PTH_CARHZ
ID PTH_CARHZ Reviewed; 187 AA.
AC Q9F8Q3; Q3AFL6;
DT 16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 2.
DT 25-MAY-2022, entry version 101.
DE RecName: Full=Peptidyl-tRNA hydrolase {ECO:0000255|HAMAP-Rule:MF_00083};
DE Short=PTH {ECO:0000255|HAMAP-Rule:MF_00083};
DE EC=3.1.1.29 {ECO:0000255|HAMAP-Rule:MF_00083};
GN Name=pth {ECO:0000255|HAMAP-Rule:MF_00083}; OrderedLocusNames=CHY_0196;
OS Carboxydothermus hydrogenoformans (strain ATCC BAA-161 / DSM 6008 /
OS Z-2901).
OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Carboxydothermus.
OX NCBI_TaxID=246194;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Gonzalez J.M., Robb F.T.;
RT "A genomic survey of the extreme thermophilic, CO-utilizing bacterium
RT Carboxydothermus hydrogenoformans.";
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-161 / DSM 6008 / Z-2901;
RX PubMed=16311624; DOI=10.1371/journal.pgen.0010065;
RA Wu M., Ren Q., Durkin A.S., Daugherty S.C., Brinkac L.M., Dodson R.J.,
RA Madupu R., Sullivan S.A., Kolonay J.F., Nelson W.C., Tallon L.J.,
RA Jones K.M., Ulrich L.E., Gonzalez J.M., Zhulin I.B., Robb F.T., Eisen J.A.;
RT "Life in hot carbon monoxide: the complete genome sequence of
RT Carboxydothermus hydrogenoformans Z-2901.";
RL PLoS Genet. 1:563-574(2005).
CC -!- FUNCTION: The natural substrate for this enzyme may be peptidyl-tRNAs
CC which drop off the ribosome during protein synthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00083}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N-acyl-L-alpha-aminoacyl-tRNA + H2O = a tRNA + an N-acyl-L-
CC amino acid + H(+); Xref=Rhea:RHEA:54448, Rhea:RHEA-COMP:10123,
CC Rhea:RHEA-COMP:13883, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:59874, ChEBI:CHEBI:78442, ChEBI:CHEBI:138191;
CC EC=3.1.1.29; Evidence={ECO:0000255|HAMAP-Rule:MF_00083};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00083}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00083}.
CC -!- SIMILARITY: Belongs to the PTH family. {ECO:0000255|HAMAP-
CC Rule:MF_00083}.
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DR EMBL; AF244580; AAG23529.1; -; Genomic_DNA.
DR EMBL; CP000141; ABB14729.1; -; Genomic_DNA.
DR RefSeq; WP_011343144.1; NC_007503.1.
DR AlphaFoldDB; Q9F8Q3; -.
DR SMR; Q9F8Q3; -.
DR STRING; 246194.CHY_0196; -.
DR EnsemblBacteria; ABB14729; ABB14729; CHY_0196.
DR KEGG; chy:CHY_0196; -.
DR eggNOG; COG0193; Bacteria.
DR HOGENOM; CLU_062456_4_1_9; -.
DR OMA; HVLSKFH; -.
DR OrthoDB; 1676462at2; -.
DR Proteomes; UP000002706; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004045; F:aminoacyl-tRNA hydrolase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR CDD; cd00462; PTH; 1.
DR Gene3D; 3.40.50.1470; -; 1.
DR HAMAP; MF_00083; Pept_tRNA_hydro_bact; 1.
DR InterPro; IPR001328; Pept_tRNA_hydro.
DR InterPro; IPR018171; Pept_tRNA_hydro_CS.
DR InterPro; IPR036416; Pept_tRNA_hydro_sf.
DR PANTHER; PTHR17224; PTHR17224; 1.
DR Pfam; PF01195; Pept_tRNA_hydro; 1.
DR SUPFAM; SSF53178; SSF53178; 1.
DR TIGRFAMs; TIGR00447; pth; 1.
DR PROSITE; PS01195; PEPT_TRNA_HYDROL_1; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Hydrolase; Reference proteome.
FT CHAIN 1..187
FT /note="Peptidyl-tRNA hydrolase"
FT /id="PRO_0000187714"
FT CONFLICT 1..7
FT /note="MFIIAGL -> MYHSRI (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 101
FT /note="R -> C (in Ref. 1; AAG23529)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 187 AA; 20267 MW; 4946FC8B76B487E6 CRC64;
MFIIAGLGNP GQEYENTRHN AGFMVVDELA KKHGILITKR KFKSLVGEGE ILGVKVLLLK
PQTYMNLSGT AVQEAVSFYK LPLSRLVVVY DDLDLPLGKI RLRLKGSAGG HRGMGSIISC
LGSEEIPRLK IGIGRPAVGD VKDYVLQPFT GAEREILEPT LKLAAEAITV ALTEGFNKAM
TDFNRGG
