ALAXS_PYRHO
ID ALAXS_PYRHO Reviewed; 157 AA.
AC O58307;
DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Alanyl-tRNA editing protein AlaX-S;
DE Short=AlaX-S;
DE AltName: Full=Alanyl-tRNA deacylase AlaX-S;
DE AltName: Full=PhoAlaX;
GN Name=alaXS; OrderedLocusNames=PH0574;
OS Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS 100139 / OT-3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=70601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT "Complete sequence and gene organization of the genome of a hyper-
RT thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL DNA Res. 5:55-76(1998).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.88 ANGSTROMS) OF THE APO FORM IN COMPLEX WITH ZINC
RP WITH AND WITHOUT NON-COGNATE SERINE, CHARACTERIZATION, SUBUNIT, COFACTOR,
RP AND MUTAGENESIS OF THR-30.
RX PubMed=16087889; DOI=10.1073/pnas.0502119102;
RA Sokabe M., Okada A., Yao M., Nakashima T., Tanaka I.;
RT "Molecular basis of alanine discrimination in editing site.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:11669-11674(2005).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS), COFACTOR, AND SUBUNIT.
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=16374837; DOI=10.1002/prot.20760;
RA Ishijima J., Uchida Y., Kuroishi C., Tuzuki C., Takahashi N., Okazaki N.,
RA Yutani K., Miyano M.;
RT "Crystal structure of alanyl-tRNA synthetase editing-domain homolog
RT (PH0574) from a hyperthermophile, Pyrococcus horikoshii OT3 at 1.45 A
RT resolution.";
RL Proteins 62:1133-1137(2006).
CC -!- FUNCTION: Functions in trans to edit the amino acid moiety from
CC mischarged charged Ser-tRNA(Ala). Has little activity against Gly-
CC tRNA(Ala).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:16087889, ECO:0000269|PubMed:16374837};
CC Note=Binds 1 zinc ion per subunit; the homodimer seems not to bind
CC zinc. The zinc is probably not catalytic (PubMed:16087889). Another
CC report suggests the zinc is catalytic (PubMed:16374837).
CC {ECO:0000269|PubMed:16087889, ECO:0000269|PubMed:16374837};
CC -!- SUBUNIT: Monomer and homodimer; the dimer is less active in tRNA
CC editing and does not have a zinc ion associated with it
CC (PubMed:16087889). Another report shows only a monomeric form
CC (PubMed:16374837). {ECO:0000269|PubMed:16087889,
CC ECO:0000269|PubMed:16374837}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC Editing domain AlaX-S subfamily. {ECO:0000305}.
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DR EMBL; BA000001; BAA29663.1; -; Genomic_DNA.
DR PIR; B71172; B71172.
DR RefSeq; WP_010884673.1; NC_000961.1.
DR PDB; 1V4P; X-ray; 1.45 A; A/B/C=1-157.
DR PDB; 1V7O; X-ray; 2.62 A; A/B=1-157.
DR PDB; 1WNU; X-ray; 2.80 A; A/B=1-157.
DR PDB; 1WXO; X-ray; 1.88 A; A/B/C=1-157.
DR PDB; 3RFN; X-ray; 1.80 A; A=2-154.
DR PDB; 3RHU; X-ray; 2.80 A; A/B=2-154.
DR PDBsum; 1V4P; -.
DR PDBsum; 1V7O; -.
DR PDBsum; 1WNU; -.
DR PDBsum; 1WXO; -.
DR PDBsum; 3RFN; -.
DR PDBsum; 3RHU; -.
DR AlphaFoldDB; O58307; -.
DR SMR; O58307; -.
DR STRING; 70601.3256980; -.
DR PRIDE; O58307; -.
DR EnsemblBacteria; BAA29663; BAA29663; BAA29663.
DR GeneID; 1442907; -.
DR KEGG; pho:PH0574; -.
DR eggNOG; arCOG01256; Archaea.
DR OMA; AKWTASV; -.
DR OrthoDB; 84200at2157; -.
DR BRENDA; 6.1.1.7; 5244.
DR EvolutionaryTrace; O58307; -.
DR Proteomes; UP000000752; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR InterPro; IPR018163; Thr/Ala-tRNA-synth_IIc_edit.
DR SUPFAM; SSF55186; SSF55186; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Metal-binding; Zinc.
FT CHAIN 1..157
FT /note="Alanyl-tRNA editing protein AlaX-S"
FT /id="PRO_0000391644"
FT BINDING 9
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 13
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 116
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 120
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT MUTAGEN 30
FT /note="T->V: Significant deacylation of correctly charged
FT L-alanyl-tRNA(Ala) occurs."
FT /evidence="ECO:0000269|PubMed:16087889"
FT HELIX 4..23
FT /evidence="ECO:0007829|PDB:1V4P"
FT HELIX 25..27
FT /evidence="ECO:0007829|PDB:1V4P"
FT STRAND 30..36
FT /evidence="ECO:0007829|PDB:1V4P"
FT STRAND 39..45
FT /evidence="ECO:0007829|PDB:1V4P"
FT HELIX 52..68
FT /evidence="ECO:0007829|PDB:1V4P"
FT STRAND 73..78
FT /evidence="ECO:0007829|PDB:1V4P"
FT HELIX 79..86
FT /evidence="ECO:0007829|PDB:1V4P"
FT HELIX 87..90
FT /evidence="ECO:0007829|PDB:1V4P"
FT STRAND 102..108
FT /evidence="ECO:0007829|PDB:1V4P"
FT TURN 109..111
FT /evidence="ECO:0007829|PDB:1V4P"
FT STRAND 112..115
FT /evidence="ECO:0007829|PDB:1V4P"
FT HELIX 124..126
FT /evidence="ECO:0007829|PDB:1V4P"
FT STRAND 130..138
FT /evidence="ECO:0007829|PDB:1V4P"
FT TURN 139..142
FT /evidence="ECO:0007829|PDB:1V4P"
FT STRAND 143..150
FT /evidence="ECO:0007829|PDB:1V4P"
SQ SEQUENCE 157 AA; 18152 MW; A11540DEA111B84F CRC64;
MYSIEVRTHS ALHVVKGAVV KVLGSEAKWT YSTYVKGNKG VLIVKFDRKP SDEEIREIER
LANEKVKENA PIKIYELPRE EAEKMFGEDM YDLFPVPEDV RILKVVVIED WNVNACNKEH
TKTTGEIGPI KIRKVRFRKS KGLLEIHFEL LELENPS
