MNMA_RUBXD
ID MNMA_RUBXD Reviewed; 488 AA.
AC Q1AWB1;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Bifunctional protein NifU/MnmA;
DE Includes:
DE RecName: Full=NifU-like protein;
DE Includes:
DE RecName: Full=tRNA-specific 2-thiouridylase MnmA;
DE EC=2.8.1.13;
GN Name=nifU/mnmA; OrderedLocusNames=Rxyl_1354;
OS Rubrobacter xylanophilus (strain DSM 9941 / NBRC 16129 / PRD-1).
OC Bacteria; Actinobacteria; Rubrobacteria; Rubrobacterales; Rubrobacteraceae;
OC Rubrobacter.
OX NCBI_TaxID=266117;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 9941 / NBRC 16129 / PRD-1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., da Costa M.S.,
RA Rainey F.A., Empadinhas N., Jolivet E., Battista J.R., Richardson P.;
RT "Complete sequence of Rubrobacter xylanophilus DSM 9941.";
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May be involved in the formation or repair of [Fe-S] clusters
CC present in iron-sulfur proteins. {ECO:0000305}.
CC -!- FUNCTION: Catalyzes the 2-thiolation of uridine at the wobble position
CC (U34) of tRNA, leading to the formation of s(2)U34. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=AH2 + ATP + S-sulfanyl-L-cysteinyl-[protein] + uridine(34) in
CC tRNA = 2-thiouridine(34) in tRNA + A + AMP + diphosphate + H(+) + L-
CC cysteinyl-[protein]; Xref=Rhea:RHEA:47032, Rhea:RHEA-COMP:10131,
CC Rhea:RHEA-COMP:11726, Rhea:RHEA-COMP:11727, Rhea:RHEA-COMP:11728,
CC ChEBI:CHEBI:13193, ChEBI:CHEBI:15378, ChEBI:CHEBI:17499,
CC ChEBI:CHEBI:29950, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:61963, ChEBI:CHEBI:65315, ChEBI:CHEBI:87170,
CC ChEBI:CHEBI:456215; EC=2.8.1.13;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the NifU family.
CC {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the MnmA/TRMU family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000386; ABG04317.1; -; Genomic_DNA.
DR RefSeq; WP_011564334.1; NC_008148.1.
DR AlphaFoldDB; Q1AWB1; -.
DR SMR; Q1AWB1; -.
DR STRING; 266117.Rxyl_1354; -.
DR EnsemblBacteria; ABG04317; ABG04317; Rxyl_1354.
DR KEGG; rxy:Rxyl_1354; -.
DR eggNOG; COG0482; Bacteria.
DR eggNOG; COG0822; Bacteria.
DR HOGENOM; CLU_035188_0_0_11; -.
DR OMA; VHLLCEQ; -.
DR OrthoDB; 1054741at2; -.
DR PhylomeDB; Q1AWB1; -.
DR Proteomes; UP000006637; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:InterPro.
DR GO; GO:0016783; F:sulfurtransferase activity; IEA:InterPro.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IEA:InterPro.
DR GO; GO:0006400; P:tRNA modification; IEA:UniProtKB-UniRule.
DR CDD; cd06664; IscU_like; 1.
DR CDD; cd01998; tRNA_Me_trans; 1.
DR Gene3D; 2.30.30.280; -; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR HAMAP; MF_00144; tRNA_thiouridyl_MnmA; 1.
DR InterPro; IPR023382; Adenine_a_hdrlase_dom.
DR InterPro; IPR002871; NIF_FeS_clus_asmbl_NifU_N.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR004506; tRNA-specific_2-thiouridylase.
DR Pfam; PF01592; NifU_N; 1.
DR TIGRFAMs; TIGR00420; trmU; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Disulfide bond; Multifunctional enzyme;
KW Nucleotide-binding; Reference proteome; RNA-binding; Transferase;
KW tRNA processing; tRNA-binding.
FT CHAIN 1..488
FT /note="Bifunctional protein NifU/MnmA"
FT /id="PRO_0000349872"
FT REGION 1..130
FT /note="NifU-like protein"
FT REGION 143..488
FT /note="tRNA-specific 2-thiouridylase MnmA"
FT REGION 283..285
FT /note="Interaction with tRNA"
FT /evidence="ECO:0000250"
FT REGION 433..434
FT /note="Interaction with tRNA"
FT /evidence="ECO:0000250"
FT ACT_SITE 240
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 333
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000250"
FT BINDING 149..156
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 175
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 264
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT SITE 265
FT /note="Interaction with tRNA"
FT /evidence="ECO:0000250"
FT SITE 465
FT /note="Interaction with tRNA"
FT /evidence="ECO:0000250"
FT DISULFID 240..333
FT /note="Alternate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 488 AA; 52640 MW; 4D2E592D897808B7 CRC64;
MPERYGPRVI EHLVNPRNAG EVGGPSGVGE AGNAACGDQV RFTLRVGGDL RLQEVRYRAY
GCAACIAAGS ALAELAEGRS ITGAAQISRG DIQEALGGPL PPGKEHGATL ALDALHRAFE
DYWSRQGDAL LGGEGLGDGS GGRRGVVAAM SGGVDSAVTA LLLKERGYEV VAVTFRLHDG
EPGSRSCCSP DTVLFARETA HGLGIPHFTL NLRELFDRRV MRDFVGSYAA GRTPNPCVAC
NAHVKFHAAA FLADRLGLRH VATGHYARVG EGPCLERPED GRKDQTYVLW PVPPRLLGRT
IFPLGDYRKS EVRRIAEERG LAVARTPESQ DICFIPDGDY RSFVRRRVRS EPGEIVDRQG
RVLGRHAGVV DFTVGQRRGL GISAPTPLYV TEVRPRSRQV VVGSRRELEV RRMLVRGANW
FLDPREAALV QVRYNGEPVP CELEEGAGGW EVALLEPVFG VAPGQSAVFY TRDGAKVVGG
GIIARRDA
