QUEG_BACSU
ID QUEG_BACSU Reviewed; 386 AA.
AC P97030; Q796Y4;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-APR-2009, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Epoxyqueuosine reductase {ECO:0000255|HAMAP-Rule:MF_00916, ECO:0000303|PubMed:21502530};
DE EC=1.17.99.6 {ECO:0000255|HAMAP-Rule:MF_00916, ECO:0000269|PubMed:21502530};
DE AltName: Full=Queuosine biosynthesis protein QueG {ECO:0000255|HAMAP-Rule:MF_00916};
GN Name=queG {ECO:0000255|HAMAP-Rule:MF_00916, ECO:0000303|PubMed:21502530};
GN Synonyms=ygaP, yhbA; OrderedLocusNames=BSU08910;
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 Cummings N.J., Ruiz-Teran F., Connerton I.F.;
RL Submitted (MAR-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).
RN [3]
RP FUNCTION AS A REDUCTASE, CATALYTIC ACTIVITY, ACTIVITY REGULATION, PATHWAY,
RP SUBCELLULAR LOCATION, AND GENE NAME.
RX PubMed=21502530; DOI=10.1073/pnas.1018636108;
RA Miles Z.D., McCarty R.M., Molnar G., Bandarian V.;
RT "Discovery of epoxyqueuosine (oQ) reductase reveals parallels between
RT halorespiration and tRNA modification.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:7368-7372(2011).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND SUBUNIT.
RX PubMed=26230193; DOI=10.1021/acs.biochem.5b00335;
RA Miles Z.D., Myers W.K., Kincannon W.M., Britt R.D., Bandarian V.;
RT "Biochemical and Spectroscopic Studies of Epoxyqueuosine Reductase: A Novel
RT Iron-Sulfur Cluster- and Cobalamin-Containing Protein Involved in the
RT Biosynthesis of Queuosine.";
RL Biochemistry 54:4927-4935(2015).
RN [5] {ECO:0007744|PDB:5D08, ECO:0007744|PDB:5D0A, ECO:0007744|PDB:5D0B, ECO:0007744|PDB:5T8Y}
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 2-386 IN COMPLEXES WITH
RP IRON-SULFUR (4FE-4S) CLUSTERS; COBALAMIN AND TRNA, COFACTOR, REACTION
RP MECHANISM, AND ACTIVE SITE.
RX PubMed=27638883; DOI=10.1093/nar/gkw806;
RA Dowling D.P., Miles Z.D., Kohrer C., Maiocco S.J., Elliott S.J.,
RA Bandarian V., Drennan C.L.;
RT "Molecular basis of cobalamin-dependent RNA modification.";
RL Nucleic Acids Res. 44:9965-9976(2016).
CC -!- FUNCTION: Catalyzes the conversion of epoxyqueuosine (oQ) to queuosine
CC (Q), which is a hypermodified base found in the wobble positions of
CC tRNA(Asp), tRNA(Asn), tRNA(His) and tRNA(Tyr). {ECO:0000255|HAMAP-
CC Rule:MF_00916, ECO:0000269|PubMed:21502530,
CC ECO:0000269|PubMed:26230193}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=AH2 + epoxyqueuosine(34) in tRNA = A + H2O + queuosine(34) in
CC tRNA; Xref=Rhea:RHEA:32159, Rhea:RHEA-COMP:10345, Rhea:RHEA-
CC COMP:10346, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:17499,
CC ChEBI:CHEBI:82831, ChEBI:CHEBI:82834; EC=1.17.99.6;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00916,
CC ECO:0000269|PubMed:21502530, ECO:0000269|PubMed:26230193};
CC -!- COFACTOR:
CC Name=cob(II)alamin; Xref=ChEBI:CHEBI:16304;
CC Evidence={ECO:0000269|PubMed:26230193, ECO:0000269|PubMed:27638883};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000269|PubMed:26230193, ECO:0000269|PubMed:27638883};
CC Note=Binds 2 [4Fe-4S] clusters per monomer.
CC {ECO:0000269|PubMed:26230193, ECO:0000269|PubMed:27638883};
CC -!- PATHWAY: tRNA modification; tRNA-queuosine biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00916, ECO:0000269|PubMed:21502530}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:26230193}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:21502530}.
CC -!- SIMILARITY: Belongs to the QueG family. {ECO:0000255|HAMAP-
CC Rule:MF_00916}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB07527.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; Z93102; CAB07527.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL009126; CAB12719.2; -; Genomic_DNA.
DR PIR; E69820; E69820.
DR RefSeq; NP_388772.2; NC_000964.3.
DR RefSeq; WP_003245522.1; NZ_JNCM01000035.1.
DR PDB; 5D08; X-ray; 1.75 A; A/B=2-386.
DR PDB; 5D0A; X-ray; 2.10 A; A/B/C/D=1-386.
DR PDB; 5D0B; X-ray; 2.65 A; A/B=1-386.
DR PDB; 5T8Y; X-ray; 2.65 A; A/B=1-386.
DR PDBsum; 5D08; -.
DR PDBsum; 5D0A; -.
DR PDBsum; 5D0B; -.
DR PDBsum; 5T8Y; -.
DR AlphaFoldDB; P97030; -.
DR SMR; P97030; -.
DR STRING; 224308.BSU08910; -.
DR PaxDb; P97030; -.
DR PRIDE; P97030; -.
DR DNASU; 939243; -.
DR EnsemblBacteria; CAB12719; CAB12719; BSU_08910.
DR GeneID; 939243; -.
DR KEGG; bsu:BSU08910; -.
DR PATRIC; fig|224308.179.peg.962; -.
DR eggNOG; COG1600; Bacteria.
DR InParanoid; P97030; -.
DR OMA; ICDTDLS; -.
DR PhylomeDB; P97030; -.
DR BioCyc; BSUB:BSU08910-MON; -.
DR BRENDA; 1.17.99.6; 658.
DR UniPathway; UPA00392; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0052693; F:epoxyqueuosine reductase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008616; P:queuosine biosynthetic process; IBA:GO_Central.
DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-UniRule.
DR Gene3D; 1.25.10.10; -; 1.
DR HAMAP; MF_00916; QueG; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR004155; PBS_lyase_HEAT.
DR InterPro; IPR004453; QueG.
DR InterPro; IPR013542; QueG_DUF1730.
DR PANTHER; PTHR30002; PTHR30002; 1.
DR Pfam; PF08331; DUF1730; 1.
DR SMART; SM00567; EZ_HEAT; 2.
DR SUPFAM; SSF48371; SSF48371; 1.
DR TIGRFAMs; TIGR00276; TIGR00276; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; 4Fe-4S; Cytoplasm; Iron; Iron-sulfur; Metal-binding;
KW Oxidoreductase; Queuosine biosynthesis; Reference proteome;
KW tRNA processing.
FT CHAIN 1..386
FT /note="Epoxyqueuosine reductase"
FT /id="PRO_0000360648"
FT DOMAIN 178..208
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00916"
FT REPEAT 333..357
FT /note="HEAT-like PBS-type"
FT ACT_SITE 134
FT /note="Proton donor"
FT /evidence="ECO:0000305|PubMed:27638883"
FT BINDING 57
FT /ligand="cob(II)alamin"
FT /ligand_id="ChEBI:CHEBI:16304"
FT /evidence="ECO:0000269|PubMed:27638883,
FT ECO:0007744|PDB:5D0B"
FT BINDING 97
FT /ligand="cob(II)alamin"
FT /ligand_id="ChEBI:CHEBI:16304"
FT /evidence="ECO:0000269|PubMed:27638883,
FT ECO:0007744|PDB:5D0B"
FT BINDING 134
FT /ligand="cob(II)alamin"
FT /ligand_id="ChEBI:CHEBI:16304"
FT /evidence="ECO:0000269|PubMed:27638883,
FT ECO:0007744|PDB:5D0B"
FT BINDING 139..141
FT /ligand="cob(II)alamin"
FT /ligand_id="ChEBI:CHEBI:16304"
FT /evidence="ECO:0000269|PubMed:27638883,
FT ECO:0007744|PDB:5D0B"
FT BINDING 152
FT /ligand="cob(II)alamin"
FT /ligand_id="ChEBI:CHEBI:16304"
FT /evidence="ECO:0000269|PubMed:27638883,
FT ECO:0007744|PDB:5D0B"
FT BINDING 155
FT /ligand="cob(II)alamin"
FT /ligand_id="ChEBI:CHEBI:16304"
FT /evidence="ECO:0000269|PubMed:27638883,
FT ECO:0007744|PDB:5D0B"
FT BINDING 158
FT /ligand="cob(II)alamin"
FT /ligand_id="ChEBI:CHEBI:16304"
FT /evidence="ECO:0000269|PubMed:27638883,
FT ECO:0007744|PDB:5D0B"
FT BINDING 169
FT /ligand="cob(II)alamin"
FT /ligand_id="ChEBI:CHEBI:16304"
FT /evidence="ECO:0000269|PubMed:27638883,
FT ECO:0007744|PDB:5D0B"
FT BINDING 188
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:27638883,
FT ECO:0007744|PDB:5D0B"
FT BINDING 191
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:27638883,
FT ECO:0007744|PDB:5D0B"
FT BINDING 194
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:27638883,
FT ECO:0007744|PDB:5D0B"
FT BINDING 198
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:27638883,
FT ECO:0007744|PDB:5D0B"
FT BINDING 214
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:27638883,
FT ECO:0007744|PDB:5D0B"
FT BINDING 216
FT /ligand="cob(II)alamin"
FT /ligand_id="ChEBI:CHEBI:16304"
FT /evidence="ECO:0000269|PubMed:27638883,
FT ECO:0007744|PDB:5D0B"
FT BINDING 220
FT /ligand="tRNA"
FT /ligand_id="ChEBI:CHEBI:17843"
FT /ligand_part="tRNA anticodon stem loop"
FT /evidence="ECO:0000269|PubMed:27638883"
FT BINDING 222
FT /ligand="tRNA"
FT /ligand_id="ChEBI:CHEBI:17843"
FT /ligand_part="tRNA anticodon stem loop"
FT /evidence="ECO:0000269|PubMed:27638883"
FT BINDING 240..241
FT /ligand="cob(II)alamin"
FT /ligand_id="ChEBI:CHEBI:16304"
FT /evidence="ECO:0000269|PubMed:27638883,
FT ECO:0007744|PDB:5D0B"
FT BINDING 240
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:27638883,
FT ECO:0007744|PDB:5D0B"
FT BINDING 243
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:27638883,
FT ECO:0007744|PDB:5D0B"
FT BINDING 247
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:27638883,
FT ECO:0007744|PDB:5D0B"
FT BINDING 280
FT /ligand="tRNA"
FT /ligand_id="ChEBI:CHEBI:17843"
FT /ligand_part="tRNA anticodon stem loop"
FT /evidence="ECO:0000269|PubMed:27638883"
FT BINDING 281
FT /ligand="tRNA"
FT /ligand_id="ChEBI:CHEBI:17843"
FT /ligand_part="tRNA anticodon stem loop"
FT /evidence="ECO:0000269|PubMed:27638883"
FT BINDING 295
FT /ligand="tRNA"
FT /ligand_id="ChEBI:CHEBI:17843"
FT /ligand_part="tRNA anticodon stem loop"
FT /evidence="ECO:0000269|PubMed:27638883"
FT BINDING 297
FT /ligand="tRNA"
FT /ligand_id="ChEBI:CHEBI:17843"
FT /ligand_part="tRNA anticodon stem loop"
FT /evidence="ECO:0000269|PubMed:27638883"
FT BINDING 298
FT /ligand="tRNA"
FT /ligand_id="ChEBI:CHEBI:17843"
FT /ligand_part="tRNA anticodon stem loop"
FT /evidence="ECO:0000269|PubMed:27638883"
FT HELIX 3..16
FT /evidence="ECO:0007829|PDB:5D08"
FT STRAND 20..26
FT /evidence="ECO:0007829|PDB:5D08"
FT HELIX 31..43
FT /evidence="ECO:0007829|PDB:5D08"
FT HELIX 54..58
FT /evidence="ECO:0007829|PDB:5D08"
FT HELIX 60..63
FT /evidence="ECO:0007829|PDB:5D08"
FT STRAND 69..76
FT /evidence="ECO:0007829|PDB:5D08"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:5D08"
FT HELIX 98..100
FT /evidence="ECO:0007829|PDB:5D08"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:5D08"
FT HELIX 105..121
FT /evidence="ECO:0007829|PDB:5D08"
FT STRAND 129..138
FT /evidence="ECO:0007829|PDB:5D08"
FT HELIX 140..146
FT /evidence="ECO:0007829|PDB:5D08"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:5D08"
FT TURN 161..163
FT /evidence="ECO:0007829|PDB:5D08"
FT STRAND 167..175
FT /evidence="ECO:0007829|PDB:5D08"
FT HELIX 193..197
FT /evidence="ECO:0007829|PDB:5D08"
FT STRAND 203..205
FT /evidence="ECO:0007829|PDB:5D08"
FT HELIX 211..213
FT /evidence="ECO:0007829|PDB:5D08"
FT HELIX 215..219
FT /evidence="ECO:0007829|PDB:5D08"
FT HELIX 227..230
FT /evidence="ECO:0007829|PDB:5D08"
FT STRAND 236..238
FT /evidence="ECO:0007829|PDB:5D08"
FT HELIX 242..245
FT /evidence="ECO:0007829|PDB:5D08"
FT HELIX 248..250
FT /evidence="ECO:0007829|PDB:5D08"
FT HELIX 259..261
FT /evidence="ECO:0007829|PDB:5D08"
FT HELIX 265..268
FT /evidence="ECO:0007829|PDB:5D08"
FT HELIX 272..275
FT /evidence="ECO:0007829|PDB:5D08"
FT HELIX 280..287
FT /evidence="ECO:0007829|PDB:5D08"
FT HELIX 291..293
FT /evidence="ECO:0007829|PDB:5D08"
FT HELIX 298..310
FT /evidence="ECO:0007829|PDB:5D08"
FT HELIX 314..316
FT /evidence="ECO:0007829|PDB:5D08"
FT HELIX 317..326
FT /evidence="ECO:0007829|PDB:5D08"
FT HELIX 330..343
FT /evidence="ECO:0007829|PDB:5D08"
FT HELIX 346..348
FT /evidence="ECO:0007829|PDB:5D08"
FT HELIX 349..356
FT /evidence="ECO:0007829|PDB:5D08"
FT HELIX 362..382
FT /evidence="ECO:0007829|PDB:5D08"
SQ SEQUENCE 386 AA; 43142 MW; 56E5477D0D01CB30 CRC64;
MNVYQLKEEL IEYAKSIGVD KIGFTTADTF DSLKDRLILQ ESLGYLSGFE EPDIEKRVTP
KLLLPKAKSI VAIALAYPSR MKDAPRSTRT ERRGIFCRAS WGKDYHDVLR EKLDLLEDFL
KSKHEDIRTK SMVDTGELSD RAVAERAGIG FSAKNCMITT PEYGSYVYLA EMITNIPFEP
DVPIEDMCGS CTKCLDACPT GALVNPGQLN AQRCISFLTQ TKGFLPDEFR TKIGNRLYGC
DTCQTVCPLN KGKDFHLHPE MEPDPEIAKP LLKPLLAISN REFKEKFGHV SGSWRGKKPI
QRNAILALAH FKDASALPEL TELMHKDPRP VIRGTAAWAI GKIGDPAYAE ELEKALEKEK
DEEAKLEIEK GIELLKASGM TKQGLS
