ID   QUEA_PROMP              Reviewed;         374 AA.
AC   Q7V2R3;
DT   26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   25-MAY-2022, entry version 95.
DE   RecName: Full=S-adenosylmethionine:tRNA ribosyltransferase-isomerase;
DE            EC=2.4.99.17;
DE   AltName: Full=Queuosine biosynthesis protein QueA;
GN   Name=queA; OrderedLocusNames=PMM0406;
OS   Prochlorococcus marinus subsp. pastoris (strain CCMP1986 / NIES-2087 /
OS   MED4).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=59919;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCMP1986 / NIES-2087 / MED4;
RX   PubMed=12917642; DOI=10.1038/nature01947;
RA   Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P., Ahlgren N.A.,
RA   Arellano A., Coleman M., Hauser L., Hess W.R., Johnson Z.I., Land M.L.,
RA   Lindell D., Post A.F., Regala W., Shah M., Shaw S.L., Steglich C.,
RA   Sullivan M.B., Ting C.S., Tolonen A., Webb E.A., Zinser E.R.,
RA   Chisholm S.W.;
RT   "Genome divergence in two Prochlorococcus ecotypes reflects oceanic niche
RT   differentiation.";
RL   Nature 424:1042-1047(2003).
CC   -!- FUNCTION: Synthesizes oQ from preQ1 in a single S-adenosylmethionine-
CC       requiring step. The ribosyl moiety of AdoMet is transferred and
CC       isomerized to the epoxycyclopentane residue of oQ (By similarity).
CC       {ECO:0000250}.
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;
CC   -!- PATHWAY: tRNA modification; tRNA-queuosine biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the QueA family. {ECO:0000305}.
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DR   EMBL; BX548174; CAE18865.1; -; Genomic_DNA.
DR   RefSeq; WP_011132042.1; NC_005072.1.
DR   AlphaFoldDB; Q7V2R3; -.
DR   SMR; Q7V2R3; -.
DR   STRING; 59919.PMM0406; -.
DR   EnsemblBacteria; CAE18865; CAE18865; PMM0406.
DR   KEGG; pmm:PMM0406; -.
DR   eggNOG; COG0809; Bacteria.
DR   HOGENOM; CLU_039110_1_0_3; -.
DR   OMA; YSYGDGM; -.
DR   OrthoDB; 368001at2; -.
DR   UniPathway; UPA00392; -.
DR   Proteomes; UP000001026; 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; -; 1.
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; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..374
FT                   /note="S-adenosylmethionine:tRNA ribosyltransferase-
FT                   isomerase"
FT                   /id="PRO_0000165424"
SQ   SEQUENCE   374 AA;  42624 MW;  9A8EBEAB3893B6D6 CRC64;
     MNFEIHNEEI DHKLEAYDYI LDETLIANKP SKVRHESRLM IVRDSSLEED FTTNKYTKNL
     LDELRKGDLV VVNDTKVMKA RLKVELENGK LVELLVLEKA DQSTWLCLAR PAKKLKINSQ
     LNLKSSLAKD IKLHISGTDK ETGGRFIKFP ENINDLISMN NLLDIYGETP LPPYIKSAEE
     ESFHENSYQT EYASNPGAVA APTAGLHLSK SLISNLKKKG ILVMPITLHV GYGTFKPIDQ
     EDLSNLKLHK EWVRVSSEVV EEIKRVKKTD RRVIAIGTTS VRALESCYSY EMGDLIPIDK
     YVDLVIKPGY KFKVVDGLLT NFHLPKSSLL LLVSAMIGRE RLLNLYKKAI REKFRFFSYG
     DAMYISPDSF LVKK