ID   QUEA_PROM4              Reviewed;         375 AA.
AC   A9BE25;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   25-MAY-2022, entry version 76.
DE   RecName: Full=S-adenosylmethionine:tRNA ribosyltransferase-isomerase {ECO:0000255|HAMAP-Rule:MF_00113};
DE            EC=2.4.99.17 {ECO:0000255|HAMAP-Rule:MF_00113};
DE   AltName: Full=Queuosine biosynthesis protein QueA {ECO:0000255|HAMAP-Rule:MF_00113};
GN   Name=queA {ECO:0000255|HAMAP-Rule:MF_00113}; OrderedLocusNames=P9211_04041;
OS   Prochlorococcus marinus (strain MIT 9211).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=93059;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 9211;
RX   PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA   Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA   Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA   Richardson P., Chisholm S.W.;
RT   "Patterns and implications of gene gain and loss in the evolution of
RT   Prochlorococcus.";
RL   PLoS Genet. 3:2515-2528(2007).
CC   -!- FUNCTION: Transfers and isomerizes the ribose moiety from AdoMet to the
CC       7-aminomethyl group of 7-deazaguanine (preQ1-tRNA) to give
CC       epoxyqueuosine (oQ-tRNA). {ECO:0000255|HAMAP-Rule:MF_00113}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=7-aminomethyl-7-carbaguanosine(34) in tRNA + S-adenosyl-L-
CC         methionine = adenine + epoxyqueuosine(34) in tRNA + H(+) + L-
CC         methionine; Xref=Rhea:RHEA:32155, Rhea:RHEA-COMP:10342, Rhea:RHEA-
CC         COMP:10346, ChEBI:CHEBI:15378, ChEBI:CHEBI:16708, ChEBI:CHEBI:57844,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:82833, ChEBI:CHEBI:82834;
CC         EC=2.4.99.17; Evidence={ECO:0000255|HAMAP-Rule:MF_00113};
CC   -!- PATHWAY: tRNA modification; tRNA-queuosine biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00113}.
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00113}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00113}.
CC   -!- SIMILARITY: Belongs to the QueA family. {ECO:0000255|HAMAP-
CC       Rule:MF_00113}.
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DR   EMBL; CP000878; ABX08335.1; -; Genomic_DNA.
DR   RefSeq; WP_012194958.1; NC_009976.1.
DR   AlphaFoldDB; A9BE25; -.
DR   SMR; A9BE25; -.
DR   STRING; 93059.P9211_04041; -.
DR   EnsemblBacteria; ABX08335; ABX08335; P9211_04041.
DR   KEGG; pmj:P9211_04041; -.
DR   eggNOG; COG0809; Bacteria.
DR   HOGENOM; CLU_039110_1_0_3; -.
DR   OMA; YSYGDGM; -.
DR   UniPathway; UPA00392; -.
DR   Proteomes; UP000000788; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0051075; F:S-adenosylmethionine:tRNA ribosyltransferase-isomerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008616; P:queuosine biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 2.40.10.240; -; 1.
DR   Gene3D; 3.40.1780.10; -; 2.
DR   HAMAP; MF_00113; QueA; 1.
DR   InterPro; IPR003699; QueA.
DR   InterPro; IPR042118; QueA_dom1.
DR   InterPro; IPR042119; QueA_dom2.
DR   InterPro; IPR036100; QueA_sf.
DR   PANTHER; PTHR30307; PTHR30307; 1.
DR   Pfam; PF02547; Queuosine_synth; 1.
DR   SUPFAM; SSF111337; SSF111337; 1.
DR   TIGRFAMs; TIGR00113; queA; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Queuosine biosynthesis; Reference proteome;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..375
FT                   /note="S-adenosylmethionine:tRNA ribosyltransferase-
FT                   isomerase"
FT                   /id="PRO_1000094799"
SQ   SEQUENCE   375 AA;  41754 MW;  D42152BF0F14CED3 CRC64;
     MLVNSQDLSL SSYDYELDSK LIAQKPLNPR HDARLMVVSK DNGPNLCVSH LKVWNLLDEL
     RAGDLLVINN TRVLKARLRV RLKSGAMAEL LLLEPHGDGR WLCLAKPAKK FLPGDYVWME
     ALEQESLKLQ VLTKDLETGG RIVQFPQEFS NRKSIENLLE RYGEVPLPPY IRQHDPSDAD
     RYQTRFASTP GSVAAPTAGL HLSDEILNAL IQRGIEKASV TLHVGLGTFR PIEEEDLTNL
     KLHSEWVEVG EEVVSAVQAC RSRGGRIFAV GTTTVRSLEA SFLLGGGSMK AFQGLVDLVI
     KPGYQFGVVN GLLTNFHLPK SSLLLLVSAL IGRERLLELY QEAIERKYRF FSYGDAMFIT
     PEAVLPGAKS PRVLQ