SYA_TREDE
ID SYA_TREDE Reviewed; 600 AA.
AC P61708;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2004, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Alanine--tRNA ligase;
DE EC=6.1.1.7;
DE AltName: Full=Alanyl-tRNA synthetase;
DE Short=AlaRS;
GN Name=alaS; OrderedLocusNames=TDE_1659;
OS Treponema denticola (strain ATCC 35405 / DSM 14222 / CIP 103919 / JCM 8153
OS / KCTC 15104).
OC Bacteria; Spirochaetes; Spirochaetales; Treponemataceae; Treponema.
OX NCBI_TaxID=243275;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35405 / DSM 14222 / CIP 103919 / JCM 8153 / KCTC 15104;
RX PubMed=15064399; DOI=10.1073/pnas.0307639101;
RA Seshadri R., Myers G.S.A., Tettelin H., Eisen J.A., Heidelberg J.F.,
RA Dodson R.J., Davidsen T.M., DeBoy R.T., Fouts D.E., Haft D.H., Selengut J.,
RA Ren Q., Brinkac L.M., Madupu R., Kolonay J.F., Durkin S.A., Daugherty S.C.,
RA Shetty J., Shvartsbeyn A., Gebregeorgis E., Geer K., Tsegaye G.,
RA Malek J.A., Ayodeji B., Shatsman S., McLeod M.P., Smajs D., Howell J.K.,
RA Pal S., Amin A., Vashisth P., McNeill T.Z., Xiang Q., Sodergren E.,
RA Baca E., Weinstock G.M., Norris S.J., Fraser C.M., Paulsen I.T.;
RT "Comparison of the genome of the oral pathogen Treponema denticola with
RT other spirochete genomes.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:5646-5651(2004).
CC -!- FUNCTION: Catalyzes the attachment of alanine to tRNA(Ala) in a two-
CC step reaction: alanine is first activated by ATP to form Ala-AMP and
CC then transferred to the acceptor end of tRNA(Ala). Also edits
CC incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing
CC domain (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-
CC tRNA(Ala); Xref=Rhea:RHEA:12540, Rhea:RHEA-COMP:9657, Rhea:RHEA-
CC COMP:9923, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57972,
CC ChEBI:CHEBI:78442, ChEBI:CHEBI:78497, ChEBI:CHEBI:456215; EC=6.1.1.7;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- DOMAIN: Consists of two domains; the N-terminal catalytic domain (in
CC this organism this is shorter than usual) and the editing domain; the
CC C-terminal C-Ala domain found in most orthologs is missing. The editing
CC domain removes incorrectly charged amino acids (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
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DR EMBL; AE017226; AAS12175.1; -; Genomic_DNA.
DR RefSeq; NP_972264.1; NC_002967.9.
DR RefSeq; WP_002679355.1; NC_002967.9.
DR AlphaFoldDB; P61708; -.
DR SMR; P61708; -.
DR STRING; 243275.TDE_1659; -.
DR EnsemblBacteria; AAS12175; AAS12175; TDE_1659.
DR GeneID; 2739000; -.
DR KEGG; tde:TDE_1659; -.
DR PATRIC; fig|243275.7.peg.1586; -.
DR eggNOG; COG0013; Bacteria.
DR HOGENOM; CLU_004485_0_2_12; -.
DR OMA; YHHTMFE; -.
DR OrthoDB; 91428at2; -.
DR Proteomes; UP000008212; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004813; F:alanine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006419; P:alanyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.930.10; -; 1.
DR HAMAP; MF_00036_B; Ala_tRNA_synth_B; 1.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR002318; Ala-tRNA-lgiase_IIc.
DR InterPro; IPR018162; Ala-tRNA-ligase_IIc_anticod-bd.
DR InterPro; IPR018165; Ala-tRNA-synth_IIc_core.
DR InterPro; IPR018164; Ala-tRNA-synth_IIc_N.
DR InterPro; IPR023033; Ala_tRNA_ligase_euk/bac.
DR InterPro; IPR018163; Thr/Ala-tRNA-synth_IIc_edit.
DR InterPro; IPR012947; tRNA_SAD.
DR Pfam; PF01411; tRNA-synt_2c; 1.
DR Pfam; PF07973; tRNA_SAD; 1.
DR PRINTS; PR00980; TRNASYNTHALA.
DR SMART; SM00863; tRNA_SAD; 1.
DR SUPFAM; SSF101353; SSF101353; 1.
DR SUPFAM; SSF55186; SSF55186; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00344; alaS; 1.
DR PROSITE; PS50860; AA_TRNA_LIGASE_II_ALA; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; Metal-binding;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome; RNA-binding;
KW tRNA-binding; Zinc.
FT CHAIN 1..600
FT /note="Alanine--tRNA ligase"
FT /id="PRO_0000075236"
FT BINDING 463
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255"
FT BINDING 467
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255"
FT BINDING 565
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255"
FT BINDING 569
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255"
SQ SEQUENCE 600 AA; 67091 MW; 575D13322A37E394 CRC64;
MNKNITIDEL RSKYIDFFKS KGHVEISGRS LIPENDPTVL FTTAGMHPLV PYLMGEPHPA
GTRLTDVQKC VRTGDIDDVG DASHLTFFEM LGNWSLGDYF KKESIAYSFE FLTDEKYLGI
PIDKLSFTVF EGNEDAPRDE ESASIWESLG VSKDRIFFLP KEDNWWGPAG ETGPCGPDTE
IFIDTGKPAC GSNCRPGCNC GKYVEIWNNV FMQYHKNMDG SYSPLKRKCV DTGMGVERTV
AMLQGKPSVY NTEAFTSIIK SIEDISGVKY GDNEKTDTSI RIIADHVRTA CFILGDPKTT
LPSNIGAGYV LRRLIRRAVR HGKKLGIDGN FLSVPASAVI AQNAGFYTEL KENETLILTE
LKAEEDKFLE TLKKGEAEFE KMLPNLLKNP KKIIPGRMAF KLYDTYGFPI ELTEELASES
GLTVNREEFD EAFKKHQELS RAGSEQVFKG GLADHSEQTT AYHTATHLLH KALRMVLGDH
VQQKGSNITA ERLRFDFSHP EPMTEAEKKE VERLVNEAIK ADLPVTMEVM PLEEAKKIGA
MALFGEKYED VVKVYKIGDF STEVCGGPHV ERTGSLGRFC IKKEQSSSSG VRRIRAVLEH
