QUEH_STAAM
ID QUEH_STAAM Reviewed; 240 AA.
AC A0A0H3JUG6;
DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT 16-SEP-2015, sequence version 1.
DT 03-AUG-2022, entry version 32.
DE RecName: Full=Epoxyqueuosine reductase QueH {ECO:0000255|HAMAP-Rule:MF_02089, ECO:0000303|PubMed:28128549};
DE EC=1.17.99.6 {ECO:0000255|HAMAP-Rule:MF_02089, ECO:0000305|PubMed:28128549};
DE AltName: Full=Queuosine biosynthesis protein QueH {ECO:0000255|HAMAP-Rule:MF_02089, ECO:0000305};
GN Name=queH {ECO:0000255|HAMAP-Rule:MF_02089, ECO:0000303|PubMed:28128549};
GN OrderedLocusNames=SAV2591 {ECO:0000312|EMBL:BAB58753.1};
OS Staphylococcus aureus (strain Mu50 / ATCC 700699).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=158878;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mu50 / ATCC 700699;
RX PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA Hiramatsu K.;
RT "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL Lancet 357:1225-1240(2001).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND 3D-STRUCTURE MODELING.
RC STRAIN=Mu50 / ATCC 700699;
RX PubMed=28128549; DOI=10.1021/acschembio.6b01100;
RA Zallot R., Ross R., Chen W.H., Bruner S.D., Limbach P.A.,
RA de Crecy-Lagard V.;
RT "Identification of a novel epoxyqueuosine reductase family by comparative
RT genomics.";
RL ACS Chem. Biol. 12:844-851(2017).
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_02089, ECO:0000269|PubMed:28128549}.
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_02089,
CC ECO:0000305|PubMed:28128549};
CC -!- PATHWAY: tRNA modification; tRNA-queuosine biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_02089, ECO:0000305|PubMed:28128549}.
CC -!- SIMILARITY: Belongs to the QueH family. {ECO:0000255|HAMAP-
CC Rule:MF_02089, ECO:0000305}.
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DR EMBL; BA000017; BAB58753.1; -; Genomic_DNA.
DR RefSeq; WP_000606210.1; NC_002758.2.
DR AlphaFoldDB; A0A0H3JUG6; -.
DR SMR; A0A0H3JUG6; -.
DR PaxDb; A0A0H3JUG6; -.
DR EnsemblBacteria; BAB58753; BAB58753; SAV2591.
DR KEGG; sav:SAV2591; -.
DR HOGENOM; CLU_088177_1_0_9; -.
DR OMA; PNIHPYT; -.
DR PhylomeDB; A0A0H3JUG6; -.
DR BioCyc; SAUR158878:SAV_RS14125-MON; -.
DR UniPathway; UPA00392; -.
DR Proteomes; UP000002481; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR GO; GO:0052693; F:epoxyqueuosine reductase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008616; P:queuosine biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-UniRule.
DR HAMAP; MF_02089; QueH; 1.
DR InterPro; IPR003828; QueH.
DR PANTHER; PTHR36701; PTHR36701; 1.
DR Pfam; PF02677; QueH; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; Disulfide bond; Iron; Iron-sulfur; Metal-binding; Oxidoreductase;
KW Queuosine biosynthesis; Redox-active center; tRNA processing.
FT CHAIN 1..240
FT /note="Epoxyqueuosine reductase QueH"
FT /id="PRO_0000439903"
FT BINDING 43
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02089,
FT ECO:0000305|PubMed:28128549"
FT BINDING 44
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02089,
FT ECO:0000305|PubMed:28128549"
FT BINDING 129
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02089,
FT ECO:0000305|PubMed:28128549"
FT BINDING 132
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02089,
FT ECO:0000305|PubMed:28128549"
FT DISULFID 211..213
FT /note="Redox-active"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02089,
FT ECO:0000305|PubMed:28128549"
SQ SEQUENCE 240 AA; 27789 MW; AAC101093C11E0B3 CRC64;
MINAEPIISK MKNQKINYDK VLKKLIGQWE REAIRPKILL HSCCAPCSTY TLEFLTQYAD
IAIYFANSNI HPKNEYLRRA KVQEQFVEDF NRKTGANVKY IEAPYEPHKF VKMVKDKELA
DEKEGGLRCT ACFEMRLDIV AKAAVEHGYD YFGSAITLSP KKNAQLINEL GMDVQKIYDV
NYLPSDFKKS KGYERSIEMC NDYNIFRQCY CGCVFAAMQQ GIDFKTVNKE AKAFLEQYPD
