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Database: UniProt
Entry: A0A139BRQ2_9PROT
LinkDB: A0A139BRQ2_9PROT
Original site: A0A139BRQ2_9PROT 
ID   A0A139BRQ2_9PROT        Unreviewed;       335 AA.
AC   A0A139BRQ2;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=tRNA-dihydrouridine synthase B {ECO:0000256|HAMAP-Rule:MF_02042};
DE            EC=1.3.1.- {ECO:0000256|HAMAP-Rule:MF_02042};
GN   Name=dusB {ECO:0000256|HAMAP-Rule:MF_02042};
GN   ORFNames=AWT59_2233 {ECO:0000313|EMBL:KXS31632.1};
OS   Candidatus Gallionella acididurans.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC   Gallionellaceae; Gallionella.
OX   NCBI_TaxID=1796491 {ECO:0000313|EMBL:KXS31632.1, ECO:0000313|Proteomes:UP000070578};
RN   [1] {ECO:0000313|EMBL:KXS31632.1, ECO:0000313|Proteomes:UP000070578}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ShG14-8 {ECO:0000313|EMBL:KXS31632.1};
RA   Wen L., He K., Yang H.;
RL   Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KXS31632.1, ECO:0000313|Proteomes:UP000070578}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ShG14-8 {ECO:0000313|EMBL:KXS31632.1};
RA   Kadnikov V., Ivasenko D., Beletsky A., Mardanov A., Danilova E.,
RA   Pimenov N., Karnachuk O., Ravin N.;
RT   "New uncultured bacterium of the family Gallionellaceae from acid mine
RT   drainage: description and reconstruction of genome based on metagenomic
RT   analysis of microbial community.";
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the synthesis of 5,6-dihydrouridine (D), a modified
CC       base found in the D-loop of most tRNAs, via the reduction of the C5-C6
CC       double bond in target uridines. {ECO:0000256|ARBA:ARBA00002790,
CC       ECO:0000256|HAMAP-Rule:MF_02042, ECO:0000256|PIRNR:PIRNR006621}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 5,6-dihydrouridine in tRNA + NAD(+) = a uridine in tRNA +
CC         H(+) + NADH; Xref=Rhea:RHEA:54452, Rhea:RHEA-COMP:13339, Rhea:RHEA-
CC         COMP:13887, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:65315, ChEBI:CHEBI:74443;
CC         Evidence={ECO:0000256|ARBA:ARBA00001387, ECO:0000256|HAMAP-
CC         Rule:MF_02042};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 5,6-dihydrouridine in tRNA + NADP(+) = a uridine in tRNA +
CC         H(+) + NADPH; Xref=Rhea:RHEA:23624, Rhea:RHEA-COMP:13339, Rhea:RHEA-
CC         COMP:13887, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:65315, ChEBI:CHEBI:74443;
CC         Evidence={ECO:0000256|ARBA:ARBA00001183, ECO:0000256|HAMAP-
CC         Rule:MF_02042};
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000256|ARBA:ARBA00001917,
CC         ECO:0000256|HAMAP-Rule:MF_02042, ECO:0000256|PIRNR:PIRNR006621};
CC   -!- SIMILARITY: Belongs to the Dus family. DusB subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_02042}.
CC   -!- SIMILARITY: Belongs to the dus family. {ECO:0000256|PIRNR:PIRNR006621}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KXS31632.1}.
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DR   EMBL; LSLI01000064; KXS31632.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A139BRQ2; -.
DR   PATRIC; fig|1796491.3.peg.2441; -.
DR   Proteomes; UP000070578; Unassembled WGS sequence.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0010181; F:FMN binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0017150; F:tRNA dihydrouridine synthase activity; IEA:UniProtKB-UniRule.
DR   CDD; cd02801; DUS_like_FMN; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   HAMAP; MF_02042; DusB_subfam; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR035587; DUS-like_FMN-bd.
DR   InterPro; IPR001269; DUS_fam.
DR   InterPro; IPR032887; DusB.
DR   InterPro; IPR004652; DusB-like.
DR   InterPro; IPR024036; tRNA-dHydroUridine_Synthase_C.
DR   InterPro; IPR018517; tRNA_hU_synthase_CS.
DR   NCBIfam; TIGR00737; nifR3_yhdG; 1.
DR   PANTHER; PTHR45846; TRNA-DIHYDROURIDINE(47) SYNTHASE [NAD(P)(+)]-LIKE; 1.
DR   PANTHER; PTHR45846:SF1; TRNA-DIHYDROURIDINE(47) SYNTHASE [NAD(P)(+)]-LIKE; 1.
DR   Pfam; PF01207; Dus; 1.
DR   PIRSF; PIRSF006621; Dus; 1.
DR   SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
DR   PROSITE; PS01136; UPF0034; 1.
PE   3: Inferred from homology;
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630, ECO:0000256|HAMAP-
KW   Rule:MF_02042};
KW   FMN {ECO:0000256|ARBA:ARBA00022643, ECO:0000256|HAMAP-Rule:MF_02042};
KW   NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_02042};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW   Rule:MF_02042}; Reference proteome {ECO:0000313|Proteomes:UP000070578};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW   Rule:MF_02042};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW   Rule:MF_02042}; tRNA-binding {ECO:0000256|HAMAP-Rule:MF_02042}.
FT   DOMAIN          13..319
FT                   /note="DUS-like FMN-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01207"
FT   ACT_SITE        100
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02042,
FT                   ECO:0000256|PIRSR:PIRSR006621-1"
FT   BINDING         16..18
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02042"
FT   BINDING         70
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02042"
FT   BINDING         139
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02042"
FT   BINDING         200..202
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02042"
FT   BINDING         224..225
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02042"
SQ   SEQUENCE   335 AA;  36332 MW;  26A4846842199999 CRC64;
     MRIGPYQLKN NLIVAPMAGV TDRPFRMLCK SMGAGMAVSE MVSSNSLLYG SEKTMRRANH
     EGEVDPISVQ IVGADPVMLA QAAKYNVDNG AQIIDINMGC PAKKICNVMA GSALLQNEPL
     VAALLEAVVG AVNVPVTLKI RTGWDKANRN AIRIARIAES SGIQALAIHG RTRACAYTGD
     AEYDTIAAVK ASVNIPIIAN GDITTPEKVK YVLEITGADA VMIGRAAQGR PWLFREIGHF
     LETGKHLPAP QVGEIHRVLR NHVHALYSFY GEHTGLRVAR KHISWYTKGL SGSAHFRHAM
     NQLENPDEQL AAVDEFFAEQ ALCGTQLHYV EELAA
//
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