ID R5BIJ2_9FIRM Unreviewed; 262 AA.
AC R5BIJ2;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE RecName: Full=tRNA pseudouridine synthase A {ECO:0000256|HAMAP-Rule:MF_00171};
DE EC=5.4.99.12 {ECO:0000256|HAMAP-Rule:MF_00171};
DE AltName: Full=tRNA pseudouridine(38-40) synthase {ECO:0000256|HAMAP-Rule:MF_00171};
DE AltName: Full=tRNA pseudouridylate synthase I {ECO:0000256|HAMAP-Rule:MF_00171};
DE AltName: Full=tRNA-uridine isomerase I {ECO:0000256|HAMAP-Rule:MF_00171};
GN Name=truA {ECO:0000256|HAMAP-Rule:MF_00171};
GN ORFNames=BN814_02247 {ECO:0000313|EMBL:CCX55263.1};
OS Veillonella sp. CAG:933.
OC Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC Veillonella.
OX NCBI_TaxID=1262980 {ECO:0000313|EMBL:CCX55263.1, ECO:0000313|Proteomes:UP000018347};
RN [1] {ECO:0000313|EMBL:CCX55263.1, ECO:0000313|Proteomes:UP000018347}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:933 {ECO:0000313|Proteomes:UP000018347};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Formation of pseudouridine at positions 38, 39 and 40 in the
CC anticodon stem and loop of transfer RNAs. {ECO:0000256|HAMAP-
CC Rule:MF_00171}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=uridine(38/39/40) in tRNA = pseudouridine(38/39/40) in tRNA;
CC Xref=Rhea:RHEA:22376, Rhea:RHEA-COMP:10085, Rhea:RHEA-COMP:10087,
CC ChEBI:CHEBI:65314, ChEBI:CHEBI:65315; EC=5.4.99.12;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00171,
CC ECO:0000256|RuleBase:RU003792};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00171}.
CC -!- SIMILARITY: Belongs to the tRNA pseudouridine synthase TruA family.
CC {ECO:0000256|ARBA:ARBA00009375, ECO:0000256|HAMAP-Rule:MF_00171,
CC ECO:0000256|RuleBase:RU003792}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00171}.
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:CCX55263.1}.
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DR EMBL; CAWP010000110; CCX55263.1; -; Genomic_DNA.
DR AlphaFoldDB; R5BIJ2; -.
DR Proteomes; UP000018347; Unassembled WGS sequence.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0106029; F:tRNA pseudouridine synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0031119; P:tRNA pseudouridine synthesis; IEA:UniProtKB-UniRule.
DR CDD; cd02570; PseudoU_synth_EcTruA; 1.
DR Gene3D; 3.30.70.660; Pseudouridine synthase I, catalytic domain, C-terminal subdomain; 1.
DR Gene3D; 3.30.70.580; Pseudouridine synthase I, catalytic domain, N-terminal subdomain; 1.
DR HAMAP; MF_00171; TruA; 1.
DR InterPro; IPR020103; PsdUridine_synth_cat_dom_sf.
DR InterPro; IPR001406; PsdUridine_synth_TruA.
DR InterPro; IPR020097; PsdUridine_synth_TruA_a/b_dom.
DR InterPro; IPR020095; PsdUridine_synth_TruA_C.
DR InterPro; IPR020094; TruA/RsuA/RluB/E/F_N.
DR NCBIfam; TIGR00071; hisT_truA; 1.
DR PANTHER; PTHR11142; PSEUDOURIDYLATE SYNTHASE; 1.
DR PANTHER; PTHR11142:SF0; TRNA PSEUDOURIDINE SYNTHASE-LIKE 1; 1.
DR Pfam; PF01416; PseudoU_synth_1; 2.
DR PIRSF; PIRSF001430; tRNA_psdUrid_synth; 1.
DR SUPFAM; SSF55120; Pseudouridine synthase; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_00171};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW Rule:MF_00171}.
FT DOMAIN 11..106
FT /note="Pseudouridine synthase I TruA alpha/beta"
FT /evidence="ECO:0000259|Pfam:PF01416"
FT DOMAIN 147..249
FT /note="Pseudouridine synthase I TruA alpha/beta"
FT /evidence="ECO:0000259|Pfam:PF01416"
FT ACT_SITE 56
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00171,
FT ECO:0000256|PIRSR:PIRSR001430-1"
FT BINDING 114
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00171,
FT ECO:0000256|PIRSR:PIRSR001430-2"
SQ SEQUENCE 262 AA; 29237 MW; 7606E9A8F6A9A397 CRC64;
MATEQRNIRL IVAYDGTELN GYQSQVNGIT VQDCLEAALT KVCNEPISIY GASRTDAGVH
AKFQVVTFFT TGRVPVENLT RALIAHLPPF IVIRRAEEIP LDWRPRWKIV GKEYIYTIHN
DVIEDPLGMR FHWHVKKPLN REAMVAAAKA LEGTHDFTTL QGANSTPANP VKTMFAVSLK
FNGPAVYIHV IGDGFLYHMV RNIAGLLVDV GLGRIEPAKI PELLAARNRR LIGKTAPPQG
LCLEEIFFDE ERRQAVIDSL QA
//
