDAGP EIRPNDEVIV LGKKALCVGR
AMMSGREMKE SGRGVAVDVR HVKKL
