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Database: UniProt
Entry: C7JEJ1_ACEP3
LinkDB: C7JEJ1_ACEP3
Original site: C7JEJ1_ACEP3 
ID   C7JEJ1_ACEP3            Unreviewed;       262 AA.
AC   C7JEJ1;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   27-MAR-2024, entry version 81.
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   ECO:0000313|EMBL:BAH98821.1};
GN   OrderedLocusNames=APA01_06720 {ECO:0000313|EMBL:BAH98821.1};
OS   Acetobacter pasteurianus (strain NBRC 105184 / IFO 3283-01).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Acetobacter.
OX   NCBI_TaxID=634452 {ECO:0000313|EMBL:BAH98821.1, ECO:0000313|Proteomes:UP000000948};
RN   [1] {ECO:0000313|EMBL:BAH98821.1, ECO:0000313|Proteomes:UP000000948}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 105184 / IFO 3283-01 {ECO:0000313|Proteomes:UP000000948};
RX   PubMed=19638423; DOI=10.1093/nar/gkp612;
RA   Azuma Y., Hosoyama A., Matsutani M., Furuya N., Horikawa H., Harada T.,
RA   Hirakawa H., Kuhara S., Matsushita K., Fujita N., Shirai M.;
RT   "Whole-genome analyses reveal genetic instability of Acetobacter
RT   pasteurianus.";
RL   Nucleic Acids Res. 37:5768-5783(2009).
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}.
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DR   EMBL; AP011121; BAH98821.1; -; Genomic_DNA.
DR   RefSeq; WP_003629109.1; NC_013209.1.
DR   AlphaFoldDB; C7JEJ1; -.
DR   STRING; 634452.APA01_06720; -.
DR   KEGG; apt:APA01_06720; -.
DR   eggNOG; COG0101; Bacteria.
DR   HOGENOM; CLU_014673_0_2_5; -.
DR   BioCyc; APAS634452:APA01_RS03400-MONOMER; -.
DR   Proteomes; UP000000948; Chromosome.
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          17..116
FT                   /note="Pseudouridine synthase I TruA alpha/beta"
FT                   /evidence="ECO:0000259|Pfam:PF01416"
FT   DOMAIN          155..257
FT                   /note="Pseudouridine synthase I TruA alpha/beta"
FT                   /evidence="ECO:0000259|Pfam:PF01416"
FT   ACT_SITE        61
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00171,
FT                   ECO:0000256|PIRSR:PIRSR001430-1"
FT   BINDING         122
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00171,
FT                   ECO:0000256|PIRSR:PIRSR001430-2"
SQ   SEQUENCE   262 AA;  29155 MW;  E5A7C906CEBFBBDF CRC64;
     MMEEELAPVQ RWAVKLEYDG TGLVGWQRQK SGLSVQSLLE EAAARLANNR PVSSITAGRT
     DSGVHALAQV AHLDFPADVR FSRHSVREGL SYHLKPHNVV VLDAAQVDTD WSARFSAIWR
     SYQYRILNRR SRPTLLAGQV WHVKSTLDVE KMQEAANILV GSHDFTSFRA VACQAHSPMR
     TLDQLEISRH GDEVIVFAKA RSFLHHQVRN MVGTLKLVGI GAWQPERVAE ALEARNRCAA
     GPTAPPEGLY LNGVGYDPDP FD
//
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