QUEA_BACSU
ID QUEA_BACSU Reviewed; 342 AA.
AC O32054;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 128.
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=BSU27720;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RA Tosato V., Bolotin A., Bertani I., Valentino I., Bruschi C.V.;
RT "A 17.8 kb segment in the spoVB-nadC region of the Bacillus subtilis 168
RT chromosome: sequencing and ruv operon identification.";
RL Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
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; Y15896; CAB75332.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14732.1; -; Genomic_DNA.
DR PIR; A69688; A69688.
DR RefSeq; NP_390650.1; NC_000964.3.
DR RefSeq; WP_003229723.1; NZ_JNCM01000036.1.
DR PDB; 1YY3; X-ray; 2.88 A; A/B=2-342.
DR PDBsum; 1YY3; -.
DR AlphaFoldDB; O32054; -.
DR SMR; O32054; -.
DR STRING; 224308.BSU27720; -.
DR PaxDb; O32054; -.
DR PRIDE; O32054; -.
DR EnsemblBacteria; CAB14732; CAB14732; BSU_27720.
DR GeneID; 937975; -.
DR KEGG; bsu:BSU27720; -.
DR PATRIC; fig|224308.179.peg.3011; -.
DR eggNOG; COG0809; Bacteria.
DR InParanoid; O32054; -.
DR OMA; YSYGDGM; -.
DR PhylomeDB; O32054; -.
DR BioCyc; BSUB:BSU27720-MON; -.
DR BRENDA; 2.4.99.17; 658.
DR UniPathway; UPA00392; -.
DR EvolutionaryTrace; O32054; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0051075; F:S-adenosylmethionine:tRNA ribosyltransferase-isomerase activity; IBA:GO_Central.
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; 2.40.10.240; -; 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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Queuosine biosynthesis; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..342
FT /note="S-adenosylmethionine:tRNA ribosyltransferase-
FT isomerase"
FT /id="PRO_0000165380"
FT TURN 12..14
FT /evidence="ECO:0007829|PDB:1YY3"
FT STRAND 26..30
FT /evidence="ECO:0007829|PDB:1YY3"
FT TURN 33..35
FT /evidence="ECO:0007829|PDB:1YY3"
FT HELIX 45..49
FT /evidence="ECO:0007829|PDB:1YY3"
FT STRAND 54..58
FT /evidence="ECO:0007829|PDB:1YY3"
FT STRAND 66..76
FT /evidence="ECO:0007829|PDB:1YY3"
FT STRAND 79..86
FT /evidence="ECO:0007829|PDB:1YY3"
FT STRAND 91..96
FT /evidence="ECO:0007829|PDB:1YY3"
FT HELIX 99..101
FT /evidence="ECO:0007829|PDB:1YY3"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:1YY3"
FT STRAND 113..122
FT /evidence="ECO:0007829|PDB:1YY3"
FT STRAND 128..133
FT /evidence="ECO:0007829|PDB:1YY3"
FT HELIX 138..146
FT /evidence="ECO:0007829|PDB:1YY3"
FT HELIX 152..155
FT /evidence="ECO:0007829|PDB:1YY3"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:1YY3"
FT HELIX 186..195
FT /evidence="ECO:0007829|PDB:1YY3"
FT STRAND 197..201
FT /evidence="ECO:0007829|PDB:1YY3"
FT STRAND 203..206
FT /evidence="ECO:0007829|PDB:1YY3"
FT HELIX 207..211
FT /evidence="ECO:0007829|PDB:1YY3"
FT STRAND 227..231
FT /evidence="ECO:0007829|PDB:1YY3"
FT HELIX 233..244
FT /evidence="ECO:0007829|PDB:1YY3"
FT STRAND 249..252
FT /evidence="ECO:0007829|PDB:1YY3"
FT TURN 254..256
FT /evidence="ECO:0007829|PDB:1YY3"
FT HELIX 257..265
FT /evidence="ECO:0007829|PDB:1YY3"
FT TURN 266..268
FT /evidence="ECO:0007829|PDB:1YY3"
FT STRAND 274..278
FT /evidence="ECO:0007829|PDB:1YY3"
FT STRAND 292..297
FT /evidence="ECO:0007829|PDB:1YY3"
FT HELIX 305..313
FT /evidence="ECO:0007829|PDB:1YY3"
FT HELIX 315..327
FT /evidence="ECO:0007829|PDB:1YY3"
FT STRAND 332..336
FT /evidence="ECO:0007829|PDB:1YY3"
FT STRAND 338..340
FT /evidence="ECO:0007829|PDB:1YY3"
SQ SEQUENCE 342 AA; 38512 MW; D8A28DCC9AC05DAD CRC64;
MKVDLFDFEL PERLIAQVPL EQRDASRLMV LDKHTGELTD SSFKHIISFF NEGDCLVLNN
TRVLPARLFG TKEDTGAKVE LLLLKQETGD KWETLAKPAK RVKKGTVVTF GDGRLKAICT
EELEHGGRKM EFQYDGIFYE VLESLGEMPL PPYIKEQLDD KERYQTVYSK EIGSAAAPTA
GLHFTEEILQ QLKDKGVQIE FITLHVGLGT FRPVSADEVE EHNMHAEFYQ MSEETAAALN
KVRENGGRII SVGTTSTRTL ETIAGEHDGQ FKASSGWTSI FIYPGYEFKA IDGMITNFHL
PKSSLIMLVS ALAGRENILR AYNHAVEEEY RFFSFGDAML II
